ID A0A4R0PE86_9HYPH Unreviewed; 448 AA.
AC A0A4R0PE86;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE RecName: Full=Biotin carboxylase {ECO:0000256|ARBA:ARBA00017242, ECO:0000256|RuleBase:RU365063};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263, ECO:0000256|RuleBase:RU365063};
DE AltName: Full=Acetyl-coenzyme A carboxylase biotin carboxylase subunit A {ECO:0000256|ARBA:ARBA00033786, ECO:0000256|RuleBase:RU365063};
GN Name=accC {ECO:0000313|EMBL:TCD14505.1};
GN ORFNames=E0D97_10630 {ECO:0000313|EMBL:TCD14505.1};
OS Oricola cellulosilytica.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Ahrensiaceae; Oricola.
OX NCBI_TaxID=1429082 {ECO:0000313|EMBL:TCD14505.1, ECO:0000313|Proteomes:UP000291301};
RN [1] {ECO:0000313|EMBL:TCD14505.1, ECO:0000313|Proteomes:UP000291301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 52183 {ECO:0000313|EMBL:TCD14505.1,
RC ECO:0000313|Proteomes:UP000291301};
RX PubMed=25566955; DOI=10.1007/s10482-014-0370-6;
RA Hameed A., Shahina M., Lai W.A., Lin S.Y., Young L.S., Liu Y.C., Hsu Y.H.,
RA Young C.C.;
RT "Oricola cellulosilytica gen. nov., sp. nov., a cellulose-degrading
RT bacterium of the family Phyllobacteriaceae isolated from surface seashore
RT water, and emended descriptions of Mesorhizobium loti and Phyllobacterium
RT myrsinacearum.";
RL Antonie Van Leeuwenhoek 107:759-771(2015).
CC -!- FUNCTION: This protein is a component of the acetyl coenzyme A
CC carboxylase complex; first, biotin carboxylase catalyzes the
CC carboxylation of the carrier protein and then the transcarboxylase
CC transfers the carboxyl group to form malonyl-CoA.
CC {ECO:0000256|ARBA:ARBA00003761, ECO:0000256|RuleBase:RU365063}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-biotinyl-L-lysyl-[protein] + hydrogencarbonate + ATP =
CC N(6)-carboxybiotinyl-L-lysyl-[protein] + ADP + phosphate + H(+);
CC Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC ChEBI:CHEBI:456216; EC=6.3.4.14;
CC Evidence={ECO:0000256|ARBA:ARBA00048600,
CC ECO:0000256|RuleBase:RU365063};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956,
CC ECO:0000256|RuleBase:RU365063}.
CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer of biotin carboxyl
CC carrier protein, biotin carboxylase and the two subunits of carboxyl
CC transferase in a 2:2 complex. {ECO:0000256|ARBA:ARBA00011750,
CC ECO:0000256|RuleBase:RU365063}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TCD14505.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SJST01000003; TCD14505.1; -; Genomic_DNA.
DR RefSeq; WP_131568597.1; NZ_JAINFK010000002.1.
DR AlphaFoldDB; A0A4R0PE86; -.
DR OrthoDB; 9763189at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000291301; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR FunFam; 3.30.1490.20:FF:000018; Biotin carboxylase; 1.
DR FunFam; 3.40.50.20:FF:000010; Propionyl-CoA carboxylase subunit alpha; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR051602; ACC_Biotin_Carboxylase.
DR InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CPAse_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR NCBIfam; TIGR00514; accC; 1.
DR NCBIfam; NF006367; PRK08591.1; 1.
DR PANTHER; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Biotin {ECO:0000256|ARBA:ARBA00023267, ECO:0000256|RuleBase:RU365063};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW ECO:0000256|RuleBase:RU365063};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832,
KW ECO:0000256|RuleBase:RU365063};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU365063};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|RuleBase:RU365063};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU365063}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000291301}.
FT DOMAIN 1..444
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 448 AA; 48547 MW; 8B59DC37C82AFFBD CRC64;
MFNKVLIANR GEIALRVLRA CKELGIPTVA VHSTADESAM HVRLADESVC IGPPPSRDSY
LNIHQIVAAC EITGADAVHP GYGFLSENAK FAEILEAHNI TFIGPTAEHI SVMGDKIEAK
RTAAKLGIPV VPGSEGGVSD EGEAKKIAAD IGYPVIIKAT AGGGGRGMKV ARSEDDLLVA
LQTARSEAGA AFGNDAVYIE KYLGQPRHIE IQVVGDGAGA GVHLGERDCS LQRRHQKVWE
EANSPALNEK QRNEIGMICA NAIAEMGYRG AGTIEFLYEN GEFYFIEMNT RLQVEHPVTE
AITGIDLVHE QLRVASGAGL SVTQDQITFE GHAIECRINA EDARTFVPSP GTITHYHTPG
GLGVRVDSGV YAGYRIPPYY DSLIGKLIVH GRNRVECMMR LRRCLDEFVV DGIKSTLPLF
QDLVQNPDIA NGDYDIHWLE KYLANHAA
//
