PYR1_EMENI
ID PYR1_EMENI Reviewed; 2275 AA.
AC O93937; C8VSK1; Q5BFW5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Protein pyrABCN;
DE Includes:
DE RecName: Full=Glutamine-dependent carbamoyl-phosphate;
DE EC=6.3.5.5;
DE Includes:
DE RecName: Full=Aspartate carbamoyltransferase;
DE EC=2.1.3.2;
GN Name=pyrABCN {ECO:0000312|EMBL:AAD09129.1}; ORFNames=AN0565;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1] {ECO:0000312|EMBL:AAD09129.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=10417650; DOI=10.1046/j.1365-2958.1999.01507.x;
RA Aleksenko A., Liu W., Gojkovic Z., Nielsen J., Piskur J.;
RT "Structural and transcriptional analysis of the pyrABCN, pyrD and pyrF
RT genes in Aspergillus nidulans and the evolutionary origin of fungal
RT dihydroorotases.";
RL Mol. Microbiol. 33:599-611(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: This protein is a 'fusion' protein encoding three enzymatic
CC activities of the pyrimidine pathway (GATase, CPSase, and ATCase).
CC {ECO:0000250|UniProtKB:P07259}.
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 -!- 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; Evidence={ECO:0000305};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 2/3.
CC -!- DOMAIN: The DHOase domain is defective.
CC -!- MISCELLANEOUS: GATase (glutamine amidotransferase) and CPSase
CC (carbamoyl phosphate synthase) form together the glutamine-dependent
CC CPSase (GD-CPSase) (EC 6.3.5.5). {ECO:0000305}.
CC -!- MISCELLANEOUS: In eukaryotes EC 6.3.5.5 is synthesized by two pathway-
CC specific (arginine and pyrimidine) genes under separate control.
CC -!- SIMILARITY: In the central section; belongs to the metallo-dependent
CC hydrolases superfamily. DHOase family. CAD subfamily. {ECO:0000305}.
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DR EMBL; AF112473; AAD09129.1; -; Genomic_DNA.
DR EMBL; AACD01000007; EAA66664.1; -; Genomic_DNA.
DR EMBL; BN001308; CBF89223.1; -; Genomic_DNA.
DR RefSeq; XP_658169.1; XM_653077.1.
DR AlphaFoldDB; O93937; -.
DR SMR; O93937; -.
DR STRING; 162425.CADANIAP00002113; -.
DR MEROPS; C26.956; -.
DR PRIDE; O93937; -.
DR EnsemblFungi; CBF89223; CBF89223; ANIA_00565.
DR EnsemblFungi; EAA66664; EAA66664; AN0565.2.
DR GeneID; 2876339; -.
DR KEGG; ani:AN0565.2; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_2_1_1; -.
DR InParanoid; O93937; -.
DR OMA; IPCTSML; -.
DR OrthoDB; 273358at2759; -.
DR UniPathway; UPA00070; UER00115.
DR UniPathway; UPA00070; UER00116.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; TAS:UniProtKB.
DR GO; GO:0004151; F:dihydroorotase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IDA:UniProtKB.
DR GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IDA:UniProtKB.
DR GO; GO:0006228; P:UTP biosynthetic process; IBA:GO_Central.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 1.10.1030.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.1370; -; 2.
DR Gene3D; 3.40.50.1380; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.50.30.20; -; 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 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; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF48108; SSF48108; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR SUPFAM; SSF52021; SSF52021; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52335; SSF52335; 1.
DR SUPFAM; SSF52440; SSF52440; 2.
DR SUPFAM; SSF53671; SSF53671; 1.
DR TIGRFAMs; TIGR00670; asp_carb_tr; 1.
DR TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
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; Ligase; Multifunctional enzyme; Nucleotide-binding;
KW Pyrimidine biosynthesis; Reference proteome; Repeat; Transferase.
FT CHAIN 1..2275
FT /note="Protein pyrABCN"
FT /id="PRO_0000199509"
FT DOMAIN 265..453
FT /note="Glutamine amidotransferase type-1"
FT DOMAIN 604..796
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255"
FT DOMAIN 1139..1330
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255"
FT DOMAIN 1396..1575
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..440
FT /note="GATase (Glutamine amidotransferase)"
FT /evidence="ECO:0000250"
FT REGION 441..482
