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Streptococcus mutans Search Results

Record: 1 of 1  
MiniMap IGR1364 IGR1359 IGR1363 IGR1361 IGR1362 IGR1358 IGR1360 bccP,accB, - SMu1584 fabG, - SMu1586 accD, - SMu1581 fabD, - SMu1587 fabK, - SMu1588 fabF, - SMu1585 accC, - SMu1582 snf, - SMu1579 bccP,accB, - SMu1584 fabG, - SMu1586 accD, - SMu1581 fabD, - SMu1587 fabK, - SMu1588 fabF, - SMu1585 accC, - SMu1582 snf, - SMu1579 bccP,accB, - SMu1584 fabG, - SMu1586 accD, - SMu1581 fabD, - SMu1587 fabK, - SMu1588 fabF, - SMu1585 accC, - SMu1582 snf, - SMu1579 fabZ, - SMu1583 accA, - SMu1580 fabZ, - SMu1583 accA, - SMu1580


LANL Gene ID: SMu1582

GenBank Locus Tag: SMU.1736c

DNA Molecule Name:
1  

GenBank ID:


Gene Name:
accC  

Definition:
acetyl-CoA carboxylase biotin carboxylase subunit

Cellular Location:
Cytoplasm [Evidence]

Gene Start:
1644225

Gene Stop:
1642855

Gene Length:
1371

Molecular Weight*:
49688

pI*:
4.90

Net Charge*:
-14.46

EC:
6.4.1.2  

Functional Class:
Fatty acid and phospholipid metabolism; Biosynthesis  

Gene Ontology:
Biological process
  GO:0007186    G-protein coupled receptor protein signaling pathway
  GO:0007601    visual perception
  GO:0008152    metabolic process

Cellular component
  GO:0016021    integral to membrane

Molecular function
  GO:0001584    rhodopsin-like receptor activity
  GO:0003824    catalytic activity
  GO:0005524    ATP binding
  GO:0009374    biotin binding
  GO:0016874    ligase activity


Pathway: pathway table
Fatty acid biosynthesis (path 1)
Propanoate metabolism
Pyruvate metabolism
Tetracycline biosynthesis

Secondary Evidence:
Marini PE, Perez CA, de Mendoza D.
Growth-rate regulation of the Bacillus subtilis accBC operon encoding subunits of acetyl-CoA carboxylase, the first enzyme of fatty acid synthesis.
Arch Microbiol. 2001 Mar;175(3):234-7.
PMID: 11357516

Marini P, Li SJ, Gardiol D, Cronan JE Jr, de Mendoza D.
The genes encoding the biotin carboxyl carrier protein and biotin carboxylase subunits of Bacillus subtilis acetyl coenzyme A carboxylase, the first enzyme of fatty
acid synthesis.
J Bacteriol. 1995 Dec;177(23):7003-6.
PMID: 7592499

Comment:
For other 'acc' genes see SMu1580 (accA) and SMu1581 (accD).



View in HOMD Genome Viewer

Blast Summary:  PSI-Blast Search
Similarities in gapped BLAST to accC proteins. Residues 1-454 are 82% similar to gi15675594 from S.pyogenes. Residues 1-451 are 80% similar to gi15900344 from S.pneumoniae.





The best hit to the Streptococcus agalactiae 2603 V/R genome is to SAG0352 (0.0).


Top Blast Hits:  Updated monthly
Click here to view the entire PsiBlast results.
 gi|24380108|ref|NP_722063.1|  acetyl-CoA carboxylase [Strept...   859   0.0  
 gi|55820482|ref|YP_138924.1|  acetyl-CoA carboxylase [Strept...   760   0.0  
 gi|116627302|ref|YP_819921.1|  Biotin carboxylase [Streptoco...   758   0.0  
 gi|125718724|ref|YP_001035857.1|  Biotin carboxylase, putati...   748   0.0  
 gi|157074994|gb|ABV09677.1|  acetyl-CoA carboxylase, biotin ...   743   0.0  
 gi|81097242|ref|ZP_00875542.1|  Acetyl-CoA carboxylase, biot...   736   0.0  
 gi|15675594|ref|NP_269768.1|  acetyl-CoA carboxylase [Strept...   735   0.0  
 gi|21911055|ref|NP_665323.1|  acetyl-CoA carboxylase [Strept...   734   0.0  
 gi|146319453|ref|YP_001199165.1|  Biotin carboxylase [Strept...   734   0.0  
 gi|71904137|ref|YP_280940.1|  acetyl-CoA carboxylase [Strept...   734   0.0


