ID A0A975HL52_9GAMM Unreviewed; 648 AA.
AC A0A975HL52;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE RecName: Full=Biotin carboxylase {ECO:0000256|ARBA:ARBA00017242};
DE AltName: Full=Acetyl-coenzyme A carboxylase biotin carboxylase subunit A {ECO:0000256|ARBA:ARBA00033786};
GN ORFNames=J5O05_01825 {ECO:0000313|EMBL:QTH71726.1};
OS Pseudoalteromonas xiamenensis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=882626 {ECO:0000313|EMBL:QTH71726.1, ECO:0000313|Proteomes:UP000664904};
RN [1] {ECO:0000313|EMBL:QTH71726.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=STKMTI.2 {ECO:0000313|EMBL:QTH71726.1};
RA Handayani D.P., Isnansetyo A., Istiqomah I., Jumina J.;
RT "Complete Genome of Pseudoalteromonas xiamenensis STKMTI.2, a new potential
RT marine bacterium producing anti-Vibrio compounds.";
RL Submitted (MAR-2021) 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}.
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 -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956}.
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}.
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DR EMBL; CP072133; QTH71726.1; -; Genomic_DNA.
DR RefSeq; WP_208843350.1; NZ_CP072133.1.
DR AlphaFoldDB; A0A975HL52; -.
DR KEGG; pxi:J5O05_01825; -.
DR Proteomes; UP000664904; Chromosome.
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:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR FunFam; 3.30.1490.20:FF:000003; acetyl-CoA carboxylase isoform X1; 1.
DR FunFam; 3.30.470.20:FF:000028; Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial; 1.
DR FunFam; 3.40.50.20:FF:000010; Propionyl-CoA carboxylase subunit alpha; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR050856; Biotin_carboxylase_complex.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CPAse_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; NF006367; PRK08591.1; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 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 SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 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}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000664904}.
FT DOMAIN 1..446
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 571..644
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 648 AA; 70350 MW; 759862016015C6F7 CRC64;
MLKKILIANR GEIACRVMKT AKSLGMTTVA VYSDADANSQ HVKMADEAYH IGPAPTKDSY
LVASKILEVA KRAGADCVHP GYGFLSENDS FANTCEEVGI VFIGPPTSAI EAMGSKTRAK
EIMAEANVPL VPGYYGQNQD TQFLASEAEK IGYPVLIKAA FGGGGKGMRV VRAAADFISA
LEGAKREAKA SFGNDLVLIE RFVDKPRHVE VQVFADNHGN AVYLGDRDCS LQRRHQKVIE
EAPAPGLSAE LRKAMGEAAV RCAQAINYRG AGTVEFLLCG NEFFFMEMNT RLQVEHPVTE
MVTGQDLVAW QIRVANGEKL PLTQEQITLS GHSFEARIYA EDPTENFMPC SGTLSCLTFP
AEAFGVRIDT GVQCGDEISP FYDPMIAKLI VHGETREVAL NKLSHALEQV HLSGLKSNIA
FLHHLANHGT FKAGAPDTHF IDTQTEVLTH FAVPERTMTE LAALAYVLHQ NPCKKTPWKN
IGFRLNQNAV IKIPFVDVKT LATRVEEAWH LDIAGDNVIA QGQLDGQILS ASIDGKKLTA
HVVLNEESIT VMFGPHQFTL ALSSKHYVSD HEHEAAPLAA PLNGTVVKHL QSVGTKLKKG
DPVVVIEAMK MEYTLNAPFD GTLASYCFAE GELVSHGAML AIVDAEEA
//
