ID A0A066YVM2_9ACTN Unreviewed; 767 AA.
AC A0A066YVM2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=KCH_28380 {ECO:0000313|EMBL:KDN85257.1};
OS Kitasatospora cheerisanensis KCTC 2395.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=1348663 {ECO:0000313|EMBL:KDN85257.1, ECO:0000313|Proteomes:UP000027178};
RN [1] {ECO:0000313|EMBL:KDN85257.1, ECO:0000313|Proteomes:UP000027178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2395 {ECO:0000313|EMBL:KDN85257.1,
RC ECO:0000313|Proteomes:UP000027178};
RA Nam D.H.;
RT "Draft Genome Sequence of Kitasatospora cheerisanensis KCTC 2395.";
RL Submitted (MAY-2014) 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:KDN85257.1}.
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DR EMBL; JNBY01000085; KDN85257.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066YVM2; -.
DR PATRIC; fig|1348663.4.peg.2735; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_1_11; -.
DR Proteomes; UP000027178; 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; 3.30.700.40; -; 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:UP000027178}.
FT DOMAIN 18..487
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 142..358
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 649..726
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 728..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 767 AA; 81377 MW; D13070E15FAB3AA0 CRC64;
MHRQLAHPFF SQRRHTSMFD TVLVANRGEI ALRVIRTLRR LGVRSVAVHS DADADAPHVR
AADLAVRLGP ADRSDSSAAE TYLRTDLILD AARRTGARAV HPGYGFLAEN PAFAEACNQA
GLVFIGPPPA AVELMGDKIN AKEAVRVAGV PVVPGSEDGS PSDEQLIEAA ARIGYPVLLK
PSAGGGGKGM RLVRDPAELP AELAAARRVA RTAFGDDTLL LERWVDQPRH IEVQVLADTH
GRTVHLGERE CSLQRRHQKL IEEAPSVLLN ARTRAAMGAA AVRAAEACGY TGAGTVEFIV
PGGDPAGPDA DDVLDFFFME MNTRLQVEHP VTELAVSVDG PEGPQRLDLV EWQLRVAAGE
ALSFTQSDIS FLGHAIEARI CAEDPERDFL PTGGQVLLLD EPSGEGIRVD SGIAPGERIG
SLYDPMLAKV IAYGPDRPTA IRRLRAALAE TRILGVTTNT GYLRRLLAQP EVTAGRLDTG
LVERSAQQDP SVLSSPYTRP ESIDLLHFAA ALVRQLELGP TDASDGWTDP FSLPSGWRLG
GETAWTTHRL RLAGREPVAV SCRMTTSGEF ESASGFSAAT TPEWEVRLDG GPIRRARASR
DGNLLRLAVD GLQATFTVAE ERTAEGITHW LGTDGDAWPV HPFDPIAERA AAGTVHHGTL
TAPMPGTVTV VKVEAGERVR RGQALLVLEA MKMEHVIAAP HDGTVEDLRV TAGATVAMDE
ALVAVAPDDE DAGAAAGTEA DSTAGGEAGA STEAAAGTTA KLSEAAR
//
