ID PYR1_EMENI Reviewed; 2275 AA. AC O93937; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 22-JUL-2008, entry version 51. 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; OS Emericella nidulans (Aspergillus nidulans). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Emericella. OX NCBI_TaxID=162425; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=FGSC 4; RX MEDLINE=99348390; PubMed=10417650; 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). CC -!- FUNCTION: This protein is a "fusion" protein encoding three CC enzymatic activities of the pyrimidine pathway (GATase, CPSase, CC and ATCase) (By similarity). CC -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 CC ADP + phosphate + L-glutamate + carbamoyl phosphate. CC -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-aspartate = phosphate CC + N-carbamoyl-L-aspartate. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; UMP from HCO(3)(-): step 1/6. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; UMP from HCO(3)(-): step 2/6. CC -!- DOMAIN: The DHOase domain is defective. CC -!- MISCELLANEOUS: GATase (glutamine amidotransferase) and CPSase CC (carbamoyl phosphate synthase) form together the glutamine- CC dependent CPSase (GD-CPSase) (EC 6.3.5.5). CC -!- MISCELLANEOUS: In eukaryotes EC 6.3.5.5 is synthesized by two CC pathway-specific (arginine and pyrimidine) genes under separate CC control. CC -!- SIMILARITY: In the central section; belongs to the DHOase family. CC -!- SIMILARITY: Contains 2 ATP-grasp domains. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF112473; AAD09129.1; -; Genomic_DNA. DR HSSP; P00968; 1M6V. DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; TAS:UniProtKB. DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hyd...; TAS:UniProtKB. DR GO; GO:0006207; P:'de novo' pyrimidine base biosynthetic process; TAS:UniProtKB. DR GO; GO:0006520; P:amino acid metabolic process; IDA:UniProtKB. DR InterPro; IPR006220; Anth_synthII. DR InterPro; IPR006130; Asp/Orn_carbamoyltranf. DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P_bd. DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn_bd. DR InterPro; IPR002082; Aspartate_carbamoyltransf_euk. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR001317; CarbamoylP_synth_GATase. DR InterPro; IPR005483; CarbamoylP_synth_lsu. DR InterPro; IPR005479; CarbamoylP_synth_lsu_ATP-bd. DR InterPro; IPR006275; CarbamoylP_synth_lsu_Gln-dep. DR InterPro; IPR005481; CarbamoylP_synth_lsu_N. DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo. DR InterPro; IPR006274; CarbamoylP_synth_ssu. DR InterPro; IPR002474; CarbamoylP_synth_ssu_N. DR InterPro; IPR011702; GATASE. DR InterPro; IPR012998; GATase_1_AS. DR InterPro; IPR000991; GATase_class1_C. DR InterPro; IPR011607; MGS. DR InterPro; IPR013817; Pre-ATP_grasp. DR Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 2. DR Gene3D; G3DSA:3.40.50.20; Pre-ATP_grasp; 2. DR Pfam; PF00289; CPSase_L_chain; 2. 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; PR00097; ANTSNTHASEII. DR PRINTS; PR00100; AOTCASE. DR PRINTS; PR00101; ATCASE. DR PRINTS; PR00098; CPSASE. DR PRINTS; PR00099; CPSGATASE. DR PRINTS; PR00096; GATASE. 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. PE 3: Inferred from homology; KW Ligase; Multifunctional enzyme; Pyrimidine biosynthesis; Repeat; KW Transferase. FT CHAIN 1 2275 Protein pyrABCN. FT /FTId=PRO_0000199509. FT DOMAIN 265 453 Glutamine amidotransferase type-1. FT DOMAIN 604 796 ATP-grasp 1. FT DOMAIN 1139 1330 ATP-grasp 2. FT REGION 1 440 GATase (Glutamine amidotransferase) (By FT similarity). FT REGION 441 482 Linker (By similarity). FT REGION 483 1522 CPSase (Carbamoyl-phosphate synthase) (By FT similarity). FT REGION 1523 1532 Linker (By similarity). FT REGION 1533 1862 Defective DHOase domain (By similarity). FT REGION 1863 1953 Linker (By similarity). FT REGION 1954 2258 ATCase (Aspartate transcarbamylase) (By FT similarity). FT ACT_SITE 342 342 For GATase activity (By similarity). FT ACT_SITE 426 426 For GATase activity (By similarity). FT ACT_SITE 428 428 For GATase activity (By similarity). SQ SEQUENCE 2275 AA; 249741 MW; 27BA9C1FA751436A CRC64; MPETVGHEEP ALPSSPQARG AVAYNAISKE LQPLPPTETA NGGIIPPASS RIEGSTGRLC ALELEDGTVY QGYNFGAEKS VAGELVFQTG MVGYPESITD PSYRGQILVI TFPLVGNYGV PSRETMDELL KTLPKHFEST EIHIAALVVA TYAGENYSHF LAESSLGQCV KEQGVPAIHG VDTRALTKRI RQKGSMLGRL LLHKADVAET DAALAQDTWK SSFEQIDWVD PNTKNLVSEV SIREPKLFSP PENVALKHPS SRPIRVLCLD VGLKFNQLRC LVARGVEVLV VPWDYDFPTL AGKDYDGLFV SNGPGDPATM TTTVNNLAKT MQEARTPIFG ICLGHQLIAR SVGAQTLKMK FGNRGHNIPC TSLVTGKCHI TSQNHGYAVD SSTLPSDWQE LFDNANDGSN EGIRHVSRPY FSVQFHPEST PGPRDTEYLF DVFINAIKDT IASAEALQKP 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 ANAMAAGYRL DDIWKLTNID KWFLTRLKGL SDFGKLMTNY NASTVTAPLL RQAKQLGFSD RQLAKFLSSN ELAIRRLRVE AGIIPIVKQI DTVAAEFPSV TNYLYLAYNA 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 REDQKALWEH 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 FDVAMQRLGG RTIAISTEHS STKKGETLQD TLRTLGCYGD AVVLRHPEPS STEVAAKFSP VPVINGGNGS VEHPTQAFLD LFTIREELGT VGGLTITFTG DLKYGRPVHS LIKLLQFYDV RVQLVAPKDL SLPADIRQQL LATGQLLTES EELTPEIVAR SDVLYSTRVQ KERFADLEQY ERLKNSFIID NALLKHAKSH MVVMHPLPRN AEVSEEVDFD QRAAYFRLVS LQSRGPSSEF DMLMWMQMRY GLYCRMALIE LIMAP //