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Streptococcus mutans Search Results

Record: 1 of 1  
MiniMap IGR602 IGR604 IGR603 IGR598 IGR601 IGR605 IGR606 IGR599 IGR600 IGR607 SMu0699 SMu0689 SMu0696 hitA, - SMu0698 SMu0697 SMu0688 ahpC, - SMu0692 SMu0695 SMu0690 yugD, - SMu0691 ahpF,nox1, - SMu0693 SMu0699 SMu0689 SMu0696 hitA, - SMu0698 SMu0697 SMu0688 ahpC, - SMu0692 SMu0695 SMu0690 yugD, - SMu0691 ahpF,nox1, - SMu0693 SMu0699 SMu0689 SMu0696 hitA, - SMu0698 SMu0697 SMu0688 ahpC, - SMu0692 SMu0695 SMu0690 yugD, - SMu0691 ahpF,nox1, - SMu0693 SMu0694 SMu0694


LANL Gene ID: SMu0693

GenBank Locus Tag: SMU.765

DNA Molecule Name:
1  

GenBank ID:
24379224

Gene Name:
ahpF  nox1  

Definition:
alkyl hydroperoxide reductase, subunit F

Cellular Location:
Cytoplasm [Evidence]

Gene Start:
713482

Gene Stop:
715014

Gene Length:
1533

Molecular Weight*:
55137

pI*:
4.60

Net Charge*:
-24.01

EC:
 

Functional Class:
Cellular processes; Detoxification  

Gene Ontology:
Biological process
  GO:0006118    electron transport
  GO:0008152    metabolic process

Molecular function
  GO:0016491    oxidoreductase activity
  GO:0016651    oxidoreductase activity, acting on NADH or NADPH
  GO:0050660    FAD binding
  GO:0051287    NAD binding


Pathway: pathway table

Primary Evidence:
Abranches J, Lemos JA, Burne RA.,
Osmotic stress responses of Streptococcus mutans UA159.
FEMS Microbiol Lett. 2006 Feb;255(2):240-6.
PMID: 16448501

Poole,L.B., Higuchi,M., Shimada,M., Calzi,M.L. and Kamio,Y.
Streptococcus mutans H2O2-forming NADH oxidase is an alkyl
hydroperoxide reductase protein
Free Radic. Biol. Med. 28 (1), 108-120 (2000)
PubMed: 10656297

Higuchi,M., Shimada,M., Matsumoto,J., Yamamoto,Y., Rhaman,A. and
Kamio,Y.
Molecular cloning and sequence analysis of the gene encoding the
H2O2-forming NADH oxidase from Streptococcus mutans
Biosci. Biotechnol. Biochem. 58 (9), 1603-1607 (1994)
PubMed: 7765479

Secondary Evidence:
Poole LB.
Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductases.
Arch Biochem Biophys. 2005 Jan;433(1):240-54.
PMID: 15581580

Ross RP, Claiborne A.
Molecular cloning and analysis of the gene encoding the NADH oxidase from Streptococcus faecalis 10C1. Comparison with NADH peroxidase and the flavoprotein disulfide reductases.
J Mol Biol. 1992 Oct;227(3):658-71.
PMID: 1404382

Kuriyan J, Krishna TS, Wong L, Guenther B, Pahler A, Williams CH, Model P.
Convergent evolution of similar function in two structurally divergent enzymes.
Nature. 1991 Jul;352(6331):172-4.
PMID: 2067578

Xu,X.M., Koyama,N., Cui,M., Yamagishi,A., Nosoh,Y. and Oshima,T.
Nucleotide sequence of the gene encoding NADH dehydrogenase from an alkalophile, Bacillus sp. strain YN-1
J. Biochem. 109 (5), 678-683 (1991)
PubMed: 1917890

Eggink G, Engel H, Vriend G, Terpstra P, Witholt B.
Rubredoxin reductase of Pseudomonas oleovorans. Structural relationship to other flavoprotein oxidoreductases based on one NAD and two FAD fingerprints.
J Mol Biol. 1990 Mar;212(1):135-42.
PMID: 2319593

Xu,X.M., Kanaya,S., Koyama,N., Sekiguchi,T., Nosoh,Y., Ohashi,S.
and Tsuda,K.
Tryptic digestion of NADH dehydrogenase from alkalophilic Bacillus
J. Biochem. 105 (4), 626-632 (1989)
PubMed: 2760020








Comment:
For other 'ahp' genes see SMu0692 (ahpC).

