Reviewed, UniProtKB/Swiss-Prot Q57417 (ACCD_SYNY3)

Names and origin

Protein names

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

Gene names

Name:	accD
Synonyms:	zfpA
Ordered Locus Names:	sll0336

Organism

Synechocystis sp. (strain PCC 6803) [Complete proteome] [HAMAP]

Taxonomic identifier

1148 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechocystis

Protein attributes

Sequence length	326 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO2 group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA By similarity.
Catalytic activity	ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. HAMAP MF_01395
Cofactor	Binds 1 zinc ion per subunit By similarity.
Pathway	Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. HAMAP MF_01395
Subunit structure	Acetyl-CoA carboxylase is a 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.
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the accD/PCCB family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Cytoplasm
Domain	Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Ligase
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 zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 326	326	Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta HAMAP MF_01395		PRO_0000199776
Regions
	Zinc finger	36 – 58	23	C4-type Potential
Sites
	Metal binding	36	1	Zinc By similarity
	Metal binding	39	1	Zinc By similarity
	Metal binding	55	1	Zinc By similarity
	Metal binding	58	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q57417-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 99177B806671A85B	FASTA	326	36,396
	10 20 30 40 50 60 MSLFDWFANR EKAEPPVLQP QSPQEREVAD GLWTKCPACG VLTYTKDLQG NWMVCVECGH 70 80 90 100 110 120 HLRVDSDERI RQLIDAKTWQ PINEHLRPTD PLKFKDRKSY KDRIRDTQKA TDLTDAVQTG 130 140 150 160 170 180 HGRLDGLPIA LGVMDFRFMG GSMGSVVGEK LCRLIEYATL ERLPVVIICA SGGARMQEGM 190 200 210 220 230 240 LSLMQMAKIS GALQNHREQK LLYIPVLTHP TTGGVTASFA MLGDLILAEP KATIGFAGRR 250 260 270 280 290 300 VIEQTLREKL PDDFQTSEYL LHHGFVDAIV PRPQLKRTLA QLISLHQPFY PILPPLNADS 310 320 NQVNPELVLS HTALAVDNQI SVNQDG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Gene encoding a putative zinc finger protein in Synechocystis PCC6803." Ogura Y., Yoshida T., Nakamura Y., Takemura M., Oda K., Ohyama K. Agric. Biol. Chem. 55:2259-2264(1991) [PubMed: 1368738] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome." Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S. DNA Res. 2:153-166(1995) [PubMed: 8590279] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	D10004 Genomic DNA. Translation: BAA00893.1. S77740 Genomic DNA. Translation: AAC60398.1. BA000022 Genomic DNA. Translation: BAA10092.1.
PIR	JQ1238.
RefSeq	NP_442022.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q57417. 5 interactions.
STRING	Q57417.
Genome annotation databases
GeneID	952744.
GenomeReviews	Gene locus sll0336 in contig BA000022_GR.
KEGG	syn:sll0336.
NMPDR	fig|1148.1.peg.2123.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG285696.
OMA	ENLWIKC.
Enzyme and pathway databases
BioCyc	SSP1148:SLL0336-MON.
Family and domain databases
HAMAP	MF_01395. [Tree]
InterPro	IPR000438. Acetyl_CoA_COase_Trfase_b_su. IPR000022. Carboxyl_trans. IPR011762. COA_CT_N. [Graphical view]
Pfam	PF01039. Carboxyl_trans. 1 hit. [Graphical view]
PRINTS	PR01070. ACCCTRFRASEB.
PROSITE	PS50980. COA_CT_NTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACCD_SYNY3

Accession

Primary (citable) accession number: Q57417

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	December 15, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)