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
//