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Database: UniProt
Entry: B6HNN0_PENRW
LinkDB: B6HNN0_PENRW
Original site: B6HNN0_PENRW 
ID   B6HNN0_PENRW            Unreviewed;       800 AA.
AC   B6HNN0;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   SubName: Full=Pc21g09450 protein {ECO:0000313|EMBL:CAP95842.1};
GN   ORFNames=Pc21g09450 {ECO:0000313|EMBL:CAP95842.1}, PCH_Pc21g09450
GN   {ECO:0000313|EMBL:CAP95842.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP95842.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP95842.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; AM920436; CAP95842.1; -; Genomic_DNA.
DR   RefSeq; XP_002567984.1; XM_002567938.1.
DR   AlphaFoldDB; B6HNN0; -.
DR   STRING; 500485.B6HNN0; -.
DR   GeneID; 8304110; -.
DR   KEGG; pcs:Pc21g09450; -.
DR   VEuPathDB; FungiDB:PCH_Pc21g09450; -.
DR   eggNOG; KOG0238; Eukaryota.
DR   HOGENOM; CLU_000395_3_1_1; -.
DR   OMA; RDIRYET; -.
DR   OrthoDB; 1459320at2759; -.
DR   BioCyc; PCHR:PC21G09450-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c21.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; 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:UP000000724}.
FT   DOMAIN          36..493
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          157..357
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   800 AA;  87769 MW;  94919A0F65E00988 CRC64;
     MTMANTNKYE DTSNASPLRK PLFVAQPPLG SDGRQIIRKV LIANRGEIAC RIIKTCRVLN
     ILSVAVYVDE DASSRHVRDA DEAINIGSID RSERNPFLDI DLLIRTAVSA GAQAIHPGYG
     YLSENADFAN TVRKAGLIFV GPSASAMSTL GDKRSSKEYL RQQAPDVPLI PGFSGSSQDE
     DALKQAAQEI GFPVMLKASA GGGGKGMRIV REAGELKQEL ARAQSEAQRS FGSSDCILEK
     YIESSKHVEI QILGDSHGEV ISFFDRDCSV QRRHQKVIEE TPCTFLTDET RQNMSNTAVR
     IAKLIGYENA GTVEFIVDIK TNHFYFLEVN ARLQVEHPIT EEVTQVDLVA LQLFVAASGK
     LQSLPVVQNV TQKGHAIECR LCAEDPQKSF FPEHGKVHLW LPASGALGPG RDIRYETAIE
     TGSTVSIYFD SMIAKIVVWA PTRPLAVEKM AKVLAHTACV GVKTNQLFLQ ACLLNKAFYD
     PAYETSFIPT HIDELLQPYW SGDLQEVEKV LSVLPGLVVR KIPSFIPVGI QKKPFWGVRA
     QFRNQRMDPV SVHCDIVTTV DWPGKKQEDI DFATTMCIWK PQIKQSSSSE AEAYLIPVEK
     VGQSQEESAA AATQVSAQYN SISQALRSGK AMSSSPYRVS IDSWHPSQGN PAMVESWLAS
     TIQLSIDGTK FLAHVALPSA KPHALVGEID RGQRVFCHLP ALGTYVEFKR DTLLSFAESI
     RSVAKAKGGP EQRTIEAPMP CKVLSILKSN GEEVQSGESV MVIESMKMEV SIAVSVSGKF
     ETRWKQGDAV EEGKILCSVV
//
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