ID A0A0V8HVA6_9MICC Unreviewed; 678 AA.
AC A0A0V8HVA6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=AS038_10435 {ECO:0000313|EMBL:KSU66081.1};
OS Arthrobacter sp. NIO-1057.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=993071 {ECO:0000313|EMBL:KSU66081.1, ECO:0000313|Proteomes:UP000054434};
RN [1] {ECO:0000313|EMBL:KSU66081.1, ECO:0000313|Proteomes:UP000054434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIO-1057 {ECO:0000313|EMBL:KSU66081.1,
RC ECO:0000313|Proteomes:UP000054434};
RA Dastager S.G., Mawlankar R.B., Thorat M.N., Jiao J.-Y., Sonalkar V.,
RA Li W.-J.;
RT "Arthrobacter sp NIO-1057.";
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:KSU66081.1}.
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DR EMBL; LNQJ01000004; KSU66081.1; -; Genomic_DNA.
DR RefSeq; WP_058255864.1; NZ_KQ758456.1.
DR AlphaFoldDB; A0A0V8HVA6; -.
DR STRING; 993071.AS038_10435; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000054434; 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; 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; 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 5..460
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 124..333
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 590..667
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 678 AA; 73332 MW; 9060A820AE8D1AF3 CRC64;
MKRQLFDTVL VANRGEIAVR IIRTLRALGI KSVTVYSDAD ANALHVAQAD TAIRLGGATA
QESYLNIDAV INACKASGAQ AVHPGYGFLS ENVDFARALE SAGITFIGPP VNSINLMGDK
IRSKNHVQSH QVPVVPGIAE PSLSDEQLVV AAAQVGFPLL IKPSAGGGGK GMFAVETPEQ
LPEALASARR TARNAFGDDA LFLERLVRNP RHIEVQILAD AHGTTVHLGE RECSLQRRHQ
KVIEEAPAPL FENLDRGAQI RERIGAAAIA AAQSVGYVGA GTVEFLVSDE NPDEFFFMEM
NTRLQVEHPV TEEVVRVKGQ KLDLVDWQVR IAAGQPLDFA QDDVSLLGHA IEARLYAEDP
SANFLPSVGT ILQVHEPQSV RVDSSLREGL EISAHYDPML AKLIAWGPDR VSALNRLDHA
LAQSAVLGVL TNSEYLRLLL ADEEVAAGRL DTNLIERKMK QFSFRACGPR ELAVAAHLES
LRLPATTTPW GVRDGWRSRQ HRPLTTHFES GEAQIETSLL PTAQGSNVTV SGEQFHVQTL
DSGFEINGVR ASIQHAFAAD GTLWLNDQGW NAAVRKLTRE EVLERQLASI AKESGSYSPD
VLSPMPGTVI SVQVSDGQQV MTGQVLAIVE AMKMEHQSLA PADGIVRIQG LTAGDLVKAK
QVIATVEPLE VEAEEQPT
//
