ID M0QRU1_9ACTN Unreviewed; 699 AA.
AC M0QRU1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=GS4_34_00630 {ECO:0000313|EMBL:GAC70377.1};
OS Gordonia soli NBRC 108243.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1223545 {ECO:0000313|EMBL:GAC70377.1, ECO:0000313|Proteomes:UP000011666};
RN [1] {ECO:0000313|EMBL:GAC70377.1, ECO:0000313|Proteomes:UP000011666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108243 {ECO:0000313|EMBL:GAC70377.1,
RC ECO:0000313|Proteomes:UP000011666};
RA Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia soli NBRC 108243.";
RL Submitted (JAN-2013) 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:GAC70377.1}.
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DR EMBL; BANX01000034; GAC70377.1; -; Genomic_DNA.
DR RefSeq; WP_007624348.1; NZ_BANX01000034.1.
DR AlphaFoldDB; M0QRU1; -.
DR STRING; 1223545.GS4_34_00630; -.
DR eggNOG; COG4770; Bacteria.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000011666; 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; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; 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:UP000011666}.
FT DOMAIN 13..462
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 132..331
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 610..684
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 699 AA; 73628 MW; CE114C5A3746894D CRC64;
MTDNRTRESR TRIIRSVLVA NRGEIAVRVI TTLRRMGIRS IAVYSDADRD ARHVRAADVA
VRIGPAAATL SYLDIAAVVD AARRTGADAV HPGYGFLSEN QKFAAALAEA GIVFIGPPAS
AIATMGDKIT ARAAVGERDV PVVPGLSRPG LTDTDLVAAA PEIGFPVLIK PSAGGGGKGM
HRVADPADLA AALQRARREA ASAFGDDTLF LEHFVDTPRH IEVQVLADEH GNVIHLGERE
CSLQRRHQKV IEEAPSALLD PETRHRIGTA ACDAARSVGY TGAGTVEFIV SAHRPDEFFF
MEMNTRLQVE HPVTELVTGV DLVEQQIRVA RGEVLGIAQT DVTMTGHAVE ARVYAEDPAN
GFLPTGGTIV ALAEPAEGRG GVRVDSAMLD GLVVGSDYDP MLAKVIAHGA DRAEAIDRLD
RALADTRVLG VTTNIDFCRF VLARPEVTDA DLDTELLDRL VVDYVAPQPV PAAYALAALL
RLEPADDLWG SAVGWRVGDR APIVTRLAHP DGHVAVSAVV QPGTDGTVDA RAEVTADVTV
TRDGADADTG QREWRAVVAL RRDDATSASV TSVVDGVGEH WTAARSDGRW WIAGPQGTWV
FEQAHALVEG AEDEHAGDIV SPMPGTVVAV SAASGDPLTA GTAVVVVEAM KMEHALTAPF
DGTAEVQVAV GDKVGAGQVL AHIRPAEESG TTGAAEGDR
//
