ID A0A0F0L5N4_9MICO Unreviewed; 651 AA.
AC A0A0F0L5N4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN Name=accA1 {ECO:0000313|EMBL:KJL27994.1};
GN ORFNames=RS83_03056 {ECO:0000313|EMBL:KJL27994.1};
OS Microbacterium oxydans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=82380 {ECO:0000313|EMBL:KJL27994.1, ECO:0000313|Proteomes:UP000033640};
RN [1] {ECO:0000313|EMBL:KJL27994.1, ECO:0000313|Proteomes:UP000033640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BEL4b {ECO:0000313|EMBL:KJL27994.1,
RC ECO:0000313|Proteomes:UP000033640};
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:KJL27994.1}.
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DR EMBL; JYIW01000026; KJL27994.1; -; Genomic_DNA.
DR RefSeq; WP_045280325.1; NZ_JYIW01000026.1.
DR AlphaFoldDB; A0A0F0L5N4; -.
DR PATRIC; fig|82380.11.peg.3090; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000033640; 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}.
FT DOMAIN 18..460
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 137..336
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 571..645
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 651 AA; 68263 MW; B534FEDB1F08AEB6 CRC64;
MTDQTLTEAA PASDVGPEFD TVLVANRGEI ARRVIRTLRR RGIRSVAVYS DADADAPHVR
EADVAVRIGP APAAESYLDI EAVIAAAMRT GAQAIHPGYG FLSESVGLAQ ACAEQGIVFI
GPGAEALQIM GDKARAREHV VAHGVPVVPG FDAAGLSESQ IADAAAEIGF PLLVKPSAGG
GGKGMEVVTD AAGLSTALAS ARRVAASAFG DDSLILERLI RRPRHIEVQV FGDAHGTVIA
LGERECTLQR RHQKVIEEAP SAGIPERTRT QLLDAAVRAA ESVSYVGAGT VEFLIDADDP
DEVFFIEMNT RLQVEHPVTE EVTGLDLVAL QLRVAAGRAL DVTPAVHGHA VEARIYAESP
ERGFLPSTGT ILLFDAPAGV RVDAAIETGS NVTGFYDPMI AKVIAFADDR ATALARLDLA
LSRTVVLGVD TNIAFLRLLC RDARVVSGDL DTGLIETLLP FDAATPTDDM VAAAARAHVA
RSAPLRSDAL WRELPGWRLG AAGVPDAAGA FLTDADEVVT AVRDGESGAC AIRTAVDADG
AVWVSAEGTS ARLRPVDRRE RMLRRLRAAD AGTGAATPEG RAPMPGAVVA VHVADGATVT
AGTPLLSIEA MKMEHPVLAP LDGTVHLLVT VGDQVRRDQL VARVTTMEEN R
//
