ID A0A429AIZ5_9ACTN Unreviewed; 583 AA.
AC A0A429AIZ5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JUN-2023, entry version 14.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=DMB42_40390 {ECO:0000313|EMBL:RSN00190.1};
OS Nonomuraea sp. WAC 01424.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=2203200 {ECO:0000313|EMBL:RSN00190.1, ECO:0000313|Proteomes:UP000286861};
RN [1] {ECO:0000313|EMBL:RSN00190.1, ECO:0000313|Proteomes:UP000286861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC 01424 {ECO:0000313|EMBL:RSN00190.1,
RC ECO:0000313|Proteomes:UP000286861};
RA Waglechner N., Wright G.D.;
RT "Evolution of GPA BGCs.";
RL Submitted (MAY-2018) 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:RSN00190.1}.
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DR EMBL; QHHZ01000018; RSN00190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A429AIZ5; -.
DR OrthoDB; 5166719at2; -.
DR Proteomes; UP000286861; 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; 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:UP000286861}.
FT DOMAIN 1..443
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 503..581
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 583 AA; 61384 MW; 30EBF59CBD9EB135 CRC64;
MRKVLIANRG EIAVRVARAC TDAGIGSVAV YADQDIDALH VRVADEAYAL GGQSPAETYL
DIAKLLDVAA RSGADAVHPG YGFLAENAAF AQAVIDAGLV WIGPPPAAIA ALGDKVQARH
IAQKVGAPLV AGTKDPVSGA EEVVAFAEQH GLPIAIKAAY GGGGRGIKVA RRLEEVAELY
ESAVREAVAA FGRGECFVER YLDRPRHVET QCLADHEGNV VVVSTRDCSL QRRHQKLVEE
APAPFLSQEQ IDLLYTSSKA ILKEAGYVGA GTCEFLVGQD GTISFLEVNT RLQVEHPVSE
EVAGIDLVRE MFRIADGELL GYDDPVLRGH SIEFRVNAED PGRNFLPAPG TLTAMRTPAG
PGVRLDSGYE AGMTVPQTFD SLVAKLIVTG RTRREALDRS RRALAEFEID GMPTVLPFHR
AIVTDPAFTS EPFAVHTRWI ETEWDNPVEP YAGEVATAPA APAVRETVTV EVGGKRIEVV
LPAGLGTAGP APAAGKAPRR AGGARKHAAA GGDALVSPMQ GTIVKVVAND GDVVSEGDTV
VVLEAMKMEQ PLTAHKSGTV TGLSAAVGQT VTSGATICEI KDA
//