From InterPro: IPR001327

FAD-dependent pyridine nucleotide-disulphide oxidoreductase.

This entry describes both class I and class II oxidoreductases. FAD flavoproteins belonging to the family of pyridine nucleotide-disulphide oxidoreductases (glutathione reductase, trypanothione reductase, lipoamide dehydrogenase, mercuric reductase, thioredoxin reductase, alkyl hydroperoxide reductase) share sequence similarity with a number of other flavoprotein oxidoreductases, in particular with ferredoxin-NAD+ reductases involved in oxidative metabolism of a variety of hydrocarbons (rubredoxin reductase, putidaredoxin reductase, terpredoxin reductase, ferredoxin-NAD+ reductase components of benzene 1,2-dioxygenase, toluene 1,2-dioxygenase, chlorobenzene dioxygenase, biphenyl dioxygenase), NADH oxidase and NADH peroxidase. Comparison of the crystal structures of human glutathione reductase and Escherichia coli thioredoxin reductase reveals different locations of their active sites, suggesting that the enzymes diverged from an ancestral FAD/NAD(P)H reductase and acquired their disulphide reductase activities independently.



View in HOMD Genome Viewer

Blast Summary:  PSI-Blast Search
Matches in gapped BLAST to NADH oxidase/alkyl hydroperoxidase reductase: residues 1-510 are 100% similar to a previously published enzyme in S.mutans (3062839).

Residues 1-509 are 75% similar to the enzyme from S.pyogenes (15675838) and are 63% similar to the enzyme from Thermus aquaticus (8927564).






The best hit to the Streptococcus agalactiae 2603 V/R genome is to SAG1834 (0.0).


Top Blast Hits:  Updated monthly
Click here to view the entire PsiBlast results.
 gi|24379224|ref|NP_721179.1|  NADH oxidase/alkyl hydroperoxi...  1003   0.0  
 gi|464216|dbj|BAA04825.1|  NADH oxidase [Streptococcus mutans]    967   0.0  
 gi|139474527|ref|YP_001129243.1|  NADH dehydrogenase [Strept...   770   0.0  
 gi|19746953|ref|NP_608089.1|  putative NADH oxidase/alkyl hy...   768   0.0  
 gi|77408425|ref|ZP_00785164.1|  alkyl hydroperoxide reductas...   768   0.0  
 gi|15675838|ref|NP_270012.1|  putative NADH oxidase/alkyl hy...   768   0.0  
 gi|71904415|ref|YP_281218.1|  peroxiredoxin reductase (NAD(P...   768   0.0  
 gi|22537973|ref|NP_688824.1|  alkyl hydroperoxide reductase,...   768   0.0  
 gi|94991344|ref|YP_599444.1|  Peroxiredoxin reductase (NAD(P...   768   0.0  
 gi|94995257|ref|YP_603355.1|  Peroxiredoxin reductase (NAD(P...   767   0.0


