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
//