ID A0A1H4PQG1_9MICO Unreviewed; 683 AA.
AC A0A1H4PQG1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=SAMN04489806_2582 {ECO:0000313|EMBL:SEC09605.1};
OS Microbacterium humi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=640635 {ECO:0000313|EMBL:SEC09605.1, ECO:0000313|Proteomes:UP000199183};
RN [1] {ECO:0000313|EMBL:SEC09605.1, ECO:0000313|Proteomes:UP000199183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21799 {ECO:0000313|EMBL:SEC09605.1,
RC ECO:0000313|Proteomes:UP000199183};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; FNRY01000001; SEC09605.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4PQG1; -.
DR STRING; 640635.SAMN04489806_2582; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000199183; 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; 3.30.700.40; -; 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; IPR048429; MCC_alpha_BT.
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 Pfam; PF21139; MCC_alpha_BT; 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:UP000199183}.
FT DOMAIN 1..444
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 576..649
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 648..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 683 AA; 72870 MW; BABED819BCFCA28E CRC64;
MFTTVLVANR GEIARRVIRT LRRMGIRSVA VYSDADAAEP HVREADVAVR LGPARPAESY
LNIARIVDAA VRAGAEAIHP GYGFLSENAA FAQAVSDAGL VFIGPGVEAL EVMGDKIRAK
QRVTRDGVPV IPGIAEPGLD DDALTAAAAQ IGYPVLIKPS AGGGGKGMLD VSDPSELPEA
LRAARRVAAT AFGDDTLFLE RLVTAPRHIE VQVLADEHGR VIHLGERECS LQRRHQKVIE
EAPSPLIDED TRERIGAAAC AVARSVDYRG AGTVEFLVSA EQPGEFFFME MNTRLQVEHP
VTELVTGIDI VEQQLRIAAG EPLAVEQEQI RLSGHAVEAR VYAEDDQFLP QAGRVLELRL
PDEVRVDSGI AGGSVIGGDY DPMLAKIIAH AGTREHAFAA LARALERTVV LGVTTNTRFL
HGLVTDPGVL SGDFDTTTID RRIAERAPAE VPETTWRAAA LALHADAWRS APTDSVWAAP
TGWRLGGAPR GIDYRLSCDG EERTLRVAGR PEAASVDSSP AACRAVDGAL LVHIDGLTTT
IEAARDDDVL WLHDGHGARA FRIIDRDAAT AHARGAADDA APELRSPMPG TVVAVAADDG
THVAEGDTIL VIEAMKMEHR ITAPRAGRVD LHVGHGQAVA RDAVVATVVP DDQETSDERG
RAEPGDHPAP TPHEGDQSEH RTR
//
