ID A0A0C9T620_PLICR Unreviewed; 2249 AA.
AC A0A0C9T620;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KII84749.1};
GN ORFNames=PLICRDRAFT_45557 {ECO:0000313|EMBL:KII84749.1};
OS Plicaturopsis crispa FD-325 SS-3.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Amylocorticiales; Amylocorticiaceae; Plicaturopsis.
OX NCBI_TaxID=944288 {ECO:0000313|EMBL:KII84749.1, ECO:0000313|Proteomes:UP000053263};
RN [1] {ECO:0000313|EMBL:KII84749.1, ECO:0000313|Proteomes:UP000053263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-325 SS-3 {ECO:0000313|EMBL:KII84749.1,
RC ECO:0000313|Proteomes:UP000053263};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001062};
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 2nd section; belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00043998}.
CC -!- SIMILARITY: In the 3rd section; belongs to the metallo-dependent
CC hydrolases superfamily. DHOase family. CAD subfamily.
CC {ECO:0000256|ARBA:ARBA00043968}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
CC {ECO:0000256|ARBA:ARBA00043979}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CarA family.
CC {ECO:0000256|ARBA:ARBA00043984}.
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DR EMBL; KN832569; KII84749.1; -; Genomic_DNA.
DR HOGENOM; CLU_000513_2_1_1; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000053263; Unassembled WGS sequence.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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:UP000053263};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 596..788
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1131..1322
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1387..1544
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 189..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1877..1903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 335
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 419
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 421
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2249 AA; 245737 MW; E145FF5A5D02DC64 CRC64;
MTLPNGRPAL SRAPSNFLPA APATAHTFND ENGQNAKKDA VLELGDGSAF RGISFGAEGK
SVAGECVFQT GMVGYTESLT DPSYEGQILV LTYPLIGNYG VPARGETAID AIPLEFESSR
IHIAALVVGY YSEDYSHFLA SSSLGAWLKE NGIPAIYGVD TRALTKKIRE KGSMLGKILA
RKNEAPVGRP RSLLVESQPA SRAPSPPGAA GWREDYVDVP FRDPNQDNLV ASVSITSPRL
YKPTGTTKPL LHPSGRPLRV LAIDVGMKYN QIRCFTHRGI ELKVVPWDYD FLSEAEPYDG
LFLSNGPGDP TTLKSTIQRL ATAMEKGDRP IFGICLGHQL LALAAGASTR KMKYGNRGHN
IPCTDALSGR CYITSQNHGF EVDTTTLPSG WNELFRNAND GSNEGIYYEH KPYFSVQFHP
ESTPGPRDTE FLFDVFIQNV ADCANTGALS GPITMPGGKK ADNDQRVPRA NVQKVLILGS
GGLSIGQAGE FDYSGSQAIK ALKEEGIYTI FVNPNIATIA TSKGLADKVY FLPVTPDFVR
KIIKYEKPDG IYVSFGGQTA LTVGIKLKDE FAALGVQVLG TPIETVITTE DRQMFANAMA
EIGEKCAQSS TATTQEEAIA AATTIGFPVI VRAAYALGGL GSGFAQDEAQ LRALCSKAFA
TSPQVLVEKS MKGWKEIEYE VVRDCRDNCI TVCNMENFDP LGIHTGDSIV VAPSQTLSDA
DYNMLRTTAI NVIRHLGVVG ECNIQYALNP TSQEYCIIEV NARLSRSSAL ASKATGYPLA
FIAAKLGLGI PLNEIKNSVT KVTSACFEPS MDYCVVKIPR WDLKKFNRVS RLLSSSMKSV
GEVMSIGRTF EETIQKAIRA IDDQFTGFAS NDFVEDIDEE LVNPTDKRIF AISTAFSRGY
SVDKIWQMTN IDKWFLTKLQ YIFKMEQHIS TCNVGTIGAD VLRQAKQLGF SDRQLASGMG
STELAVRRLR QETGIAPFVK QIDTVAAEFP AFTNYLYTTY NAIEHDITFN DRGVMVLGSG
VYRIGSSVEF DWCAVRAIRT LREQGFQTIM VNYNPETVST DYDEADRLYF ENISLETILD
IYDTERSRGV ILSMGGQTPN NIALPLHRQN VKIYGTSPEM IDTAENRYKF SRLLDEIGVD
QPLWKELTSF EEAQSFCETV GYPVLVRPSY VLSGAAMNVV STGDDLSNYL TQATAVSRDH
PVVITKYIEQ AKEIEMDAVA KDGKMVMHYI SEHVENAGVH SGDATLIHPP QDLDPATVIQ
IEEATAKIGN ALNVTGPFNI QFIAKNNEIK VIECNLRAAR SFPFVSKVTG IDAIEMATKV
MLGLPIESYP DPGLPPDYVG VKVPQFSFSR LSGADPVLGV EMASTGEVAC FGTDKYEAYL
KGLIATGIIP PKKNILFSVG SYREKLEILQ SVQKLHAAGY NIFATSGTAD FFTEHNVPCK
YLETLPEDSR DEQKSEYSLT QHLANNLIDM YINLPSKNHY RRPASYTSKG YRTRRMAVDF
AVPLITNVKN AKLLAEALVR KLPLDVSAVD SKSSHRTHTF PGLINVAAFV PSLTVGDSDD
FAKTTKASIS AGFTTALFLP LGGADKIVDH LSLEHAHANA TGSAHCNYSF SITATDSNVA
TLDEEIQADT KSLFVPLQVD SVATQISTIA AHFAAWPANK PIVTDAKGSD LASILLLASL
NGRSVHVTDV RNKDDLLLIS LSKAKQLKVT CDVSVFALFF NQDQFPQSKS LPTAADQKTL
WKNLDVIDAF SVGATPYHLA LELEKSPTPW TGIEETLPLL LTAVTDGRLT LDDIRIRLHD
NPIRIFGLPD QVNTHVEVVV GRLGLFAKRN SCWSPLERSP VTGAIHRVVV HGHTVYLDGA
LSSSALGRDI SSATIAHGRT ERAGSVSSAA PRPDLTTPAQ RTSDASAQAN FMSLTSAGAS
QSITTGLHGS IPTPHVFTHL LPHPAFHRRH ILSVKQFTQR DMYDLFSLAH EMRLQVERNG
TLDILKGKVL CTLFYEPSTR TSSSFDAAMK RCGGEVVQVT ADNSSVLKGE SLPDTIRTLG
CYADAIVIRH PAVGSSQLAA KFSPVPIVNA GDGVGEHPTQ ALLDIYTIRS ELGTVNGRTI
TLLGDLKNGR TVHSLVTLLC LYSVRLNFVS PQSLAMPASV ITAARKAGVT VHQCESLDEV
LADTDVLYVT RIQKERFESE SEWAKVKDVY RIDHAVLSRA KEEMIVMHPL PRVNEIDPEV
DFDSRRAVYF RQMRYGLFIR MALLCSVMG
//