InterPro Summary:  InterProScan

InterPro
IPR001760
Family
Opsin
PS00238 [258-274]? 0.0 PS00238 OPSIN OPSIN
InterPro
IPR004549
Family
Acetyl-CoA carboxylase, biotin carboxylase
TIGR00514 [1-452]T 0.0 TIGR00514 accC accC
InterPro
IPR005479
Domain
Carbamoyl-phosphate synthase L chain, ATP-binding
PF02786 [115-330]T 9.20006495413801E-95 PF02786 CPSase_L_D2 CPSase_L_D2
PS00866 [153-167]? 0.0 PS00866 CPSASE_1 CPSASE_1
PS00867 [287-294]? 0.0 PS00867 CPSASE_2 CPSASE_2
InterPro
IPR005481
Domain
Carbamoyl-phosphate synthetase large chain, N-terminal
PF00289 [1-113]T 3.99998544139379E-43 PF00289 CPSase_L_chain CPSase_L_chain
InterPro
IPR005482
Domain
Biotin carboxylase, C-terminal
PF02785 [337-444]T 3.8999986179521804E-48 PF02785 Biotin_carb_C Biotin_carb_C
InterPro
IPR011054
Domain
Rudiment single hybrid motif
SSF51246 [331-454]T 1.4E-41 SSF51246 Rudmnt_hyb_motif Rudmnt_hyb_motif
InterPro
IPR011761
Domain
ATP-grasp fold
PS50975 [120-318]T 0.0 PS50975 ATP_GRASP ATP_GRASP
InterPro
IPR011764
Domain
Biotin carboxylation region
PS50979 [1-448]T 0.0 PS50979 BC BC
InterPro
IPR013816
Domain
ATP-grasp fold, subdomain 2
G3DSA:3.30.470.20 [86-452]T 4.200034604927659E-114 G3DSA:3.30.470.20 ATP_grasp_subdomain_2 ATP_grasp_subdomain_2
InterPro
IPR013817
Domain
Pre-ATP-grasp fold
G3DSA:3.40.50.20 [1-85]T 3.99998544139379E-34 G3DSA:3.40.50.20 Pre-ATP_grasp Pre-ATP_grasp
noIPR
unintegrated
unintegrated
PTHR18866 [4-443]T 0.0 PTHR18866 PTHR18866 PTHR18866
SSF52440 [1-115]T 1.5000000000000002E-49 SSF52440 SSF52440 SSF52440
SSF56059 [116-330]T 4.6E-64 SSF56059 SSF56059 SSF56059


COGS Summary:  COGS Search
BeTs to 12 clades of COG0439
COG name: Biotin carboxylase
Functional Class: I
The phylogenetic pattern of COG0439 is amt-YQ-CeBRhuj----inx
Number of proteins in this genome belonging to this COG is 3
Blocks Summary:  Blocks Search
***** IPB001882 (Biotin-requiring enzymes attachment site) with a combined E-value of 1.1e-89.
    IPB001882A    75-95
    IPB001882B    104-132
    IPB001882C    152-169
    IPB001882D    208-243
    IPB001882E    266-280
    IPB001882F    293-302
    IPB001882G    333-351
***** IPB000901 (Carbamoyl-phosphate synthase) with a combined E-value of 1.2e-13.
    IPB000901    148-171
***** IPB000291 (D-alanine--D-alanine ligase) with a combined E-value of 1.8e-06.
    IPB000291B    75-112
    IPB000291C    153-190
    IPB000291E    243-278


 ProDom Summary:  Protein Domain Search
Residues 54-95 are 54% similar to a (PROTEOME COMPLETE CARBOXYLASE BIOTIN) protein domain (PD377840 which is seen in Q9PN09_CAMJE.

Residues 293-443 are 79% similar to a (CARBOXYLASE BIOTIN LIGASE ACETYL-COA PYRUVATE PROTEOME) protein domain (PD000755 which is seen in Q9CHF3_LACLA.

Residues 218-292 are 52% similar to a (CARBOXYLASE BIOTIN PEPTIDE PRECURSOR) protein domain (PD253426 which is seen in O67449_AQUAE.

Residues 57-97 are 56% similar to a (PROTEOME COMPLETE BIOTIN FATTY) protein domain (PD337090 which is seen in P71538_MYCTU.

Residues 59-92 are 85% similar to a (CARBOXYLASE BIOTIN PYRUVATE LIGASE PROTEOME COMPLETE) protein domain (PD371458 which is seen in Q9FBB9_STRPN.

Residues 126-292 are 42% similar to a (LIGASE SYNTHETASE CARBOXYLASE COMPLETE PROTEOME) protein domain (PD000180 which is seen in Q9K3W3_STRCO.

Residues 3-52 are 90% similar to a (CARBOXYLASE BIOTIN PYRUVATE PROTEOME LIGASE COMPLETE) protein domain (PD000820 which is seen in Q9FBB9_STRPN.


Paralogs:  Local Blast Search
SMu1582 is paralogously related (blast p-value < 1e-3) to SMu0784, and SMu0045.


Pfam Summary:  Pfam Search
Residues 1 to 113 (E-value = 1.8e-47) place SMu1582 in the CPSase_L_chain family which is described as Carbamoyl-phosphate synthase L chain, N-terminal domain (PF00289)
Residues 115 to 330 (E-value = 2.7e-102) place SMu1582 in the CPSase_L_D2 family which is described as Carbamoyl-phosphate synthase L chain, ATP binding domain (PF02786)
Residues 337 to 444 (E-value = 4.2e-51) place SMu1582 in the Biotin_carb_C family which is described as Biotin carboxylase C-terminal domain (PF02785)

 Top PDB Hits:
pdb1DV1A Chain A, Structure Of Biotin Carboxylase (Apo) >gi9... 447 1e-126
pdb1DV2A Chain A, The Structure Of Biotin Carboxylase, Mutant... 446 3e-126
pdb1CE8A Chain A, Carbamoyl Phosphate Synthetase From Escheri... 71 4e-013

Gene Protein Sequence:
MFKKILIANRGEIAVRIIRAARELGIVTVAVYSEADKESLHTLLADEAVC
VGPAKSTDSYLNMNAILSAAIVTGAEAIHPGFGFLSENSKFATMCEEMRI
KFIGPSASVMDKMGDKINARSEMLKAKVPVIPGSDGEVFTAQEALEIAQD
IGYPVMLKASAGGGGKGIRKVDKKEDLTAAFESASQEALSAFGNGAMYLE
KVIYPARHIEVQILGDSFGNIIHLGERDCSLQRNNQKVLEESPSIAIGKT
LRGKMGDAAVRAAKAVAYENAGTIEFLLDEASGQFYFMEMNTRVQVEHPV
TEFVTGIDIVKEQIKIAAGQELTYQQKDIVISGHAIECRINAENPKFNFA
PSPGKVEDLFLPSGGVGLRVDSAMYNNYTIPPYYDSMIAKIIVHGENRFD
ALMKMQRALYEFEVTGVVTNAEFQLDLISNPNVIAGDYDTSFLMETFLPA
YANDKE

Gene Nucleotide Sequence:  Sequence Viewer
ATGTTTAAGAAAATTTTGATTGCCAATCGTGGTGAAATCGCTGTGCGTAT
CATTCGAGCAGCCAGAGAATTAGGAATTGTGACTGTTGCAGTTTATTCAG
AAGCAGATAAAGAATCGCTTCACACCCTCTTAGCAGATGAGGCTGTATGT
GTTGGACCGGCTAAATCAACGGATTCTTACCTTAATATGAATGCTATTTT
ATCAGCAGCTATTGTAACTGGAGCTGAAGCTATTCATCCAGGTTTTGGTT
TTTTAAGTGAAAATTCTAAATTTGCAACTATGTGTGAAGAGATGCGTATT
AAGTTTATTGGTCCATCTGCATCTGTTATGGACAAAATGGGTGATAAAAT
TAATGCACGTTCTGAAATGCTTAAAGCCAAGGTTCCTGTTATTCCAGGGT
CAGATGGGGAAGTTTTTACTGCCCAAGAAGCATTAGAAATTGCCCAAGAT
ATTGGCTATCCTGTTATGCTGAAAGCTTCTGCTGGTGGTGGTGGTAAGGG
CATCCGTAAGGTTGATAAAAAGGAAGATCTAACAGCAGCTTTTGAGTCAG
CCTCTCAAGAGGCTCTATCAGCTTTTGGCAATGGCGCTATGTATCTGGAA
AAAGTCATTTATCCCGCTCGCCATATAGAAGTTCAAATACTGGGGGACTC
TTTTGGCAATATTATTCATCTTGGTGAACGTGATTGTTCATTGCAACGTA
ATAATCAAAAGGTCTTAGAAGAAAGCCCTTCTATAGCTATTGGGAAAACA
CTTCGTGGTAAAATGGGTGATGCAGCAGTTCGTGCCGCTAAAGCGGTTGC
TTATGAAAATGCCGGAACAATTGAATTTCTCTTGGATGAGGCTTCAGGGC
AATTCTATTTTATGGAAATGAACACACGTGTTCAGGTCGAACATCCTGTA
ACAGAATTTGTGACTGGTATTGATATCGTTAAAGAACAGATTAAAATTGC
TGCTGGTCAAGAATTGACTTATCAACAAAAAGATATTGTTATTTCAGGGC
ATGCTATTGAATGTCGGATTAATGCAGAAAATCCTAAATTTAATTTCGCA
CCTAGCCCAGGTAAAGTTGAAGATCTCTTTTTACCAAGTGGTGGCGTTGG
TTTACGTGTTGATAGTGCTATGTACAATAACTATACTATTCCGCCTTATT
ATGACAGTATGATTGCCAAAATCATTGTTCATGGAGAAAACCGCTTTGAT
GCTTTAATGAAAATGCAGCGTGCTCTGTATGAATTTGAAGTAACTGGTGT
GGTTACGAATGCAGAGTTTCAACTGGACTTAATTTCTAATCCAAATGTTA
TTGCTGGTGATTATGATACTTCTTTTTTGATGGAAACTTTTTTACCCGCT
TATGCTAATGATAAAGAATAG

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