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Reviewed, UniProtKB/Swiss-Prot P49787 (ACCC1_BACSU)

Last modified November 3, 2009. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Biotin carboxylase 1
    EC=6.3.4.14
Alternative name(s):
    Acetyl-CoA carboxylase subunit A 1
      Short name=ACC 1
    EC=6.4.1.2
Gene names
Name: accC1
Synonyms: accC, yqhX
Ordered Locus Names: BSU24340
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA By similarity.

Catalytic activity

ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein.

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.

Pathway

Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.

Subunit structure

Acetyl-CoA carboxylase is an heterohexamer of biotin carboxyl carrier protein, biotin carboxylase and the two subunits of carboxyl transferase in a 2:2 complex By similarity.

Sequence similarities

Contains 1 ATP-grasp domain.

Contains 1 biotin carboxylation domain.

Caution

Leu-235 is present instead of the conserved His which is expected to bind ATP.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 450450Biotin carboxylase 1
PRO_0000146789

Regions

Domain1 – 447447Biotin carboxylation
Domain120 – 318199ATP-grasp

Sites

Active site2931 By similarity
Binding site1161ATP By similarity
Binding site2001ATP By similarity

Experimental info

Sequence conflict1071A → P in BAA12569. Ref.2
Sequence conflict1931G → R in BAA12569. Ref.2
Sequence conflict2401E → G in AAB00183. Ref.1
Sequence conflict2481D → G in AAB00183. Ref.1
Sequence conflict344 – 3485NPSKN → TQVK in AAB00183. Ref.1
Sequence conflict357 – 3626KMYLPP → NVPAS in AAB00183. Ref.1
Sequence conflict409 – 4102SE → QQ in AAB00183. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P49787-1 [UniParc].

Last modified July 7, 2009. Version 3.
Checksum: 2F93B3E793478334

FASTA45049,452
        10         20         30         40         50         60 
MIKKLLIANR GEIAVRIIRA CRELGIETVA VYSEADKDAL HVQMADEAFC IGPKASKDSY 

        70         80         90        100        110        120 
LNVTNIVSVA KLTGTDAIHP GYGFLAENAD FAELCEEVNV TFVGPSADAI SKMGTKDVAR 

       130        140        150        160        170        180 
ETMKQAGVPI VPGSQGIIEN VEEAVSLANE IGYPVIIKAT AGGGGKGIRV ARTEEELING 

       190        200        210        220        230        240 
IKITQQEAAT AFGNPGVYIE KYIEDFRHVE IQVLADNYGN TIHLGERDCS IQRRLQKLLE 

       250        260        270        280        290        300 
ESPSPALDSE IREQMGDAAV KAAKAVGYTG AGTVEFIYDY NEQRYYFMEM NTRIQVEHPV 

       310        320        330        340        350        360 
TEMVTGTDLI KEQIKVASGM ELSLKQEDVE FEGWAIECRI NAENPSKNFM PSPGEIKMYL 

       370        380        390        400        410        420 
PPGGLGVRVD SAAYPGYSIP PYYDSMIAKV ITYGKTRDEA IARMKRALSE FVIEGIETTI 

       430        440        450 
PFHLKLLEHE TFVSGEFNTK FLETYDVMGS

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References

« Hide 'large scale' references
[1]"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."
Marini P.E., Li S.J., Gardiol D., Cronan J.E. Jr., de Mendoza D.
J. Bacteriol. 177:7003-7006(1995) [PubMed: 7592499] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes."
Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y.
Microbiology 142:3103-3111(1996) [PubMed: 8969508] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / JH642.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[4]"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract]
Cited for: SEQUENCE REVISION TO 107 AND 193.

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Cross-references

Sequence databases

U36245 Genomic DNA. Translation: AAB00183.1.
D84432 Genomic DNA. Translation: BAA12569.1.
AL009126 Genomic DNA. Translation: CAB14365.2.
PIRA69581.
RefSeqNP_390314.2.

3D structure databases

HSSPHSSP built from PDB template 1BNC based on UniProtKB P24182.
ModBaseSearch...

Genome annotation databases

GeneID938588.
GenomeReviewsGene locus BSU24340 in contig AL009126_GR.
KEGGbsu:BSU24340.
NMPDRfig|224308.1.peg.2438.

Organism-specific databases

SubtiListBG11384. accC. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP49787.
OMADFNTKFL.

Enzyme and pathway databases

BioCycBSUB224308:BSU2432-MON.
BRENDA6.3.4.14. 150.
6.4.1.2. 150.

Family and domain databases

InterProIPR004549. Acetyl_CoA_COase_biotin_COase.
IPR011761. ATP-grasp.
IPR013816. ATP_grasp_subdomain_2.
IPR011764. BC.
IPR005482. Biotin_COase_C.
IPR005479. CarbamoylP_synth_lsu_ATP-bd.
IPR005481. CarbamoylP_synth_lsu_N.
IPR013817. Pre-ATP_grasp.
[Graphical view]
Gene3DG3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit.
G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
PfamPF02785. Biotin_carb_C. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
TIGRFAMsTIGR00514. accC. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameACCC1_BACSU
AccessionPrimary (citable) accession number: P49787
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 7, 2009
Last modified: November 3, 2009
This is version 85 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents