Q01NE1 (Q01NE1_SOLUE) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823
Short name=ACCase subunit alpha HAMAP MF_00823
Short name=Acetyl-CoA carboxylase carboxyltransferase subunit alpha HAMAP MF_00823
EC=6.4.1.2 HAMAP MF_00823

Gene names

Name:	accA HAMAP MF_00823
Ordered Locus Names:	Acid_7935

Organism

Solibacter usitatus (strain Ellin6076) [Complete proteome] [HAMAP]

Taxonomic identifier

234267 [NCBI]

Taxonomic lineage

Bacteria › Acidobacteria › Solibacteres › Solibacterales › Solibacteraceae › Candidatus Solibacter

Protein attributes

Sequence length	270 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO2 group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA By similarity. HAMAP MF_00823 SAAS SAAS011763
Catalytic activity	ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. HAMAP MF_00823 SAAS SAAS011763
Pathway	Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. HAMAP MF_00823 SAAS SAAS011763
Subunit structure	Acetyl-CoA carboxylase is an heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD) By similarity. HAMAP MF_00823 SAAS SAAS011763
Subcellular location	Cytoplasm By similarity HAMAP MF_00823 SAAS SAAS011763.
Sequence similarities	Belongs to the AccA family. HAMAP MF_00823

Ontologies

Keywords
Biological process	Fatty acid biosynthesis HAMAP MF_00823 SAAS SAAS011763 Lipid synthesis
Cellular component	Cytoplasm HAMAP MF_00823 SAAS SAAS011763
Ligand	ATP-binding HAMAP MF_00823 SAAS SAAS011763 Nucleotide-binding
Molecular function	Ligase HAMAP MF_00823 SAAS SAAS011763 Transferase EMBL ABJ88829.1
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	acetyl-CoA carboxylase complex Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetyl-CoA carboxylase activity Inferred from electronic annotation. Source: HAMAP transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q01NE1 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 605CDE3B6AC40FE1	FASTA	270	29,632
	10 20 30 40 50 60 MDQPGGNPAW RRVQLARHPK RPHSLDYIGR IFQDFQELHG DRNFGDDPAI VAGMAQFENR 70 80 90 100 110 120 PVMIVAEQKG RDTKQRFFRN FGMPKPEGYR KALRMMQLAA KFGRPIITFL DTPGAYPGID 130 140 150 160 170 180 AEERGQAEAI ARNLREMARL AVPVIVVCIG EGGSGGALAL GVGNTVLMLE NAVYSVISPE 190 200 210 220 230 240 SCAAIIYRDS AKAEQAAAAL RLTAEDLKSL GLIDGIIPEP GEGAHEDHDA AAESLRQHLS 250 260 270 ARLSELESIG PVQIVEHRYA KFRRMGNFFA

References

[1]

"Three genomes from the phylum Acidobacteria provide insight into the lifestyles of these microorganisms in soils." Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C., Davidsen T.M. , DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R. Appl. Environ. Microbiol. 75:2046-2056(2009) [PubMed: 19201974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000473 Genomic DNA. Translation: ABJ88829.1.
RefSeq	YP_829114.1. NC_008536.1.
3D structure databases
ProteinModelPortal	Q01NE1.
SMR	Q01NE1. Positions 5-267.
ModBase	Search...
Protein-protein interaction databases
STRING	Q01NE1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4424194.
GenomeReviews	Gene locus Acid_7935 in contig CP000473_GR.
KEGG	sus:Acid_7935.
NMPDR	fig|234267.9.peg.7536.
PATRIC	32018674. VBICanSol30224_8281.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0825.
HOGENOM	HBG286557.
OMA	GRDTKDN.
PhylomeDB	Q01NE1.
Family and domain databases
HAMAP	MF_00823. AcetylCoA_CT_alpha. [Tree]
InterPro	IPR001095. Acetyl_CoA_COase_a_su. IPR011763. COA_CT_C. [Graphical view]
KO	K01962.
PANTHER	PTHR22855:SF3. Ac-CoA_carboxylA. 1 hit.
Pfam	PF03255. ACCA. 1 hit. [Graphical view]
PRINTS	PR01069. ACCCTRFRASEA.
TIGRFAMs	TIGR00513. AccA. 1 hit.
PROSITE	PS50989. COA_CT_CTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q01NE1_SOLUE

Accession

Primary (citable) accession number: Q01NE1

Entry history

Integrated into UniProtKB/TrEMBL:	November 14, 2006
Last sequence update:	November 14, 2006
Last modified:	December 14, 2011
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)