Biotin carboxylase - Nostoc sp. (strain PCC 7120 / UTEX 2576)

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Q06862 (ACCC_NOSS1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 88. History...

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

Documents (2) |

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
EC=6.3.4.14

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

Gene names

Name:	accC
Ordered Locus Names:	alr0939

Organism

Nostoc sp. (strain PCC 7120 / UTEX 2576) [Complete proteome] [HAMAP]

Taxonomic identifier

103690 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Nostoc

Protein attributes

Sequence length	447 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
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 – 447

447

Biotin carboxylase

PRO_0000146787

Regions

Domain

1 – 447

447

Biotin carboxylation

Domain

121 – 318

198

ATP-grasp

Sites

Active site

293

By similarity

Binding site

117

ATP By similarity

Binding site

201

ATP By similarity

Binding site

236

ATP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q06862 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 8A541B38B39E00F9
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FASTA

447

49,104

        10         20         30         40         50         60 
MKFDKILIAN RGEIALRILR ACEEMGIATI AVHSTVDRNA LHVQLADEAV CIGEPASAKS 

        70         80         90        100        110        120 
YLNIPNIIAA ALTRNASAIH PGYGFLSENA KFAEICADHH IAFIGPTPEA IRLMGDKSTA 

       130        140        150        160        170        180 
KETMQKAGVP TVPGSEGLVE TEQEGLELAK DIGYPVMIKA TAGGGGRGMR LVRSPDEFVK 

       190        200        210        220        230        240 
LFLAAQGEAG AAFGNAGVYI EKFIERPRHI EFQILADNYG NVIHLGERDC SIQRRNQKLL 

       250        260        270        280        290        300 
EEAPSPALDS DLREKMGQAA VKAAQFINYT GAGTIEFLLD RSGQFYFMEM NTRIQVEHPV 

       310        320        330        340        350        360 
TEMVTGVDLL VEQIRIAQGE RLRLTQDQVV LRGHAIECRI NAEDPDHDFR PAPGRISGYL 

       370        380        390        400        410        420 
PPGGPGVRID SHVYTDYQIP PYYDSLIGKL IVWGPDRATA INRMKRALRE CAITGLPTTI 

       430        440 
GFHQRIMENP QFLQGNVSTS FVQEMNK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genes for two subunits of acetyl coenzyme A carboxylase of Anabaena sp. strain PCC 7120: biotin carboxylase and biotin carboxyl carrier protein." Gornicki P., Scappino L.A., Haselkorn R. J. Bacteriol. 175:5268-5272(1993) [PubMed: 8102363] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120." Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. , Takazawa M., Yamada M., Yasuda M., Tabata S. DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 7120 / UTEX 2576.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L14862 Genomic DNA. Translation: AAB51770.1. BA000019 Genomic DNA. Translation: BAB72896.1.
PIR	A53311. AH1923.
RefSeq	NP_484982.1. NC_003272.1.
3D structure databases
ProteinModelPortal	Q06862.
SMR	Q06862. Positions 3-444.
ModBase	Search...
Protein-protein interaction databases
STRING	Q06862.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1104533.
GenomeReviews	Gene locus alr0939 in contig BA000019_GR.
KEGG	ana:alr0939.
NMPDR	fig\|103690.1.peg.1249.
PATRIC	22771750. VBINosSp37423_1359.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0439.
HOGENOM	HBG535236.
OMA	WSTARTE.
PhylomeDB	Q06862.
ProtClustDB	PRK08591.
Enzyme and pathway databases
BioCyc	NSP103690:ALR0939-MONOMER.
Family and domain databases
InterPro	IPR004549. Acetyl_CoA_COase_biotin_COase. 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.
TIGRFAMs	TIGR00514. AccC. 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

ACCC_NOSS1

Accession

Primary (citable) accession number: Q06862

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	January 25, 2012
This is version 88 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

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

Protein-protein interaction 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