InterPro Summary:  InterProScan

InterPro
IPR000103
Domain
Pyridine nucleotide-disulphide oxidoreductase, class-II
PR00469 [210-232]T 4.3E-64 PR00469 PNDRDTASEII[242-257]T 4.3E-64 PR00469 PNDRDTASEII[262-272]T 4.3E-64 PR00469 PNDRDTASEII[308-316]T 4.3E-64 PR00469 PNDRDTASEII[330-342]T 4.3E-64 PR00469 PNDRDTASEII[345-369]T 4.3E-64 PR00469 PNDRDTASEII[397-413]T 4.3E-64 PR00469 PNDRDTASEII[435-456]T 4.3E-64 PR00469 PNDRDTASEII[470-488]T 4.3E-64 PR00469 PNDRDTASEII PNDRDTASEII
InterPro
IPR000759
Family
Adrenodoxin reductase
PR00419 [210-232]T 1.5E-7 PR00419 ADXRDTASE[350-364]T 1.5E-7 PR00419 ADXRDTASE ADXRDTASE
InterPro
IPR001327
Domain
Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
PD000139 [315-382]T 0.0 PD000139 FAD_pyr_redox FAD_pyr_redox
PF00070 [349-441]T 9.100004256456059E-24 PF00070 Pyr_redox Pyr_redox
InterPro
IPR003042
Family
Aromatic-ring hydroxylase
PR00420 [210-232]T 6.7E-8 PR00420 RNGMNOXGNASE[459-474]T 6.7E-8 PR00420 RNGMNOXGNASE RNGMNOXGNASE
InterPro
IPR008255
Active_site
Pyridine nucleotide-disulphide oxidoreductase, class-II, active site
PS00573 [337-357]T 8.0E-5 PS00573 PYRIDINE_REDOX_2 PYRIDINE_REDOX_2
InterPro
IPR012081
Family
Alkyl hydroperoxide reductase, subunit F
PIRSF000238 [2-510]T 0.0 PIRSF000238 AhpF AhpF
InterPro
IPR012335
Domain
Thioredoxin fold
G3DSA:3.40.30.10 [2-93]T 3.89999861795218E-27 G3DSA:3.40.30.10 Thioredoxin_fold[102-196]T 1.3000049540732399E-34 G3DSA:3.40.30.10 Thioredoxin_fold Thioredoxin_fold
InterPro
IPR012336
Domain
Thioredoxin-like fold
SSF52833 [2-101]T 9.999999999999999E-31 SSF52833 IPR012336[102-196]T 2.0E-23 SSF52833 IPR012336 IPR012336
InterPro
IPR013027
Domain
FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PR00368 [210-232]T 8.0E-27 PR00368 FADPNR[310-319]T 8.0E-27 PR00368 FADPNR[349-374]T 8.0E-27 PR00368 FADPNR[434-448]T 8.0E-27 PR00368 FADPNR[475-482]T 8.0E-27 PR00368 FADPNR FADPNR
PF07992 [210-486]T 3.89999861795218E-42 PF07992 Pyr_redox_2 Pyr_redox_2
noIPR
unintegrated
unintegrated
G3DSA:3.50.50.60 [208-318]T 4.0999959904574996E-23 G3DSA:3.50.50.60 G3DSA:3.50.50.60[319-441]T 1.2000011745813998E-39 G3DSA:3.50.50.60 G3DSA:3.50.50.60 G3DSA:3.50.50.60
PTHR22912 [212-483]T 6.90001478563499E-24 PTHR22912 PTHR22912 PTHR22912
SSF51905 [209-506]T 1.2E-51 SSF51905 SSF51905 SSF51905


COGS Summary:  COGS Search
BeTs to 17 clades of COG0492
COG name: Thioredoxin reductase/alkyl hydroperoxide reductase
Functional Class: O
The phylogenetic pattern of COG0492 is amtkYQVcEBrhUJgpolinX
Number of proteins in this genome belonging to this COG is 3
Blocks Summary:  Blocks Search
***** IPB000103 (Pyridine nucleotide-disulphide oxidoreductase class-II) with a combined E-value of 1.2e-78.
    IPB000103A    210-230
    IPB000103B    242-256
    IPB000103C    315-363
    IPB000103D    435-446
    IPB000103E    470-507
***** PR00368 (FAD-dependent pyridine nucleotide reductase signature) with a combined E-value of 9.2e-34.
    PR00368A    210-232
    PR00368B    310-319
    PR00368C    349-374
    PR00368D    434-448
    PR00368E    475-482
***** PR00420 (Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature) with a combined E-value of 4.5e-07.
    PR00420A    210-232
    PR00420D    350-366
***** PR00419 (Adrenodoxin reductase family signature) with a combined E-value of 7.9e-06.
    PR00419A    210-232
    PR00419D    350-364


 ProDom Summary:  Protein Domain Search
Residues 295-483 are 66% similar to a (OXIDOREDUCTASE FLAVOPROTEIN FAD CENTER REDOX-ACTIVE) protein domain (PD000139 which is seen in Q9KH09_THEAQ.

Residues 210-480 are 21% similar to a (PROTEOME COMPLETE OXIDOREDUCTASE) protein domain (PD132291 which is seen in Q9PHV6_CAMJE.

