ID A0A285NSZ1_9AQUI Unreviewed; 282 AA.
AC A0A285NSZ1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395};
DE Short=ACCase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395};
DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395};
DE EC=2.1.3.15 {ECO:0000256|HAMAP-Rule:MF_01395};
GN Name=accD {ECO:0000256|HAMAP-Rule:MF_01395};
GN ORFNames=SAMN06265353_0055 {ECO:0000313|EMBL:SNZ10801.1};
OS Hydrogenobacter hydrogenophilus.
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae;
OC Hydrogenobacter.
OX NCBI_TaxID=35835 {ECO:0000313|EMBL:SNZ10801.1, ECO:0000313|Proteomes:UP000218627};
RN [1] {ECO:0000313|EMBL:SNZ10801.1, ECO:0000313|Proteomes:UP000218627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2913 {ECO:0000313|EMBL:SNZ10801.1,
RC ECO:0000313|Proteomes:UP000218627};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex.
CC Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its
CC carrier protein (BCCP) and then the CO(2) group is transferred by the
CC transcarboxylase to acetyl-CoA to form malonyl-CoA.
CC {ECO:0000256|ARBA:ARBA00025280, ECO:0000256|HAMAP-Rule:MF_01395}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-
CC CoA + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:54728,
CC Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.15;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01395};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01395};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01395};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01395}.
CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin
CC carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two
CC subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta
CC (AccD). {ECO:0000256|HAMAP-Rule:MF_01395}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01395}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000256|HAMAP-
CC Rule:MF_01395}.
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DR EMBL; OBEN01000001; SNZ10801.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285NSZ1; -.
DR OrthoDB; 9772975at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000218627; Unassembled WGS sequence.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_01395; AcetylCoA_CT_beta; 1.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR041010; Znf-ACC.
DR NCBIfam; TIGR00515; accD; 1.
DR PANTHER; PTHR42995; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1.
DR PANTHER; PTHR42995:SF5; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF17848; zf-ACC; 1.
DR PRINTS; PR01070; ACCCTRFRASEB.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01395}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01395};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW Rule:MF_01395};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW Rule:MF_01395};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_01395};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_01395};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01395};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01395};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01395};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01395};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW Rule:MF_01395}.
FT DOMAIN 18..282
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT ZN_FING 22..44
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
SQ SEQUENCE 282 AA; 31818 MW; 265835448D7A71BA CRC64;
MGILDRFFKK KREEKESLWT KCPECKTILY MPELSANLKV CPKCNYHFPM SAKERIESLL
DENAQLLFEN ILPKDPLRFK DTKPYKDRLK QAQEDTGLSE AIVVVRGNLK DINVVLAVMD
FNFIGGSMGS VVGERFYRAC KLCSNEELPL ISVITSGGAR MQEGILSLMQ MAKTSIGVGF
LREKGVPYIT VLTDPTMGGV SASFAFLGDI IIAEPKSLIG FAGPRVIEQT IKQQLPEGFQ
RAEFLLEKGM IDMVVHRKEL KDTLYKLLSM ATYWKRFNLT AL
//
