ID D9WIC7_9ACTN Unreviewed; 584 AA.
AC D9WIC7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=SSOG_05199 {ECO:0000313|EMBL:EFL25485.1};
OS Streptomyces himastatinicus ATCC 53653.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces violaceusniger group.
OX NCBI_TaxID=457427 {ECO:0000313|EMBL:EFL25485.1, ECO:0000313|Proteomes:UP000003963};
RN [1] {ECO:0000313|EMBL:EFL25485.1, ECO:0000313|Proteomes:UP000003963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53653 {ECO:0000313|EMBL:EFL25485.1,
RC ECO:0000313|Proteomes:UP000003963};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces hygroscopicus strain ATCC 53653.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; GG657754; EFL25485.1; -; Genomic_DNA.
DR RefSeq; WP_009717289.1; NZ_GG657754.1.
DR AlphaFoldDB; D9WIC7; -.
DR STRING; 457427.SSOG_05199; -.
DR HOGENOM; CLU_000395_3_1_11; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000003963; 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}.
FT DOMAIN 1..443
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 504..583
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 490..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 61066 MW; F1BBAA9193F8CB97 CRC64;
MRKVLIANRG EIAVRVARAC RDAGIASVAV YADPDRDAVH VRAADEAYAL GGDTPAASYL
DQAKVLAAAA ESGADAVHPG YGFLSENAEF AQAVLDAGLT WIGPPPQAIR DLGDKVAARH
IAQRAGAPLV AGTPDPVSGA DEVVAFAEQH GLPIAIKAAF GGGGRGLKVA RTMEEVPELY
DSAVREAVAA FGRGDCFVER YLDKPRHVET QCLADTHGNV VVVSTRDCSL QRRHQKLVEE
APAPFLTEEQ NADLYRASKA ILKEAGYVGA GTVEFLVGLD GTISFLEVNT RLQVEHPVTE
EVTGIDLVRE MFRIADGEEL GYDDPQIRGH SFEFRINGED PGRNFLPAPG TVTTFAPPTG
PGVRLDAGVE SGSVIGPAWD SLLAKLIVTG ATRTQALQRA ARALAEFQVE GMATAIPFHR
AVVADPAFTS DPFAVHTRWI ETEFTNTIAP FAAAPAATDE DEAVGREIVV VEVGGKRLEV
SLPASLGVAS APAAGGSKKP KRKAVKKGGS AASGDALASP MQGTIVKVAV AEGDTVAEGD
LVVVLEAMKM EQPLNAHRAG TIKGLSAEVG GSITSGSVIC EIKD
//
