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Database: UniProt
Entry: S0DPB2_GIBF5
LinkDB: S0DPB2_GIBF5
Original site: S0DPB2_GIBF5 
ID   S0DPB2_GIBF5            Unreviewed;      2240 AA.
AC   S0DPB2;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   13-SEP-2023, entry version 46.
DE   SubName: Full=Probable URA2-multifunctional pyrimidine biosynthesis protein {ECO:0000313|EMBL:CCT64276.1};
GN   ORFNames=FFUJ_04517 {ECO:0000313|EMBL:CCT64276.1};
OS   Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS   and foot rot disease fungus) (Fusarium fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT64276.1, ECO:0000313|Proteomes:UP000016800};
RN   [1] {ECO:0000313|EMBL:CCT64276.1, ECO:0000313|Proteomes:UP000016800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC   {ECO:0000313|Proteomes:UP000016800};
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA   Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA   Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA   Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA   Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA   Tudzynski B.;
RT   "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT   Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT   novel metabolites.";
RL   PLoS Pathog. 9:E1003475-E1003475(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC         carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:456216; EC=6.3.5.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00001777};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-
CC         aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58228; EC=2.1.3.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001363};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00004812}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 2/3.
CC       {ECO:0000256|ARBA:ARBA00004852}.
CC   -!- SIMILARITY: In the central section; belongs to the metallo-dependent
CC       hydrolases superfamily. DHOase family. CAD subfamily.
CC       {ECO:0000256|ARBA:ARBA00008454}.
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DR   EMBL; HF679024; CCT64276.1; -; Genomic_DNA.
DR   STRING; 1279085.S0DPB2; -.
DR   EnsemblFungi; CCT64276; CCT64276; FFUJ_04517.
DR   VEuPathDB; FungiDB:FFUJ_04517; -.
DR   HOGENOM; CLU_000513_2_1_1; -.
DR   OrthoDB; 309at2759; -.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000016800; Chromosome 2.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01744; GATase1_CPSase; 1.
DR   CDD; cd01423; MGS_CPS_I_III; 1.
DR   Gene3D; 3.40.50.20; -; 2.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR   Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR   Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR   HAMAP; MF_00001; Asp_carb_tr; 1.
DR   HAMAP; MF_01209; CPSase_S_chain; 1.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR   InterPro; IPR002082; Asp_carbamoyltransf.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR006275; CarbamoylP_synth_lsu.
DR   InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR   InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR   InterPro; IPR006274; CarbamoylP_synth_ssu.
DR   InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR   InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR035686; CPSase_GATase1.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR036914; MGS-like_dom_sf.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   NCBIfam; TIGR00670; asp_carb_tr; 1.
DR   NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR   NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR   PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR   PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR   Pfam; PF02786; CPSase_L_D2; 2.
DR   Pfam; PF02787; CPSase_L_D3; 1.
