ID A0A098YCT0_9ACTN Unreviewed; 664 AA.
AC A0A098YCT0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=IN07_03460 {ECO:0000313|EMBL:KGH48269.1};
OS Modestobacter caceresii.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=1522368 {ECO:0000313|EMBL:KGH48269.1, ECO:0000313|Proteomes:UP000029713};
RN [1] {ECO:0000313|EMBL:KGH48269.1, ECO:0000313|Proteomes:UP000029713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KNN45-2b {ECO:0000313|EMBL:KGH48269.1,
RC ECO:0000313|Proteomes:UP000029713};
RA Bukarasam K., Bull A., Girard G., van Wezel G., Goodfellow M.;
RT "Biosystematic studies on Modestobacter strains isolated from extreme
RT hyper-arid desert soil and from historic building.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KGH48269.1}.
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DR EMBL; JPMX01000009; KGH48269.1; -; Genomic_DNA.
DR RefSeq; WP_036333566.1; NZ_JPMX01000009.1.
DR AlphaFoldDB; A0A098YCT0; -.
DR STRING; 1522368.IN07_03460; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000029713; 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; 3.30.700.40; -; 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:UP000029713}.
FT DOMAIN 1..448
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 577..656
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 664 AA; 69450 MW; 49D9FEBDBD728BCA CRC64;
MFETVLVANR GEIAVRVIRT LRAMGIRSVA VHSEADAGAL HTRLADVAVP IGPAPAALSY
LSIERVLDAA RRTGAQAVHP GYGFLSENVD FARACEKAGI VFIGPPVAAI EAMGDKIRAK
QTVAAAGVPV VPGRTEPGMD DAAVARAAVE VGFPVLLKPS AGGGGKGMRV VRDPAELAEQ
IAGARREARS SFGDDTLLVE RYLGHSRHIE VQVFGDEHGT VVHLGERECS LQRRHQKVIE
EAPSPLLSPA QRQAMGAAAV EAARAVGYTG AGTVEFIVDA DSPQDFFFLE MNTRLQVEHP
VTECVTGLDL VELQLRVAAG GRLPIGQDDV RLTGHAIEAR VYAEDPARGF LPQAGEVVGL
VEPTGAGVRV DSSLRVGGVI GTDYDPMLAK VIAWGPDRET ARARLVTALG DTAVLGVATN
TGFLRDLLTD PDVVAGRLDT GLIERRGEAL TGARPIPPHV HAAAALALLA EVEPRGTAVD
PWADTSGWRL GEPAWTVRRL QAPGADPVTV RVRGRSTAAQ VRVGDGEPMT ARVDRDGDLL
GVTLDDVTTR YTVVHAGGTV WLAGDGHAVG LREHERLATA GTAAGSDGAV TAPMPGTVTV
VQVSLGDQVE AGTPLLVVEA MKMEHVLTAP LAGTVTELPV TAGQSVRLDE RVAVVTPPAP
GEEE
//