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 483..1522
FT /note="CPSase (Carbamoyl-phosphate synthase)"
FT /evidence="ECO:0000250"
FT REGION 1523..1532
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 1533..1862
FT /note="Defective DHOase domain"
FT /evidence="ECO:0000250"
FT REGION 1863..1953
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 1863..1882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1954..2258
FT /note="ATCase (Aspartate transcarbamylase)"
FT /evidence="ECO:0000250"
FT ACT_SITE 342
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 426
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 428
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT CONFLICT 19
FT /note="G -> R (in Ref. 1; AAD09129)"
FT /evidence="ECO:0000305"
FT CONFLICT 169..170
FT /note="WL -> CV (in Ref. 1; AAD09129)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="V -> D (in Ref. 1; AAD09129)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="P -> A (in Ref. 1; AAD09129)"
FT /evidence="ECO:0000305"
FT CONFLICT 909..910
FT /note="SV -> RL (in Ref. 1; AAD09129)"
FT /evidence="ECO:0000305"
FT CONFLICT 1007
FT /note="T -> A (in Ref. 1; AAD09129)"
FT /evidence="ECO:0000305"
FT CONFLICT 1741
FT /note="A -> R (in Ref. 1; AAD09129)"
FT /evidence="ECO:0000305"
FT CONFLICT 2013
FT /note="A -> V (in Ref. 1; AAD09129)"
FT /evidence="ECO:0000305"
FT CONFLICT 2238
FT /note="Q -> L (in Ref. 1; AAD09129)"
FT /evidence="ECO:0000305"
FT CONFLICT 2269..2270
FT /note="LA -> IE (in Ref. 1; AAD09129)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2275 AA; 249540 MW; 25F581F3A50BB5CC CRC64;
MPETVGHEEP ALPSSPQAGG AVAYNAISKE LQPLPPTETA NGGIIPPASS RIEGSTGRLC
ALELEDGTVY QGYNFGAEKS VAGELVFQTG MVGYPESITD PSYRGQILVI TFPLVGNYGV
PSRETMDELL KTLPKHFEST EIHIAALVVA TYAGENYSHF LAESSLGQWL KEQGVPAIHG
VDTRALTKRI RQKGSMLGRL LLHKADVAET DAALAQDTWK SSFEQIDWVD PNTKNLVSEV
SIREPKLFSP PENVALKHPS SRPIRVLCLD VGLKFNQLRC LVARGVEVLV VPWDYDFPTL
AGKDYDGLFV SNGPGDPATM TTTVNNLAKT MQEARTPIFG ICLGHQLIAR SVGAQTLKMK
FGNRGHNIPC TSLVTGKCHI TSQNHGYAVD SSTLPSDWQE LFVNANDGSN EGIRHVSRPY
FSVQFHPEST PGPRDTEYLF DVFINAIKDT IASPEALQKP VNFPGGAVAE NIKASPRVSV
KKVLILGSGG LSIGQAGEFD YSGSQAIKAL KEEGIYTILI NPNIATIQTS KGLADKVYFL
PVNADFVRKV IKHERPDAIY VTFGGQTALQ VGIQLKDEFE SLGVKVLGTP IDTIITTEDR
ELFARSMDSI GEKCAKSASA SSLEEALQVV ESIGFPVIVR AAYALGGLGS GFADNLDELK
DLCAKAFAAS PQVLIERSMK GWKEIEYEVV RDARDNCITV CNMENFDPLG IHTGDSIVVA
PSQTLSDEDY NMLRTTAVNV IRHLGVVGEC NIQYALNPYS KEYCIIEVNA RLSRSSALAS
KATGYPLAFI AAKLGLNIPL NEIKNSVTKV TCACFEPSLD YCVVKIPRWD LKKFTRVSTQ
LGSSMKSVGE VMAIGRTFEE AIQKAIRSVD FHNLGFNETN ALMSIKTELQ TPSDQRLFAI
ANAMAAGYSV DDIWKLTNID KWFLTRLKGL SDFGKLMTNY NASTVTAPLL RQAKQLGFSD
RQLAKFLSSN ELAIRRLRVE AGIIPIVKQI DTVAAEFPSV TNYLYLTYNA SEHDVRFDDN
GIMVLGSGVY RIGSSVEFDW CSVRTIRTLR EQGHKTVMVN YNPETVSTDY DEADRLYFEN
INLETVLDIY QLESSSGVIM SMGGQTPNNI ALPLHRLNVR ILGTSPEMID GAENRYKFSR
MLDRIGVDQP AWKELTSIEE AREFCDKVGY PVLVRPSYVL SGAAMNTVYS EHDLASYLNQ
AADVSREHPV VITKYIENAK EIEMDAVARN GVMVGHFISE HVENAGVHSG DATLILPPQD
LDPETVRRIE EATRKIGNAL NVTGPFNIQF IAKDNDIKVI ECNVRASRSF PFVSKVMGVD
LIEMATKAMI GAPFAEYPPV TIPKDYVGVK VPQFSFSRLA GADPVLGVEM ASTGEVASFG
RDKYEAYLKA LLSTGFKLPK RNILLSIGSY KEKMEMLPSI IKLRDVGFEL FATSGTADFL
KENGVPVKYL EILPGEDEDI KSEYSLTQHL ANNLIDLYIN LPSSNRFRRP ANYMSKGYRT
RRMAVDYQTP LVTNVKNAKI LIEAIARHYA LNVQTIDYQT SHRSIILPGL INVGAFVPGL
GSADSKDFEA VTKASIAAGF SMIRVMPVGV DSSITDARTL KLVQQNAGKA SFCDYNFSVV
ATSSNSAEVG QLTGEVGSLF IPFNHLSGNI SKVAAVTSHF GAWPSSKPII TDAKSTDLAS
VLLLASLHSR NIHVMSVTSK EDIGLIALSK EKGLKVTCDV SIYCLFLSRD DYPEAAFLPT
AEDQKALWEH LSTIDIFSIG SIPYQLAGEK GSPAAGIAEA LPLLFTAVSE GRLTVEDIIA
RLYENPKKIF ELHDQSDSSV EVEIDRPYLF QSAQAWSPFS GKSVKGLVQR VIFQGKTSCL
DSEITPDAPK GSDMSGHRIV PASPSLKAMS PRVDGALDRR QSISIAGTPA RLGRKPVDHF
PAATGAELGP PLYTPVPRAS SPLLQMLSRS PFKQKHVLSV NQFNRADLHL LFTVAQEMRL
GVQREGVLDI LKGRLLCTLF YEPSTRTSAS FDAAMQRLGG RTIAISTEHS STKKGETLQD
TLRTLGCYGD AVVLRHPEPS STEVAAKFSP VPVINGGNGS VEHPTQAFLD LFTIREELGT
VGGLTITFTG DLKYGRPVHS LIKLLQFYDV RVQLVAPKDL SLPADIRQQL LATGQLLTES
EELTPEIVAR SDVLYSTRVQ KERFADLEQY ERLKNSFIID NALLKHAKSH MVVMHPLPRN
AEVSEEVDFD QRAAYFRQVS LQSRGPSSEF DMLMWMQMRY GLYCRMALLA LIMAP
