ID W4UWI2_9BACE Unreviewed; 504 AA.
AC W4UWI2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Biotin carboxylase {ECO:0000256|RuleBase:RU365063};
DE EC=6.3.4.14 {ECO:0000256|RuleBase:RU365063};
DE AltName: Full=Acetyl-coenzyme A carboxylase biotin carboxylase subunit A {ECO:0000256|RuleBase:RU365063};
GN ORFNames=JCM10512_3586 {ECO:0000313|EMBL:GAE85177.1};
OS Bacteroides reticulotermitis JCM 10512.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1445607 {ECO:0000313|EMBL:GAE85177.1, ECO:0000313|Proteomes:UP000019131};
RN [1] {ECO:0000313|EMBL:GAE85177.1, ECO:0000313|Proteomes:UP000019131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10512 {ECO:0000313|EMBL:GAE85177.1,
RC ECO:0000313|Proteomes:UP000019131};
RA Yuki M., Oshima K., Suda W., Sakamoto M., Iida T., Hattori M., Ohkuma M.;
RT "Draft Genome Sequence of Bacteroides reticulotermitis Strain JCM 10512T,
RT Isolated from the Gut of a Termite.";
RL Genome Announc. 2:e00072-14(2014).
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|RuleBase:RU365063}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
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|RuleBase:RU365063};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {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|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:GAE85177.1}.
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DR EMBL; BAIV01000024; GAE85177.1; -; Genomic_DNA.
DR RefSeq; WP_044164133.1; NZ_BAIV01000024.1.
DR AlphaFoldDB; W4UWI2; -.
DR STRING; 1445607.JCM10512_3586; -.
DR OrthoDB; 9807469at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000019131; Unassembled WGS sequence.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
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 GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
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; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR NCBIfam; TIGR00514; accC; 1.
DR PANTHER; PTHR45007; CARBOXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G07570)-RELATED; 1.
DR PANTHER; PTHR45007:SF1; CARBOXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G07570)-RELATED; 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}; Biotin {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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000019131}.
FT DOMAIN 1..446
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 504 AA; 56653 MW; E60A9F1CB2981BAD CRC64;
MIKKILVANR GEIAVRVMRS CREMEIKSIA IFSEADRTAK HVLYADEAYC VGPAASKESY
LNIEKIIEVA KISQADAIHP GYGFLSENAT FTRRCQEEGI IFIGPNAETM EAMGDKIAAR
IRMIEAGVPV VPGTQENLKS VEEAVELCNQ IGYPVMLKAS MGGGGKGMRL IHNADEVEEA
YTTAKSESLS SFGDDTVYLE KFVEEPHHIE FQILGDKHGN VIHLCERECS VQRRNQKIVE
ETPSAFITPE LRKDMGEKAV AAAKAVNYVG AGTIEFLVDK YRNYYFLEMN TRLQVEHPIT
EEVIGVDLVK EQIKVAGGEV LQLKQEDIQQ RGHAIECRIC AEDTEMNFMP SPGVIKQITE
PNGIGVRIDS YVYEGYEIPI YYDPMIGKLI VWATTRDYAI ERMRRVLHEY KITGIKNNIS
YLRAIMETPD FVEGHYDTGF ITKNAEYLKA YIMRTSERAE SIALIAAYID YLMNLEENNS
GLAADARPIS KWKAFGLQKG VLRI
//
