ID A0A076MYV0_AMYME Unreviewed; 653 AA.
AC A0A076MYV0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, 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=AMETH_5736 {ECO:0000313|EMBL:AIJ25828.1};
OS Amycolatopsis methanolica 239.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis; Amycolatopsis methanolica group.
OX NCBI_TaxID=1068978 {ECO:0000313|EMBL:AIJ25828.1, ECO:0000313|Proteomes:UP000062973};
RN [1] {ECO:0000313|EMBL:AIJ25828.1, ECO:0000313|Proteomes:UP000062973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=239 {ECO:0000313|EMBL:AIJ25828.1,
RC ECO:0000313|Proteomes:UP000062973};
RA Tang B.;
RT "Whole Genome Sequence of the Amycolatopsis methanolica 239.";
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};
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DR EMBL; CP009110; AIJ25828.1; -; Genomic_DNA.
DR RefSeq; WP_017984664.1; NZ_CP009110.1.
DR AlphaFoldDB; A0A076MYV0; -.
DR STRING; 1068978.AMETH_5736; -.
DR KEGG; amq:AMETH_5736; -.
DR PATRIC; fig|1068978.7.peg.6161; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_1_11; -.
DR OrthoDB; 4435847at2; -.
DR Proteomes; UP000062973; 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 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; 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; 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000062973}.
FT DOMAIN 1..444
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 115..315
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 572..650
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 653 AA; 69328 MW; 5491060C6B7D8D23 CRC64;
MFDTVLIANR GEIAVRVIST LRRLGIRSVA VYSDADADAR HVHEADTAIR IGPAEATRSY
LSIPDIVRAA VDSGAQAVHP GYGFLAENAE FAAECEKAGL VFIGPPVSAI DAMGDKIRAK
ATVSAAGVPV VPGLSDVDDF AKAADEVGYP LLLKPSAGGG GKGMRLVTEP GELAAAVESA
QREARSAFGD DRLLLERFVT TPRHIEIQVL ADTHGTVLHL GERECSLQRR HQKIVEEAPS
VLLDEETRAR MGAAAVEAAR SVGYVGAGTV EFIVSARKPD EFFFMEMNTR LQVEHPVTEM
VTGLDLVEWQ VRVAAGEPLS LTQDDIRLTG HAVEARVYAE DPARGFVPTG GTVLALDEPR
GQGVRVDSSL TEGSVVGSNY DPMLAKVIAW GPDRASALHR LDRALAGTSV LGVPTNVTFL
RALLADPDVQ AGRLDTGLVE RRMDELVESA VPAEFFVAAA MDRLLGLVPE DTSDPWAVPS
GWRLGGPGGV TFRLRAGDAE ALVTIEGSPD AAQVTVDGGE PIPVSARRNG NRLEVHYDGE
FRRYLRADAP QDRVWLGRDG HGVVVGERPN LLATHGDASE AGPVVSPMPG TVLVVKVAQG
DVVSAGAPLL VVEAMKMEHT LVAPVDGVVE ELRVQVGQQV ALDETLAVVK EQK
//
