ID A0A249MT91_SPHXE Unreviewed; 448 AA.
AC A0A249MT91; A0A401IYQ9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 28-JAN-2026, entry version 31.
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:ASY44570.1};
GN ORFNames=CJD35_09020 {ECO:0000313|EMBL:ASY44570.1}, MBESOW_P0730
GN {ECO:0000313|EMBL:GBH29476.1};
OS Sphingobium xenophagum.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Sphingomonadales; Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=121428 {ECO:0000313|EMBL:ASY44570.1, ECO:0000313|Proteomes:UP000217141};
RN [1] {ECO:0000313|EMBL:GBH29476.1, ECO:0000313|Proteomes:UP000290975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OW59 {ECO:0000313|EMBL:GBH29476.1,
RC ECO:0000313|Proteomes:UP000290975};
RA Ohta Y., Nishi S., Hatada Y.;
RT "Whole genome sequencing of Sphingobium xenophagum OW59.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ASY44570.1, ECO:0000313|Proteomes:UP000217141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C1 {ECO:0000313|EMBL:ASY44570.1,
RC ECO:0000313|Proteomes:UP000217141};
RA Song D., Chen X., Xu M.;
RT "Whole Genome Sequence of Sphingobium hydrophobicum C1: Insights into
RT Adaption to the Electronic-waste Contaminated Sediment.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP022745; ASY44570.1; -; Genomic_DNA.
DR EMBL; BBQY01000001; GBH29476.1; -; Genomic_DNA.
DR RefSeq; WP_017181022.1; NZ_BBQY01000001.1.
DR AlphaFoldDB; A0A249MT91; -.
DR STRING; 1192759.GCA_000277525_00151; -.
DR KEGG; shyd:CJD35_09020; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000217141; Chromosome I.
DR Proteomes; UP000290975; 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; 3.30.470.20; 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; 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|RuleBase:RU365063};
KW Fatty acid metabolism {ECO:0000256|RuleBase:RU365063};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU365063};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU365063};
KW Lipid metabolism {ECO:0000256|RuleBase:RU365063};
KW 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:UP000290975}.
FT DOMAIN 2..445
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 448 AA; 48873 MW; 60043AFFB5BC2FBC CRC64;
MTIEKLLIAN RGEIALRIHR ACHEMGIKTV AVHSTADADA MHVRLADEAI CIGPPAARDS
YLNIAAIISA AEISGADAIH PGYGFLSENA KFAEIVEAHG IAFVGPKPEH IRTMGDKIEA
KRTAGALGLP LVPGSDGAIS DLEEAKAIAE KAGYPVIIKA ASGGGGRGMK VCTSPDELET
LMQQAGSEAK AAFGDATVYL EKYLGNPRHI EIQVFGDGNG NAIHLGERDC SLQRRHQKVL
EEAPSPILSQ ADRERIGGVC AKAMADMGYR GAGTIEFLWE DGEFYFIEMN TRLQVEHPVT
EMITGVDLVR EQIRIAEGKP LSVAQEDLRF TGHAIECRIN AEDPRTFAPS PGTVTRYHVP
GGMHVRVDSG LYQGYKVPPY YDSMIGKLIV YGRTREGCIM RLKRALQEYV IEGMKTTIPL
HQALLEDPQF LNGDYTIKWL EDWLAREG
//