DR   Pfam; PF00988; CPSase_sm_chain; 1.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF02142; MGS; 1.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00101; ATCASE.
DR   PRINTS; PR00098; CPSASE.
DR   PRINTS; PR00099; CPSGATASE.
DR   SMART; SM01096; CPSase_L_D3; 1.
DR   SMART; SM01097; CPSase_sm_chain; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
DR   SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR   SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
DR   PROSITE; PS00866; CPSASE_1; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS51855; MGS; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016800};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          570..762
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1107..1298
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1364..1512
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
FT   ACT_SITE        308
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        392
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        394
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   2240 AA;  246495 MW;  15FE107F56E335D3 CRC64;
     MALVSQPPAS ARQIGAEDDG LVCLELEDGS SFQGYSFGAQ KSIAGELVFQ TGMVGYPESV
     TDPSYRGQIL VITFPLVGNY GVPSREAMDE LLGDLPAHFE SSEIHIAGLV TASYAGEDFS
     HFLAKSSLGT WLKEQGVPAM YGVDTRSLTK RIREKGSMLG KMRLETRGLT NGSANGQADD
     ALAALPTDNF EQVEWVNPNT KNLVAEVSIK APKLYKPPTS VARKHPSGRT IRVLCLDVGM
     KFNQLRCFLK RGVEVLVCPW DYDIASAIDE FDGLFLSNGP GDPAMLDNVV KNIAAVLEKN
     EIPVFGICLG HQLLARAAGA TTKKMKFGNR GHNIPCTSMV TGKCHITSQN HGFAVDTDSL
     TNGWKELFVN ANDGSNEGIF HTEKPYFSVQ FHPESTPGPR DTEFLFDVFI NTMANCAEKP
     ELLKAPVSFP GGTIEENERL HPRVSVRKVL VLGSGGLSIG QAGEFDYSGS QAIKALKEEG
     IYTVLINPNI ATIQTSKGLA DKVYFLPVNA DFVRKVIQYE RPDAIYVTFG GQTALQVGIQ
     LKDEFESLGV KVLGTPIDTI ITTEDRELFA RSMDSIGEKC AKSASANNID EAMHVVKDIG
     FPVIVRAAYA LGGLGSGFAN NEEELMELCN KAFAASPQVL IERSMKGWKE IEYEVVRDAQ
     DNCITVCNME NFDPLGIHTG DSIVVAPSQT LSDEDYNMLR TTAVNVIRHL GVVGECNIQY
     ALNPFSREYC IIEVNARLSR SSALASKATG YPLAFIAAKL GLGIPLKEIK NSVTKSTCAC
     FEPSLDYVVV KMPRWDLKKF TRVSTQLGSS MKSVGEVMSI GRSFEEAIQK AIRAIDFHNL
     GFNETEALMS IEDELQTPSD QRLFAIANAM HEGYTVDKIW ELTKIDKWFL RKLKGLSDFA
     KRMACYSTTD IITSPSILLQ AKRLGFSDRQ LAKFWSSNEI AVRRLRLEAG IQPFVKQIDT
     VAAEFPAFTN YLYMTYNASD HDVNFDDHGV MVLGSGVYRI GSSVEFDWCS VRAIRTLRAT
     GFKTIMVNYN PETVSTDYDE ADKLYFENIN LETVLDIYQL ENSSGVLGAM GGQTPNNIAL
     PLHRAGVKVL GTSPEMIDNA ENRYKFSRML DRIEVDQPTW KELTSFAEAQ EFCNAVSYPV
     LVRPSYVLSG AAMNTVYSEK DLKNYLDQAA EVSREHPVVI TKYIENAKEI EMDAVAKDGK
     VIGHFISEHV ENAGVHSGDA TLILPPQDLE ATTIERIEEA TRKIGQALNV TGPFNIQFIA
     KDNDIKVIEC NVRASRSFPF VSKVMGVDLI EMATKAIMGQ PFQAYPPTDL APNCVGVKVP
     QFSFSRLSGA DPVLGVEMAS TGEVACFGVD KNEAYLKALM STGFKIPKKN ILLSIGSYKD
     KREMLPSVQK LEKLGYKLFA TSGTADFLQE HGVQCQYLEV LGKEEDRSSE FSLTQHLAKN
     TIDLYINLPS NNKYRRPANY MSKGYQTRRM AVDYQIPLVT NVKNAKILVE AIARHFELEV
     SKRDYQTSHR TIVLPGLINI AAFVPGIATA SNDDLQTVTK ASISAGFSMI RVMPLGVDGA
     ITDALTLKTA QLNSRRGGYC DYNFSVAATS DNADQISHVT GEVGSLFIPF NHLSGNISKV
     AAVTAHFDSW PTHKPIVTDA KLTDLASILL LASLHNRRIH VTSVTNKDDI KLIALSKAKG
     LQVTCDVSIY SLYLSRDEYP ECERLPTVAD QKALWQHMST IDVFSIGSLP YRLATSLGHK
     GDPHMGISDA LPLLLTSVAE GRLTVDDIKD RLYTNPMEIF ELHDQSGTTI EAEIDRPYTV
     APGTFWSPFV GRTMRGSVQR VTFQNTTVCL DGEVLPVSPQ GKDMSSHIAP PMSPPVKPTT
     SIAQATDSPQ ARRMSMLGGF QPLNRLRGVD TGAVGATLPS PARGAAPFEE LAPGLQLQPL
     VSSSLQQLLA QPSSFKNTHV LSVKSYSRAD LHLLFTVAQE MRLGVQREGV LNILRGRVLT
     TLFYEPSTRT SASFDAAMQR LGGRTIAIST SHSSVQKGET LQDTLRTLAC YGDAVVLRHP
     EETSVHVAEK YSPVPVINGG NGSKEHPTQA FLDLFTIREE LGTVQGLTIT FLGDLLYGRP
     VHSLVYLLRH YHVQVQLVAP KALALPPKVR EQLVASGQLL CESETLTPEI LARSDVLYCT
     RVQRERFPTE EEYQRVKNSY RVDNASLKHA KSSSIVMHPL PRNEEVAEEV DFDQRAAYFR
     QMRYGLYCRM ALLALVMADS
//
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