ID A0A0M8Y7I3_9ACTN Unreviewed; 585 AA.
AC A0A0M8Y7I3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, 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=ADL05_05090 {ECO:0000313|EMBL:KOX20897.1};
OS Nocardiopsis sp. NRRL B-16309.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=1519494 {ECO:0000313|EMBL:KOX20897.1, ECO:0000313|Proteomes:UP000037694};
RN [1] {ECO:0000313|Proteomes:UP000037694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16309 {ECO:0000313|Proteomes:UP000037694};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-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:KOX20897.1}.
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DR EMBL; LGEC01000027; KOX20897.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8Y7I3; -.
DR STRING; 1519494.ADL05_05090; -.
DR PATRIC; fig|1519494.3.peg.1098; -.
DR Proteomes; UP000037694; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000037694}.
FT DOMAIN 1..439
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 115..312
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 507..583
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 486..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 585 AA; 60984 MW; 6A936AB8F4DA1833 CRC64;
MIANRGEIAV RIARACRDAG LGSVAVYAEP DLDALHAKVA DEAHALGGAT PADSYLDIAK
LLAVAAESGA DAVHPGYGFL AENADFAQAV IDAGLTWIGP PPSAITALGD KVQARHIAQR
VGAPLVAGTP DPVESAEEVV AFAREHGLPL AIKAAFGGGG RGLKVAHTLD QVPDAYESAV
REAVTAFGRG ECFVERYLDR PRHVETQCLA DTHGNVVVVS TRDCSLQRRH QKLVEEAPAP
FLTPEQNEQL YAASKAILAE AGYVGAGTCE FLVGADGTIS FLEVNTRLQV EHPVTEEVTG
VDLVREMFRV ADGQELGFDD PPARGHSFEF RINAEDAGRG FMPAPGTITK LSLPGGPGVR
VDTGCEAGFT VPQAFDSMVA KLIVTGRTRA EALERSRRAL AEFTVGGMPT VIPFHQAVVS
DPAFAPADPE REFGVYTRWI ETEFDNTIEP WTGTPGEAGA AERETVTVEV GGRRLDVVLP
AGLGAAAAAP AESGGERRKR ASRKGGGGAA AVSGDALVSP MQGTVVKLVA EEGAQVSEGD
TVVVIEAMKM EQPLTAHKAG TVSGLKVAAG ETIGNGAVVC EIKDA
//