ID A0A1I6KWF4_9MICO Unreviewed; 588 AA.
AC A0A1I6KWF4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Acetyl-CoA/propionyl-CoA carboxylase, biotin carboxylase, biotin carboxyl carrier protein {ECO:0000313|EMBL:SFR95555.1};
GN ORFNames=SAMN04487846_1193 {ECO:0000313|EMBL:SFR95555.1};
OS Microbacterium sp. cf046.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1761803 {ECO:0000313|EMBL:SFR95555.1, ECO:0000313|Proteomes:UP000199422};
RN [1] {ECO:0000313|EMBL:SFR95555.1, ECO:0000313|Proteomes:UP000199422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF046 {ECO:0000313|EMBL:SFR95555.1,
RC ECO:0000313|Proteomes:UP000199422};
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; FOZJ01000001; SFR95555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6KWF4; -.
DR STRING; 1761803.SAMN04487846_1193; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000199422; 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:SF126; BIOTIN CARBOXYLASE; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 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:UP000199422}.
FT DOMAIN 3..446
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 122..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 512..588
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 588 AA; 62456 MW; 009237A479865EF4 CRC64;
MPQIAKVLVA NRGEIAVRVI RAARDAGKSS VAVYADQDRD ALHARLADES YALEGATSAD
TYLSIEKILS VARRSGADAV HPGYGFLAEN AVFARAVMDA GLIWIGPSPE AIEALGDKVT
ARHVAERVGA PLAPGTPGPV ADASEVVAFA EEFGLPIAIK AAYGGGGRGL KVAREYDEIT
EMFESATREA ITAFGRGECF VEKYLDKPRH VETQCLADAA GNVVVVSTRD CSLQRRHQKL
VEEAPAPFLS EEQNRTLYEA SKAILREVGY VGAGTCEFLI GADGTISFLE VNTRLQVEHP
VSEEITGVDL VREQFRLAEG GTLDYPDPVP VGHSIEFRVN GEDPGRGFLP QPGPIHVFKT
FGGPGIRLDS GVTAGDSVSG AFDSLLGKII ITGRDRAEAL ERARRALDEF EVAGLPTVLP
FHRKVVRDPA FTAEDGVFGV FTRWIETEFV NDIPPWDGEL EAPKPAEARH TVVVEVGGKR
LEVSLPDRIV AAPGATARPA AVPPSRRSHA PTVVAGASGD AVKSPMQATI VKVAVEDGQQ
VVKGDLVVVL EAMKMEQPIQ AHKDGVIGAI NATAGTTVSA GHQLLTIS
//
