ID A0A0H4WJF7_9BORD Unreviewed; 292 AA.
AC A0A0H4WJF7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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 ECO:0000313|EMBL:AKQ56616.1};
GN ORFNames=ACR54_03314 {ECO:0000313|EMBL:AKQ56616.1}, CS347_14700
GN {ECO:0000313|EMBL:AZW17926.1};
OS Bordetella hinzii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=103855 {ECO:0000313|EMBL:AKQ56616.1, ECO:0000313|Proteomes:UP000036382};
RN [1] {ECO:0000313|EMBL:AKQ56616.1, ECO:0000313|Proteomes:UP000036382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F582 {ECO:0000313|EMBL:AKQ56616.1,
RC ECO:0000313|Proteomes:UP000036382};
RX PubMed=26316634;
RA Weigand M.R., Changayil S., Kulasekarapandian Y., Tondella M.L.;
RT "Complete Genome Sequences of Two Bordetella hinzii Strains Isolated from
RT Humans.";
RL Genome Announc. 3:e00965-e00915(2015).
RN [2] {ECO:0000313|Proteomes:UP000036382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F582 {ECO:0000313|Proteomes:UP000036382};
RA Weigand M.R., Changayil S., Kulasekarapandian Y., Batra D., Williams M.M.,
RA Tondella M.L.;
RT "Complete Genome Sequences of Two Bordetella hinzii Isolated from Humans.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000282741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H720 {ECO:0000313|Proteomes:UP000282741};
RA Weigand M.R., Loparev V., Peng Y., Bowden K.E., Tondella M.L.,
RA Williams M.M.;
RT "Whole genome sequencing of various Bordetella species.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AZW17926.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H720 {ECO:0000313|EMBL:AZW17926.1};
RX PubMed=31744907;
RA Weigand M.R., Peng Y., Batra D., Burroughs M., Davis J.K., Knipe K.,
RA Loparev V.N., Johnson T., Juieng P., Rowe L.A., Sheth M., Tang K.,
RA Unoarumhi Y., Williams M.M., Tondella M.L.;
RT "Conserved Patterns of Symmetric Inversion in the Genome Evolution of
RT Bordetella Respiratory Pathogens.";
RL mSystems 4:e00702-19(2019).
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; CP012076; AKQ56616.1; -; Genomic_DNA.
DR EMBL; CP024172; AZW17926.1; -; Genomic_DNA.
DR RefSeq; WP_032957272.1; NZ_LT906461.1.
DR STRING; 103855.ACR54_03314; -.
DR GeneID; 56621397; -.
DR KEGG; bhz:ACR54_03314; -.
DR PATRIC; fig|103855.14.peg.3203; -.
DR eggNOG; COG0777; Bacteria.
DR OrthoDB; 9772975at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000036382; Chromosome.
DR Proteomes; UP000282741; Chromosome.
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}; Ligase {ECO:0000313|EMBL:AKQ56616.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000036382};
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 27..292
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT ZN_FING 31..53
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
SQ SEQUENCE 292 AA; 31982 MW; A7101AA81FCA06E4 CRC64;
MSWIEKLLPP RINKTSDSGV RRVPEGLWVK CPSCESVLYS EDLAANLHVC PKCSHHMRIG
ARARIDSLLD VEGRVEIGQT TRSVDSLKFK DTRKYPERIQ EAMKQTGETD ALVVMSGSIR
GVPATLACFE FEFMGGSMGS VVGERFVRGV KAAIEHKTPF ICVAASGGAR MQESLLSLMQ
MAKTNAMLTQ LARDDLPFIS VLTDPTMGGV SASFAFMGDV VIAEPKALIG FAGPRVIEQT
VREKLPEGFQ RAEFLLQKGA IDMVVDRRQL REELARLLAL LTNQPADIVT AA
//
