ID A0A498C3K7_9MICO Unreviewed; 661 AA.
AC A0A498C3K7;
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=C7474_1717 {ECO:0000313|EMBL:RLK49557.1};
OS Microbacterium telephonicum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1714841 {ECO:0000313|EMBL:RLK49557.1, ECO:0000313|Proteomes:UP000273158};
RN [1] {ECO:0000313|EMBL:RLK49557.1, ECO:0000313|Proteomes:UP000273158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2T63 {ECO:0000313|EMBL:RLK49557.1,
RC ECO:0000313|Proteomes:UP000273158};
RX PubMed=26203337; DOI=.1186/s40793-015-0017-x;
RA Whitman W.B., Woyke T., Klenk H.P., Zhou Y., Lilburn T.G., Beck B.J.,
RA De Vos P., Vandamme P., Eisen J.A., Garrity G., Hugenholtz P.,
RA Kyrpides N.C.;
RT "Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III:
RT the genomes of soil and plant-associated and newly described type
RT strains.";
RL Stand. Genomic Sci. 10:26-26(2015).
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:RLK49557.1}.
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DR EMBL; RCDB01000002; RLK49557.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498C3K7; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000273158; 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; 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}; 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:UP000273158}.
FT DOMAIN 4..449
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 123..322
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 568..643
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 508..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 661 AA; 68557 MW; 8944E29E1BE429AE CRC64;
MTASLHTVLV ANRGEIARRV IRTVHRMGLR AVAVYSDADA DAPHVREADA AVRLGPASAA
RSYLDADAVL RAARESGADA VHPGYGFLSE NAAFARACAA AGIVFVGPGE EALAVMGDKI
HAKAHVAAHG VPTVPGFSAA GMDDDEIAAA ASRTGFPLLV KPSAGGGGKG MQVVRRADEL
PAALATARRI ARAAFGDDTL LLERLLERPR HIEVQVLADA HGTTLHLGER ECTLQRRHQK
VIEEAPSPIV DAALRERLGA AACRAAASVG YVGAGTVEFL VAAARPDEFF FIEMNTRLQV
EHPVTELVTG VDLVEQQLRI AAGEPLRIRQ DDVRLSGHAV EARVYAESPA TGFLPATGTV
RVWRAAPGVR TDAAVESGSV VTADYDPMIA KVIAHAPERE AALAALDRAL ADTVVLGVET
NIPFLRTLVQ DDDVVRGDLD TGLIERMPAP TVDAPTPTQL RLAAAALRAG GAPGGAAGGV
WPALAGRRFG RRDAVVAVHL EGADGHVHLV TSDDAPDPTP ASPDSDADTE AAAVVEDGVV
WVHADGATAS FVPLTRRAAW ECAHAARGRD AGAAAPELPA PMPGAVIAVH VADGDDVVAG
ERILTIEAMK MEHAVTAPHP GTVRLRVAAG AQVRRGDVVA VVDPTPTAPE TREPTASGGT
A
//
