ID T5K3N3_9MICO Unreviewed; 643 AA.
AC T5K3N3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=L687_03045 {ECO:0000313|EMBL:EQM74446.1};
OS Microbacterium maritypicum MF109.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1333857 {ECO:0000313|EMBL:EQM74446.1, ECO:0000313|Proteomes:UP000016033};
RN [1] {ECO:0000313|EMBL:EQM74446.1, ECO:0000313|Proteomes:UP000016033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MF109 {ECO:0000313|EMBL:EQM74446.1,
RC ECO:0000313|Proteomes:UP000016033};
RX PubMed=24092793;
RA Chauhan A., Green S., Pathak A., Thomas J., Venkatramanan R.;
RT "Whole-genome sequences of five oyster-associated bacteria show potential
RT for crude oil hydrocarbon degradation.";
RL Genome Announc. 1:e00802-e00813(2013).
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:EQM74446.1}.
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DR EMBL; ATAO01000206; EQM74446.1; -; Genomic_DNA.
DR RefSeq; WP_021200542.1; NZ_ATAO01000206.1.
DR AlphaFoldDB; T5K3N3; -.
DR PATRIC; fig|1333857.3.peg.2596; -.
DR Proteomes; UP000016033; 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:UP000016033}.
FT DOMAIN 11..453
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 130..329
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 564..639
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 555..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 643 AA; 68420 MW; 0235C8741109D737 CRC64;
MTTTSSSNTV SFHTVLVANR GEIARRVIRT LRTLGIRSVA VYSDADVAAP HVREADVAVR
IGPAPAAESY LDIDAVIAAA RRSGAQAIHP GYGFLSESVG LAEACAESGI VFIGPSVEAL
QIMGDKARAR EHVLRFGVPV VPGFDAKGLS DVEIAEEAEN VGYPLLVKPS AGGGGKGMEV
VADSTGLRSA LASARRVAAA AFGDDALILE RLIRRPRHIE VQVFGDAHGT VIALGERECT
LQRRHQKVVE EAPSAGIPPH TRERLLAAAV LAAESVEYIG AGTVEFLIDA DAPDEVFFIE
MNTRLQVEHP VTEEVTGLDL VALQLRAADG LPLDVSPRLR GHAVEARVYA ESPERGFLPS
TGKVLLFEPP VGVRVDAAIE TGSEVTGFYD PMIAKVIAFA DDRATALARL DEALARTVVL
GVETNIAFLR TLCRDARVIA GDLDTGLIET LLPLDAQTPS TAQLAAAKDA ISELRAPVRT
SPLWRELPGW RLGAENTVVA PFVALTDDDE EVELHEAPSA RSRVSVRAAV DGDGAVWVAE
DGHTVRLRPL DRRQRMRRRL SAREAGSGAT EPEGRAPMPG SVVAVHAADG ERVSAGDPLV
SIEAMKMEHP VLAPHDGVVH LLVAVGDQVR RDQPVARVMT EES
//