Residues 350-403 are identical to a (OXIDOREDUCTASE THIOREDOXIN FAD) protein domain (PD345560 which is seen in Q54469_STRMU.

Residues 119-180 are identical to a (REDUCTASE FLAVOPROTEIN HYDROPEROXIDE ALKYL FAD) protein domain (PD007583 which is seen in Q54469_STRMU.

Residues 436-507 are 34% similar to a (PROTEOME REDUCTASE-LIKE THIOREDOXIN) protein domain (PD232972 which is seen in Q9HHD5_HALN1.

Residues 283-501 are 26% similar to a (COMPLETE PROTEOME OXIDOREDUCTASE) protein domain (PD329335 which is seen in Q9Z9W3_BACHD.

Residues 3-115 are identical to a (REDUCTASE FLAVOPROTEIN ALKYL) protein domain (PD364642 which is seen in O66266_STRMU.

Residues 305-345 are identical to a (REDUCTASE FLAVOPROTEIN FAD OXIDOREDUCTASE THIOREDOXIN) protein domain (PD329455 which is seen in Q54469_STRMU.

Residues 404-483 are identical to a (FAD FLAVOPROTEIN OXIDOREDUCTASE NADH) protein domain (PD406982 which is seen in Q54469_STRMU.

Residues 208-315 are 30% similar to a (COMPLETE PROTEOME FAD FLAVOPROTEIN) protein domain (PD348239 which is seen in O31475_BACSU.

Residues 398-482 are 34% similar to a (REDUCTASE PROTEOME COMPLETE FAD) protein domain (PD294764 which is seen in O05268_BACSU.

Residues 411-507 are 29% similar to a (FAD THIOREDOXIN FLAVOPROTEIN) protein domain (PD396826 which is seen in Q9K4L6_STRCO.

Residues 407-507 are 29% similar to a (CENTER FAD THIOREDOXIN NADP) protein domain (PD394558 which is seen in TRXB_MYCPN.

Residues 196-265 are identical to a (REDUCTASE FLAVOPROTEIN OXIDOREDUCTASE FAD THIOREDOXIN) protein domain (PD396269 which is seen in Q54469_STRMU.

Residues 180-253 are 53% similar to a (F ALKYL SUBUNIT REDUCTASE) protein domain (PD001422 which is seen in AHPF_PSEPU.

Residues 210-253 are 72% similar to a (OXIDOREDUCTASE FAD FLAVOPROTEIN COMPLETE PROTEOME) protein domain (PD000271 which is seen in Q9KH09_THEAQ.


Paralogs:  Local Blast Search
SMu0693 is paralogously related (blast p-value < 1e-3) to SMu0420, a predicted NADH oxidase, SMu0792, a predicted thioredoxin reductase, SMu1299 and SMu0116,both predicted dihydrolipoamide dehydrogenase, SMu1020, a predicted H2O-forming NADH oxidase, SMu0762 and SMu0126, both predicted glutathione reductases.


Pfam Summary:  Pfam Search
Residues 210 to 491 (E-value = 1.7e-73) place SMu0693 in the Pyr_redox family which is described as Pyridine nucleotide-disulphide oxidoreductase (PF00070)

 Top PDB Hits:
pdb1CL0A Chain A, Crystal Structure Of Reduced Thioredoxin Re... 159 6e-040
pdb1TDE Thioredoxin Reductase (E.C.1.6.4.5) (Wild Type) 159 6e-040
pdb1F6MA Chain A, Crystal Structure Of A Complex Between Thio... 155 8e-039

Gene Protein Sequence:
MALDAEIKEQLGQYLQLLESEIVLQAQLKDDANSQKVKEFLQEIVAMSPM
ISLEEKELPRTPSFRIAKKGQESGVEFAGLPLGHEFTSFILALLQVSGRP
PKVETDIVKRIQAVDEPMHFETYVSLTCHNCPDVVQAFNIMSVVNPNISH
TMVEGGMFKDEIEAKGIMSVPTVYKDGTEFTSGRASIEQLLDLIAGPLKE
DAFDDKGVFDVLVIGGGPAGNSAAIYAARKGVKTGLLAETMGGQVMETVG
IENMIGTPYVEGPQLMAQVEEHTKSYSVDIMKAPRAKSIQKTDLVEVELD
NGAHLKAKTAVLALGAKWRKINVPGEKEFFNKGVTYCPHCDGPLFTDKKV
AVIGGGNSGLEAAIDLAGLASHVYILEFLPELKADKILQDRAEALDNITI
LTNVATKEIIGNDHVEGLRYSDRTTNEEYLLDLEGVFVQIGLVPSTDWLK
DSGLALNEKGEIIVAKDGATNIPAIFAAGDCTDSAYKQIIISMGSGATAA
LGAFDYLIRN

