ID A0A0Q8ADQ9_9MICO Unreviewed; 674 AA.
AC A0A0Q8ADQ9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=ASD56_10205 {ECO:0000313|EMBL:KQZ84343.1};
OS Microbacterium sp. Root166.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736478 {ECO:0000313|EMBL:KQZ84343.1, ECO:0000313|Proteomes:UP000051650};
RN [1] {ECO:0000313|Proteomes:UP000051650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root166 {ECO:0000313|Proteomes:UP000051650};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ84343.1, ECO:0000313|Proteomes:UP000051650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root166 {ECO:0000313|EMBL:KQZ84343.1,
RC ECO:0000313|Proteomes:UP000051650};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQZ84343.1}.
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DR EMBL; LMGL01000002; KQZ84343.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q8ADQ9; -.
DR STRING; 1736478.ASD56_10205; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000051650; 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:UP000051650}.
FT DOMAIN 6..451
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 125..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 587..660
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 674 AA; 70925 MW; 676476B390F4765B CRC64;
MTDIAPFSTV LVANRGEIAR RVIRTLRRLG IRSVAVYSDA DADAPHVREA DVAVRIGPAA
ASASYLSIDA VIAAARETGA EAIHPGYGFL SENVAFARAC AEAGVVFIGP GERALEVMGD
KIRSKEQVIA HGVPTVPGFS AAGMTDAEIA AAAASTGYPL LVKPSAGGGG KGMQVVRSES
ELPEALATAR RVAAAAFGDD TLLLERLIER PRHIEVQVLA DAHGAVIHLG ERECTLQRRH
QKVIEEAPSP VVDAATRARL GAAACAAAAS VEYRGAGTVE FLVAGDRPDE FFFIEMNTRL
QVEHPVTELV TGVDLVEQQL LVAAGRPLDL AQGDVRLDGH AIEARVYAES PERGFLPATG
TVAVWREARG VRTDAAVESG SVVSADYDPM IAKVIAHGAD RIEALERLDA ALAETVLLGL
DTNIGFLREL LADPGVREGA MDTGLIDRIP PFEAREPSPA ALRVAAMTAD IIERAADDSD
RRAGALWRRA SGWRAGSAAT VRSVAVETST GDVRQVVLPD GVGLPVVPVG RQGWRAAGSA
TDIPSGTVGA QDDDGWTWVH ADGATHRVRP LTRRQAMEKR LAERDRDAAA TDPELRAPMP
GAVVAVHVSD GATVAAGERI VTIEAMKMEH PVLAPHGGVV RLDVATGEQV RRDQVLAHVS
ASAEPAHEAS DSRS
//
