Biotin carboxylase 2 - Bacillus subtilis

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O34544 (ACCC2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 90. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Biotin carboxylase 2
EC=6.3.4.14

Alternative name(s):
Acetyl-CoA carboxylase subunit A 2
Short name=ACC 2
EC=6.4.1.2

Gene names

Name:	accC2
Synonyms:	accC, yngH
Ordered Locus Names:	BSU18240

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	444 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 + carboxy-biotin-[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.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Ligand	ATP-binding Biotin Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetyl-CoA carboxylase activity Inferred from electronic annotation. Source: EC biotin carboxylase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 444

444

Biotin carboxylase 2

PRO_0000360841

Regions

Domain

1 – 444

444

Biotin carboxylation

Domain

120 – 317

198

ATP-grasp

Sites

Active site

292

By similarity

Binding site

116

ATP By similarity

Binding site

200

ATP By similarity

Binding site

235

ATP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O34544 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: C866DEB8B4177E3B
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FASTA

444

49,087

        10         20         30         40         50         60 
MFTKVLIANR GEIAMRIIRT CSRLGIKTVA VYSEADKDAP HTKAATEAYL IGESRVSESY 

        70         80         90        100        110        120 
LNIERIIKTA KKAKADAIHP GYGLLSENSR FAERCKQENI VFIGPSPDII AKMGSKIEAR 

       130        140        150        160        170        180 
KAMEAAGVPV VPGVSESLGD IEAACRTASQ IGYPVMLKAS AGGGGIGMQR VENEEALKKA 

       190        200        210        220        230        240 
YEGNKKRAAD FFGDGSMYIE KVIEHARHIE VQLLADQHGH TVHLFERDCS VQRRHQKVIE 

       250        260        270        280        290        300 
EAPSPFVDDE LRMKIGQTAV KAAKAIGYTN AGTIEFIVDQ KQNFYFLEMN TRLQVEHPVT 

       310        320        330        340        350        360 
EEITGLDLVE QQLRIAAGHT LTFSQKDIQR NGHAIEVRIY AEDPKTFFPS PGTITAFSLP 

       370        380        390        400        410        420 
DQKGVRHECA VAKDSTVTPF YDPMIAKMIV KGQTRTEAIE KLETALRDYR VEGIKTNLPL 

       430        440 
LIQAAATKAF KEGDVTTDFL KQHL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence completion, identification and definition of the fengycin operon in Bacillus subtilis 168." Tosato V., Albertini A.M., Zotti M., Sonda S., Bruschi C.V. Microbiology 143:3443-3450(1997) [PubMed: 9387222] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"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. Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y13917 Genomic DNA. Translation: CAA74216.1. AL009126 Genomic DNA. Translation: CAB13707.1.
PIR	E69893.
RefSeq	NP_389706.1. NC_000964.3.
3D structure databases
HSSP	HSSP built from PDB template 1BNC based on UniProtKB P24182.
ProteinModelPortal	O34544.
SMR	O34544. Positions 1-443.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000000111; EBBACP00000000111; EBBACG00000000111.
GeneID	939474.
GenomeReviews	Gene locus BSU18240 in contig AL009126_GR.
KEGG	bsu:BSU18240.
NMPDR	fig\|224308.1.peg.1828.
PATRIC	18975485. VBIBacSub10457_1934.
Organism-specific databases
GenoList	BSU18240. [Micado]
Phylogenomic databases
GeneTree	EBGT00050000001329.
HOGENOM	HBG535236.
OMA	ENHVTIT.
PhylomeDB	O34544.
ProtClustDB	PRK06111.
Enzyme and pathway databases
BioCyc	BSUB:BSU18240-MONOMER.
Family and domain databases
InterPro	IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR011764. Biotin_carboxylation_dom. IPR005482. Biotin_COase_C. IPR005479. CarbamoylP_synth_lsu_ATP-bd. IPR005481. CarbamoylP_synth_lsu_N. IPR013817. Pre-ATP_grasp. IPR016185. PreATP-grasp-like. IPR011054. Rudment_hybrid_motif. [Graphical view]
Gene3D	G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit. G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
KO	K01961.
Pfam	PF02785. Biotin_carb_C. 1 hit. PF00289. CPSase_L_chain. 1 hit. PF02786. CPSase_L_D2. 1 hit. [Graphical view]
SMART	SM00878. Biotin_carb_C. 1 hit. [Graphical view]
SUPFAM	SSF52440. PreATP-grasp-like. 1 hit. SSF51246. Rudmnt_hyb_motif. 1 hit.
PROSITE	PS50975. ATP_GRASP. 1 hit. PS50979. BC. 1 hit. PS00866. CPSASE_1. 1 hit. PS00867. CPSASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACCC2_BACSU

Accession

Primary (citable) accession number: O34544
Secondary accession number(s): Q799L8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	January 1, 1998
Last modified:	January 25, 2012
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

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·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents