ID A0A0M2HAL9_9MICO Unreviewed; 588 AA.
AC A0A0M2HAL9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN Name=accC {ECO:0000313|EMBL:KJL41209.1};
GN ORFNames=RS82_03126 {ECO:0000313|EMBL:KJL41209.1};
OS Microbacterium trichothecenolyticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=69370 {ECO:0000313|EMBL:KJL41209.1, ECO:0000313|Proteomes:UP000034098};
RN [1] {ECO:0000313|EMBL:KJL41209.1, ECO:0000313|Proteomes:UP000034098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8608 {ECO:0000313|EMBL:KJL41209.1,
RC ECO:0000313|Proteomes:UP000034098};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) 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:KJL41209.1}.
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DR EMBL; JYJA01000038; KJL41209.1; -; Genomic_DNA.
DR RefSeq; WP_045300999.1; NZ_JYJA01000038.1.
DR AlphaFoldDB; A0A0M2HAL9; -.
DR PATRIC; fig|69370.6.peg.3182; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000034098; 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, ECO:0000313|EMBL:KJL41209.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000034098}.
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; 62318 MW; 0F046C07426E6DBD CRC64;
MPQIAKVLIA NRGEIAVRVI RAARDAGKAS VAVYADQDRD AMHARLADEA YALEGATSAE
TYLSIDKILS VARRSGADAV HPGYGFLAEN AEFARAVIAA GLVWIGPSPE AIEALGDKVT
ARAVAEKVGA PLAPGTPGPV AGADEVVAFA EEVGLPIAIK AAYGGGGRGL KVARTIDEVP
ELFESATREA ITAFGRGECF VEKYLDKPRH VETQCLADAA GNVVVISTRD CSLQRRHQKL
VEEAPAPFLS EEQNKTLYES SKAILKEVGY VGAGTCEFLI GADGTISFLE VNTRLQVEHP
VSEEVTGIDL VREQFRLAEG EELGYDDPKP EGHSIEFRIN GEDPGRGFLP QPGPIHVFKT
FGGPGIRLDS GVTAGDSVSG AFDSLLAKII VTGRDRAEAL ERSRRALDEF EVSGLPTVLP
FHRAVVRDPA FIAEDGRFGV FTRWIETEFV NDIAPWDGEL SEPTPAEARH TVVVEVAGRR
LEVSLPDRVV APVGVAGRPA AVPPSRRSHA PSVVAGASGD AVKSPMQATV VKVAVEEGQQ
VVKGDLVIVL EAMKMEQPIQ AHKDGVIGAI NADPGTTVSA GHQLLTIS
//
