ID A0A429F2W4_9ACTN Unreviewed; 653 AA.
AC A0A429F2W4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JUN-2023, entry version 15.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=DMH08_25380 {ECO:0000313|EMBL:RSN55906.1};
OS Actinomadura sp. WAC 06369.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=2203193 {ECO:0000313|EMBL:RSN55906.1, ECO:0000313|Proteomes:UP000288610};
RN [1] {ECO:0000313|EMBL:RSN55906.1, ECO:0000313|Proteomes:UP000288610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC 06369 {ECO:0000313|EMBL:RSN55906.1,
RC ECO:0000313|Proteomes:UP000288610};
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:RSN55906.1}.
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DR EMBL; QHJN01000103; RSN55906.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A429F2W4; -.
DR Proteomes; UP000288610; 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:UP000288610}.
FT DOMAIN 1..444
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..308
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 574..649
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 653 AA; 68288 MW; 2F73020818DCD04D CRC64;
MIKRLLVANR GEIARRVMRA CRDLGVGTVA VFSDADADAP HVREADVAGR LPGAAPADTY
LSAERVLEAA RAAGADAVHP GYGFLSENAE FARAVAAAGL TWVGPPPAAI EAMGSKIEAK
KLMAAAGVPV LPELDPDRVT EDDLPLMVKA SAGGGGRGMR VVRARAELDG AVAAARREAE
SAFGDPAVFC EPLLEHARHI EVQILADAHG TVWALGEREC SVQRRHQKIV EEAPSSAVRP
GLRDELCRAA VDAARAIGYV GAGTVEFMLA PDGGFHFLEV NTRLQVEHPV TECVYGVDLV
RWQLAVAEGA RLPEAPPEPR GHAIEVRLYA EDPALDWRPA GGVLRTFEVP GVDAEFAVPA
SYGLRLDAGV ESGSAVGVHY DPMLAKLIAW GPSRDAAARR LAAALRGARI HGLTTNRDLL
VRILEDGAFL AGDTDTGYLE RVGLDVLAAP LADAAAVRVS ALAAALAGAA AERASARVQG
GLPSGWRNVR SRPQRRSFEG PGGTIDVDYH LGRDGLVCEA FPGTSVVSAA PHEVVLERGG
LRETFAVAAA DGEVFVDSRF GPVAFRAVPR FADPSDQIAP GSLLAPMPGT VVRVETERGA
RVAEGQALVV LEAMKMEHRI AAPAAGTVAE LNVGAGQQVE AGAVLAVIEG TSE
//