Gene Nucleotide Sequence:  Sequence Viewer
ATGGCATTAGACGCAGAAATCAAAGAGCAGTTAGGACAGTATCTTCAATT
ACTTGAGTCTGAGATTGTTTTACAAGCTCAATTAAAAGACGATGCTAATT
CTCAAAAAGTTAAGGAATTTCTCCAAGAAATCGTTGCAATGTCTCCTATG
ATTTCTTTAGAAGAAAAGGAACTTCCGCGAACACCTAGTTTTCGCATAGC
TAAAAAGGGACAAGAATCTGGTGTTGAATTTGCTGGCTTACCCCTTGGTC
ACGAATTTACTTCGTTTATCTTGGCTCTGTTACAGGTTTCAGGGCGTCCG
CCTAAGGTAGAGACTGATATTGTCAAACGCATTCAAGCTGTTGATGAACC
TATGCATTTTGAAACCTATGTTAGTTTGACTTGTCATAATTGTCCAGATG
TTGTTCAGGCTTTCAATATCATGTCAGTTGTTAATCCCAACATTTCACAT
ACAATGGTGGAAGGTGGCATGTTTAAAGATGAAATTGAAGCTAAGGGAAT
TATGTCTGTGCCAACTGTCTATAAAGATGGAACAGAATTTACCTCAGGGC
GTGCTAGCATAGAGCAATTACTAGACTTGATAGCAGGTCCTCTTAAAGAA
GATGCTTTTGATGATAAAGGTGTTTTTGATGTCCTTGTTATTGGTGGGGG
TCCTGCTGGTAATAGCGCGGCTATCTATGCTGCAAGAAAGGGAGTTAAAA
CAGGACTTTTAGCTGAAACCATGGGTGGTCAAGTTATGGAAACCGTGGGT
ATTGAAAATATGATCGGTACCCCATATGTTGAAGGACCCCAATTAATGGC
TCAGGTGGAAGAGCATACCAAGTCTTATTCTGTTGACATCATGAAGGCAC
CGCGTGCTAAGTCTATTCAAAAGACAGACTTGGTTGAAGTTGAACTTGAT
AATGGAGCTCATTTGAAAGCAAAGACAGCTGTTTTGGCCTTAGGTGCCAA
GTGGCGTAAAATCAATGTACCAGGAGAAAAAGAATTCTTTAATAAAGGTG
TTACTTACTGTCCGCACTGTGATGGTCCTCTTTTCACAGACAAAAAAGTC
GCTGTCATTGGCGGTGGAAACTCAGGTTTAGAAGCAGCTATTGATTTGGC
TGGGTTAGCTAGCCATGTCTATATTTTAGAATTTTTACCTGAGTTAAAAG
CTGATAAGATCTTACAAGATCGTGCGGAAGCTCTTGATAATATTACCATT
CTAACTAATGTTGCGACTAAAGAAATTATTGGCAATGACCACGTAGAAGG
TCTTCGTTACAGTGATCGTACGACCAATGAAGAGTACTTGCTTGATTTAG
AAGGTGTTTTTGTTCAAATTGGATTGGTACCTAGTACTGACTGGTTAAAG
GATAGTGGACTAGCACTCAATGAAAAAGGTGAAATCATTGTTGCTAAAGA
TGGCGCAACTAATATTCCTGCTATTTTTGCAGCTGGTGATTGCACAGATA
GTGCCTACAAACAAATTATCATTTCCATGGGTTCTGGAGCTACTGCGGCT
TTAGGTGCCTTTGATTATTTGATTAGAAATTAA

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