ID A0A495XL86_9PSEU Unreviewed; 588 AA.
AC A0A495XL86;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-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=DFJ66_5669 {ECO:0000313|EMBL:RKT72358.1};
OS Saccharothrix variisporea.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=543527 {ECO:0000313|EMBL:RKT72358.1, ECO:0000313|Proteomes:UP000272729};
RN [1] {ECO:0000313|EMBL:RKT72358.1, ECO:0000313|Proteomes:UP000272729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43911 {ECO:0000313|EMBL:RKT72358.1,
RC ECO:0000313|Proteomes:UP000272729};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-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:RKT72358.1}.
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DR EMBL; RBXR01000001; RKT72358.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495XL86; -.
DR OrthoDB; 4435847at2; -.
DR Proteomes; UP000272729; 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; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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:UP000272729}.
FT DOMAIN 2..446
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..318
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 511..587
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 493..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 62202 MW; 31C728DBA8DB9FF7 CRC64;
MSLRKVLVAN RGEIAVRVIR ACQDAGLASV AVYADPDRDA PFVRLADEAF ALGGSTPGDS
YLSVDKLLDV AKRSGADSVH PGYGFLSENA DFAQAVLDAG LIWIGPTPQA IRDLGDKVTA
RHIAMRAGAP LVPGTKDPVS GPDEVVAFAK EHGLPVAIKA AFGGGGRGLK VARTLEEIPE
LYDSAVREAV TAFGRGECFV ERYLDKPRHV EAQVLADQHG NVIVVGTRDC SLQRRHQKLV
EEAPAPFLTD EQRARIHTSA RAICKEAGYH GAGTVEYLVA QDGTISFLEV NTRLQVEHPV
SEETAGIDLV REQFRIAAGE PLRFTEDPTP RGHSIEFRIN GEDAGRNFLP APGTVTTFVA
PSGPGVRVDA GVESGTVIGG QFDSLLAKLI VTGEDRTQAL ERARRALDEM VVEGMATVLP
FHRRIVRDPA YVGTEDGFTV HTRWIETEFD NTIPPFTDGA EAEEDEPRQT LVVEVGGRRL
EVSLPGGLSA AAPVAKGGGA KAKPRKRAGG KGGAAASGDA VAAPMQGTIV KVAVEDGQQV
EAGDLIVVLE AMKMENPVTA HKAGVVTGLA AEPGATVTQG TVLCEIKE
//
