ID A0A2T0SFA9_9ACTN Unreviewed; 652 AA.
AC A0A2T0SFA9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=CLV70_102302 {ECO:0000313|EMBL:PRY32091.1};
OS Pseudosporangium ferrugineum.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Pseudosporangium.
OX NCBI_TaxID=439699 {ECO:0000313|EMBL:PRY32091.1, ECO:0000313|Proteomes:UP000239209};
RN [1] {ECO:0000313|EMBL:PRY32091.1, ECO:0000313|Proteomes:UP000239209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45348 {ECO:0000313|EMBL:PRY32091.1,
RC ECO:0000313|Proteomes:UP000239209};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-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:PRY32091.1}.
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DR EMBL; PVZG01000002; PRY32091.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0SFA9; -.
DR OrthoDB; 249215at2; -.
DR Proteomes; UP000239209; 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:UP000239209}.
FT DOMAIN 2..448
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 116..312
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 573..649
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 652 AA; 67897 MW; 996777279946CBDA CRC64;
MPFSSVLVAN RGEIARRVFA TCRRRGLATV AVFSDADAGS PHVREADSAV RLPGVTPADT
YLRADLLIDA ARRAGADAVH PGYGFLSENA GFARAVLGAG LTWIGPGPAA IEAMGSKVEA
KRRMAAAGVP VLAELDPAGV TEADLPVLVK ASAGGGGRGM RVVRELGELA GAVASASREA
ATAFGDPTVF CERYLESGHH VEVQILADGH GTVWALGERE CSLQRRHQKV IEEAPSPLVD
RIGGDLRTRL LAAGRDAAAA VGYLGAGTVE FLADGTGGFW FLEMNTRLQV EHPVTEAVTG
TDLVALQFDI AAGRPLSGPE PAMTGHSIEA RLYAESPADD WRPQTGTLVR FEVPGVAAEF
GRTGPDGLRL DSGVDDGSEV GPHYDAMLAK VVAYAHDRGA AAGQLAAALR RSRIHGVTTN
RDLLVATLEH PDFRAGTADT GFYAAHPPAG LIAAVAPDPE PAALVAALAD AAAERGPLLP
GVTSGFRNLP VGFRTRTYEV AGRELAVRYR FGHDGLEVDG RGAVSAVEVA GDAVVLELDG
VRRRWTVGRF ADRVVVDGPR GAVELRRVPR FTDPSAQLPA GALVAPMPGT VVRVEVTVGD
TVAAGQPLIR LEAMKMEHVV HAPAAGTVAE LPVAVGRQVA QDTTLVVLTA DG
//
