ID E4ZRS4_LEPMJ Unreviewed; 1396 AA.
AC E4ZRS4;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=LEMA_P035950.1 {ECO:0000313|EMBL:CBX93921.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
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=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC ChEBI:CHEBI:456216; EC=6.3.4.16;
CC Evidence={ECO:0000256|ARBA:ARBA00043687};
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DR EMBL; FP929116; CBX93921.1; -; Genomic_DNA.
DR RefSeq; XP_003837361.1; XM_003837313.1.
DR STRING; 985895.E4ZRS4; -.
DR MEROPS; C26.956; -.
DR EnsemblFungi; CBX93921; CBX93921; LEMA_P035950.1.
DR GeneID; 13285318; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_0_1_1; -.
DR InParanoid; E4ZRS4; -.
DR OMA; YEVEYLY; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000002668; Genome.
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:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
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 HAMAP; MF_01209; CPSase_S_chain; 1.
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; IPR016185; PreATP-grasp_dom_sf.
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 PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00098; CPSASE.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM01097; CPSase_sm_chain; 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; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS51273; GATASE_TYPE_1; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 572..764
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 REGION 166..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 310
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 394
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 396
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1396 AA; 154177 MW; B4E9237887C44616 CRC64;
MAPHPDESQN LALELQDGYV CFGRSFGAEK SIAGELVFQT GMVGYPESIT DPSYRGQILV
ITFPLVGNYG VPSREDMDSL LQGVPAHFES SEIHIAGLVV ACYAEEEFSH HLATSSLGAW
LKEQGVPAIT GVDTRALTKR IREEGAMLGR LLQRTGPSPL RTIFSKITSG TETPDSREPT
EEDSEQWRSS FEQLEWSDPN TTNLVAEVSI KEPKLWSPDP ATALKHPSGR TLRVLTVDVG
LKYNQLRCLV RRGVEVLQVP WDYDFPQLAG KDYDGLFISN GPGNPAMMES TVKHIKSAME
EARTPIFGIC LGHQLLARAA GADTLKMKFG NRGANIPCTS LLTGKCHITS QNHGYAVDTK
TLKQGWEELF VNANDGSNEG IRHVQRPYFS VQFHPEHTPG PRDTEYLFDV FISTIQKAIK
APEIMQNPVE FPGGTIEENK KLSPRVDVKK VLVLGSGGLS IGQAGEFDYS GSQAIKALRE
EGIYTILINP NIATIQTSKG LADKVYFLPV NADFVRKVIQ KERPDGIYVT FGGQTALQVG
IQLKDEFEGL GVKVLGTPID TIITTEDREL FARSMESIGE KCAKSASASN VEEAMRAVKD
IGFPVIVRAA YALGGLGSGF AEDEAQLLDL CNKAFAASPQ VLIERSMKGW KEIEYEVVRD
ARDNCITVCN MENFDPLGIH TGDSIVVAPS QTLSDEDYNM LRTTAVNVIR HLGVVGECNI
QYALNPFSRE YCIIEVNARL SRSSALASKA TGYPLAFVAA KLGLNIPLNE ISNSVTRVTC
ACFEPSLDYV VVKIPRWDLK KFTRVSTLLG SSMKSVGEVM SIGRTFEEAI QKAIREIDPS
NLGFNETAAL MEIDQELQTP SDQRLFAIAN AMKSGYSVDK IWELTKIDKW FLSRLKALSN
FEKSMSSYDT NTITMPLLKQ AKALGYSDRQ LAKFWASNEL AVRRVRVDAG IFPVVKQIDT
VAAEFPAVTN YLYLTYNGTE HDITFNDHGV MVLGSGVYRI GSSVEFDWCS VRAIRTLREQ
GYKTVMLNYN PETVSTDYDE ADRLYFENIS LETVLDIYTL ESSSGVIISM GGQTPNNIAL
PLHRMNVKIL GTSPEMIDTA ENRYKFSRML DRISVDQPAW KELTSIEEAT EFCDRVSYPV
LVRPSYVLSG AAMNTVYSQH DLANYLNQAA DVSKEHPVVI TKYIENAKEI EMDAVARNGT
MIGHFISEHV ENAGVHSGDA TLILPPQDLD PETVRQIEDA TRKIGMALNI TGPYNIQFIA
KDNEIKVIEC NVRASRSFPF VSKVMGVDLI EMATKAMAGL PVVEYPPVNI PADYVGVKVP
QFSFSRLSGA DPVLGVEMAS TGEVACFGRT KYEAYIKGLI ATGLRLPKKN ILLNGRLHSR
TWHPSQVFGS SHKWRA
//
