ID A0A369JNW4_HYPMA Unreviewed; 2239 AA.
AC A0A369JNW4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Protein pyrABCN {ECO:0000313|EMBL:RDB22075.1};
GN Name=pyrABCN {ECO:0000313|EMBL:RDB22075.1};
GN ORFNames=Hypma_010892 {ECO:0000313|EMBL:RDB22075.1};
OS Hypsizygus marmoreus (White beech mushroom) (Agaricus marmoreus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae; Hypsizygus.
OX NCBI_TaxID=39966 {ECO:0000313|EMBL:RDB22075.1, ECO:0000313|Proteomes:UP000076154};
RN [1] {ECO:0000313|EMBL:RDB22075.1, ECO:0000313|Proteomes:UP000076154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=51987-8 {ECO:0000313|EMBL:RDB22075.1,
RC ECO:0000313|Proteomes:UP000076154};
RA Choi I.-G., Min B., Kim J.-G., Kim S., Oh Y.-L., Kong W.-S., Park H.,
RA Jeong J., Song E.-S.;
RT "Whole genome sequencing of Hypsizygus marmoreus.";
RL Submitted (APR-2018) 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}.
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:RDB22075.1}.
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DR EMBL; LUEZ02000053; RDB22075.1; -; Genomic_DNA.
DR STRING; 39966.A0A369JNW4; -.
DR InParanoid; A0A369JNW4; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000076154; 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:UP000076154};
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 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 336
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 420
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 422
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2239 AA; 244649 MW; 5F41E2583D95E915 CRC64;
MTLPTLSSHI SPVRPGLSRT SSTFANLPAP PVTAAPVHAD GTEHLDGILE LADGSAFRGI
SFGGEGKSIA GECVFQTGMV GYTESLTDPS YEGQILVLTY PLIGNYGVPE RPTSLDTLPA
AFESSRIHVA ALVVGYYSED YSHFLAQSSL GTWLRENGIP ALFGVDTRAL TKKIREKGSM
LGKVLARHPN GFSITPHPMT ASLSLSSSPP TPYAWREDYV DTPFVDINQK NLVAAVSITS
PRLFKPEGTT KVHPSGRPLR VLAVDVGMKY NQIRCFTRRG VELKVVPWNY DFISDPEPYD
GLFISNGPGD PTMVKETITR LTKAMAQADK PIFGICLGHQ LMALAAGATT SKMKYGNRGH
NIPCTDILSG RCYITSQNHG YQVNTSSLSA GWKELFQNAN DGSNEGIYCE DKPFFSVQFH
PESTPGPRDT EFLFDVFLQN VADCATIGSL VPISMPGGKK EENASRVPRA NVSKVIILGS
GGLSIGQAGE FDYSGSQAIK ALKEEGIYTI MVNPNIATIA TSKGLADKVY FLPVTPEFVR
KIIKYEKPDG IYVTFGGQTA LNVGIKLKDE FADLGVQVLG TPVDTIITTE DRQLFASAME
EIGEKCAESF TATNPEDAVI AARTIGFPVI IRAAYALGGL GSGFAQDEAQ LRALCSKAFA
TSPQVLVEKS MKGWKEIEYE VVRDCRDNCI TVCNMENFDP LGIHTGDSIV VAPSQTLSDE
DYNMLRTTAI NVIRHLGVIG ECNIQYALNP TSQEYCIIEV NARLSRSSAL ASKATGYPLA
FIAAKLGLGI PLNEIKNSVT KVTSACFEPS LDYVVVKIPR WDLKKFSRVS PLLSSSMKSV
GEVMSIGRTF EETFQKAIRA IDDQFAGFAK NDFVENIDEE LLNPTDKRIF AISTAFHRGY
SVDKIWKMTS IDKWFLTKLE YIFKMEKRLS LCNVSSISSE LLRQAKQLGF SDRQLANCIG
STELAVRRLR QESGIAPFVK QIDTVAAEFP AFTNYLYTTY NAIEHDVEFN DRGVMVLGSG
VYRIGSSVEF DWCAVRAIRT LRDQGLQTIM VNYNPETVST DYDEADRLYF ENISLETILD
IYDTEHSRGV ILAMGGQTPN NIALPLFRQN VKIYGTSPEM IDTAENRYKF SRLLDAIGVD
QPLWKELTSF EEATAFCNKV GYPVLVRPSY VLSGAAMNVV STGDDLENYL TQATAVSRDH
PVVITKYIEQ AKEIEMDAVA KDGKMVMHYI SEHVENAGVH SGDATLIHPP QDLDPQTVRQ
IEEATAKIGN ALNVTGPFNI QFIAKNNEIK VIECNLRAAR SFPFVSKVTG IDAIEMATKV
MLDLPFEAYP DPGLPADYVG VKVPQFSFSR LSGADPVLGV EMASTGEVAC FGHDKYEAYL
KALISTGIIP PKKNILFSIG SYREKLELLP SVQKLSAAGY NIFATSGTAD FLTEHNVPCK
YLETLGEDSR EKQKSEYSLT QHLANNLIDM YINLPSKNHY RRPASYASKG YHTRRMAVDF
AVPLITNVKN AKMLAEALVR KLPLDVSIID SKSSHRTHSF PGLINIAAFV PGLTAQDQSG
VVAATEAAIS AGFTTSLIIP WGDNGRIVDR ASLEQAQANT AGAARCNFAL SITGTTTNAQ
GFDEELLAEA KSLFIPFYAG YSPLPLPVVA AHFTSWPVDK PIVTDAKGSD LASVLLLASL
HSRSVHVTDI QTNDDLLLIS LSKAKQLKVT CDVSVYSLFF TREQFPASLS LPTAADQTAL
WKNLNLIDAF SVGPTPYRLA KETGKPTSPA SGIEETLPLL LTAVADGRLT LEDIRLRLHD
NPVLIFGLPE QANTNVEVVI GRRAPFARCS TCWSPLERNI VAGALHRVVI HGNTAFLDGS
LFPAPTGRDI SGSSVSHAPP SILGARPGTP IIKEAEPSTH APVMSLTAPG ALQSLAASHG
PSAAPLYTHL VPHPTFHRRH ILSVKQFTQR DMYDLFSLAD EMRLQVERSG TLDILKAKVL
CTLFYEPSTR TSSSFNAAMK RCGGQVVQVT ADSSSVLKGE TLPDTIRTLA CYGDAIVIRH
PDVGSAQLAA KYSPVPIINA GDGIGEHPTQ ALLDIYTIRS ELGTVNGRTI TLLGDLKNGR
TVHSLVTLLC LYSVRLNFVS PASLAMPSSV VTAARKAGIP VTICESLDEV LAETDVLYVT
RVQKERFTNE TEWQQVKDAY RVDHAVLSRA KEDMIVMHPL PRVNEIDPEV DFDLRRAVYF
RQMRYGLFIR MALLTSVML
//
