ID   ACCD_HYPNA              Reviewed;         326 AA.
AC   Q0BWJ8;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE            Short=ACCase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE            Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE            EC=2.1.3.15 {ECO:0000255|HAMAP-Rule:MF_01395};
GN   Name=accD {ECO:0000255|HAMAP-Rule:MF_01395}; OrderedLocusNames=HNE_3473;
OS   Hyphomonas neptunium (strain ATCC 15444).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomonadales;
OC   Hyphomonadaceae; Hyphomonas.
OX   NCBI_TaxID=228405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15444;
RX   PubMed=16980487; DOI=10.1128/jb.00111-06;
RA   Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G.,
RA   Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D.,
RA   Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R.,
RA   Brinkac L.M., Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G.,
RA   Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N.,
RA   Ward N.L.;
RT   "Comparative genomic evidence for a close relationship between the
RT   dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT   crescentus.";
RL   J. Bacteriol. 188:6841-6850(2006).
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. {ECO:0000255|HAMAP-
CC       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:0000255|HAMAP-Rule:MF_01395};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01395}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01395}.
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01395}.
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DR   EMBL; CP000158; ABI75588.1; -; Genomic_DNA.
DR   RefSeq; WP_011648439.1; NC_008358.1.
DR   AlphaFoldDB; Q0BWJ8; -.
DR   SMR; Q0BWJ8; -.
DR   STRING; 228405.HNE_3473; -.
DR   EnsemblBacteria; ABI75588; ABI75588; HNE_3473.
DR   KEGG; hne:HNE_3473; -.
DR   eggNOG; COG0777; Bacteria.
DR   HOGENOM; CLU_015486_1_0_5; -.
DR   OMA; PEGLWIK; -.
DR   OrthoDB; 504557at2; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000001959; 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: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.
DR   InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011762; COA_CT_N.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   PRINTS; PR01070; ACCCTRFRASEB.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..326
FT                   /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT                   subunit beta"
FT                   /id="PRO_0000389758"
FT   DOMAIN          25..308
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT   REGION          298..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   326 AA;  35843 MW;  57748D92B7DE6484 CRC64;
     MNWINKVTPP GLKTMMSKKD TPDDLWVKCP ASGELIYRND LEQSWYVTPA GAHLRISPRM
     RFRILFDDER WEPISLPQVP LDPLKFKDDK PYPARLKAAK AKILNRDIKE TEDGGAPLLQ
     EDCMVAAYGK IGGVPAVVLV QDFEFMGGSL GMAAGEAFIT AAQLALARKS AFVVCTASGG
     ARMQEGTLSL MQMPRTTLAI NDLADAKLPY VVVLTDPTSG GVSASYAMLG DVHIAEPGAM
     IAFSGPRVIE QTIRESLPKG FQRSEFLREK GQVDIVVDRR KLKATVARVL GHLLPMSRRR
     DDRSTLQLTP PKTHAPKPPE PKVKPD