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Database: UniProt
Entry: A0A2H3HZ76_FUSOX
LinkDB: A0A2H3HZ76_FUSOX
Original site: A0A2H3HZ76_FUSOX 
ID   A0A2H3HZ76_FUSOX        Unreviewed;      2240 AA.
AC   A0A2H3HZ76;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   13-SEP-2023, entry version 21.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PCD43763.1};
GN   ORFNames=AU210_002852 {ECO:0000313|EMBL:PCD43763.1};
OS   Fusarium oxysporum f. sp. radicis-cucumerinum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=327505 {ECO:0000313|EMBL:PCD43763.1, ECO:0000313|Proteomes:UP000219602};
RN   [1] {ECO:0000313|EMBL:PCD43763.1, ECO:0000313|Proteomes:UP000219602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Forc016 {ECO:0000313|EMBL:PCD43763.1,
RC   ECO:0000313|Proteomes:UP000219602};
RX   PubMed=27387256; DOI=10.1111/1462-2920.13445;
RA   van Dam P., Fokkens L., Schmidt S.M., Linmans J.H., Kistler H.C., Ma L.J.,
RA   Rep M.;
RT   "Effector profiles distinguish formae speciales of Fusarium oxysporum.";
RL   Environ. Microbiol. 18:4087-4102(2016).
RN   [2] {ECO:0000313|EMBL:PCD43763.1, ECO:0000313|Proteomes:UP000219602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Forc016 {ECO:0000313|EMBL:PCD43763.1,
RC   ECO:0000313|Proteomes:UP000219602};
RX   PubMed=28831051; DOI=10.1038/s41598-017-07995-y;
RA   van Dam P., Fokkens L., Ayukawa Y., van der Gragt M., Ter Horst A.,
RA   Brankovics B., Houterman P.M., Arie T., Rep M.;
RT   "A mobile pathogenicity chromosome in Fusarium oxysporum for infection of
RT   multiple cucurbit species.";
RL   Sci. Rep. 7:9042-9042(2017).
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}.
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:PCD43763.1}.
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DR   EMBL; MABQ02000002; PCD43763.1; -; Genomic_DNA.
DR   STRING; 327505.A0A2H3HZ76; -.
DR   OrthoDB; 309at2759; -.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000219602; 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:UP000219602};
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;  246536 MW;  36235938AE68F085 CRC64;
     MALVSQPPAS ARQIGAEDDG LVCLELEDGS SFQGYSFGAQ KSIAGELVFQ TGMVGYPESV
     TDPSYRGQIL VITFPLVGNY GVPSREAMDE LLGDLPAHFE SSEIHIAGLV TASYAGEDFS
     HFLAKSSLGT WLKEQGVPAM YGVDTRSLTK RIREKGSMLG KMRLETRGLT NGSVNSQADD
     ALAALPTDHF 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 NEEELMDLCN 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
     KRMTSYSTTD ITTSPSILLQ 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 TRKIGLALNV 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 SSISAGFSMI RVMPLGVDGA
     ITDALTLKTA QQNSRRGGYC DYNFSVAATS DNADQISHVT GEVGSLFIPF NHLSGNISKV
     AAVTAHFDSW PTHKPIVTDA KLTDLASILL LASLHNRRIH VTSVTNKDDI KLIALSKAKG
     LQVTCDVSIY SLYLSRDEYP ECERLPTAAD QKALWQHMST IDVFSIGSLP YRLATSLGHK
     GDPHMGISDV LPLLLTSVAE GRLTVDDIKD RLYTNPMEIF ELHDQSGTTI EAEIDRPYTV
     APGTFWSPFV GRTMRGSVQR VTFQNTTVCL DGEVLPVSPQ GKDMSSHIAP PMSPPVKPTT
     SIAQATDSPQ ARRMSMLGGF QPLNRLRGVD TGAVGATLPS PARGAAPVEE LAPGLQLQPL
     VSSSLQQLLA QPSSFKNTHV LSVKSYSRAD LHLLFTVAQE MRLGVQREGV LNILRGRVLT
     TLFYEPSTRT SASFDAAMQR LGGRTIAIST SHSSVQKGET LQDTLRTLAC YGDAVVLRHP
     EESSVHVAEK YSPVPVINGG NGSKEHPTQA FLDLFTIREE LGTVQGLTIT FLGDLLYGRP
     VHSLVYLLRH YHVQVQLVAP KALALPPKVR EQLVASGQLL CESETLTPEI MARSDVLYCT
     RVQRERFPTE EEYQRVKNSY RVDNASLKHA KSSSIVMHPL PRNEEVAEEV DFDQRAAYFR
     QMRYGLYCRM ALLALVMADS
//
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