ID G7GR82_9ACTN Unreviewed; 601 AA.
AC G7GR82;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN Name=accA {ECO:0000313|EMBL:GAB06107.1};
GN ORFNames=GOAMR_48_00170 {ECO:0000313|EMBL:GAB06107.1};
OS Gordonia amarae NBRC 15530.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1075090 {ECO:0000313|EMBL:GAB06107.1, ECO:0000313|Proteomes:UP000006023};
RN [1] {ECO:0000313|EMBL:GAB06107.1, ECO:0000313|Proteomes:UP000006023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 15530 {ECO:0000313|EMBL:GAB06107.1,
RC ECO:0000313|Proteomes:UP000006023};
RA Takarada H., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Gordonia amarae NBRC 15530.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00024172};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13502;
CC Evidence={ECO:0000256|ARBA:ARBA00024172};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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:GAB06107.1}.
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DR EMBL; BAED01000048; GAB06107.1; -; Genomic_DNA.
DR RefSeq; WP_005188499.1; NZ_BAED01000048.1.
DR AlphaFoldDB; G7GR82; -.
DR STRING; 1075090.GOAMR_48_00170; -.
DR eggNOG; COG4770; Bacteria.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000006023; 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:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 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; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
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:UP000006023}.
FT DOMAIN 11..455
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 130..327
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 528..601
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 601 AA; 63465 MW; 63CF1DFE6FF6DA4F CRC64;
MPTPSANTSQ GISKVLIANR GEIAVRVIRA ARDAGIPSVA VYAEPDAEAL FVKLADEAFA
LGGQTSAESY LVFDKILDAA AKSGANAIHP GYGFLSENAD FAQAVIDAGL IWIGPSPSSI
RDLGDKVTAR HIALKANAPM APGTKDPVAN ADEVVAFAQE HGVPVAIKAA FGGGGRGMKV
AYTIDEIPHL FESATREAIA AFGRGECFVE RYLDKARHVE AQVIADQHGN VVVAGTRDCS
LQRRFQKLVE EAPAPFLTDE QRTKIHESAK AICREAGYYG AGTVEFLVGN DGLVSFLEVN
TRLQVEHPVT EETAGIDLVR QQFRIANGEK LEFSEDPAPR GHAFEFRING EDAGRGFLPA
PGPISVYSEP SGPGVRVDSG VVQGDVIGGQ FDSMLAKLIV TGETREQALE RARRALDEFQ
VEGLATVLPF HRHIVSNPAF IGDGEKFDVY TKWIETDWVN PIEPYTGGQP IEDDDAAPRQ
KVVVEIGGRR VEVSLPGDLA LGGNGGGAGA GVIRKKPKAR TKKKGGGAAA SGDSVTAPMQ
GTVVKVAVEE GQEVAEGELV VVLEAMKMEN PVTAHKAGTV TGLSVEAGAA VTQGTVLLEI
K
//
