Reviewed, UniProtKB/Swiss-Prot O93937 (PYR1_EMENI)

Names and origin

Protein names

Recommended name:
    Protein pyrABCN
Including the following 2 domains:
    1- Recommended name:
            Glutamine-dependent carbamoyl-phosphate
              EC=6.3.5.5
    2- Recommended name:
            Aspartate carbamoyltransferase
              EC=2.1.3.2

Gene names

Name:

pyrABCN

Organism

Emericella nidulans (Aspergillus nidulans)

Taxonomic identifier

162425 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	2275 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	This protein is a "fusion" protein encoding three enzymatic activities of the pyrimidine pathway (GATase, CPSase, and ATCase) By similarity.
Catalytic activity	2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate. Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate.
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 1/6. Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 2/6.
Domain	The DHOase domain is defective.
Miscellaneous	GATase (glutamine amidotransferase) and CPSase (carbamoyl phosphate synthase) form together the glutamine-dependent CPSase (GD-CPSase) (EC 6.3.5.5). In eukaryotes EC 6.3.5.5 is synthesized by two pathway-specific (arginine and pyrimidine) genes under separate control.
Sequence similarities	In the central section; belongs to the DHOase family. Contains 2 ATP-grasp domains. Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Domain	Repeat
Molecular function	Ligase Transferase
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	'de novo' pyrimidine base biosynthetic process Ref.1 Traceable author statement. Source: UniProtKB glutamine metabolic process Inferred from electronic annotation. Source: InterPro pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro amino acid binding Inferred from electronic annotation. Source: InterPro aspartate carbamoyltransferase activity Ref.1 Traceable author statement. Source: UniProtKB carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Ref.1 Traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2275	2275	Protein pyrABCN		PRO_0000199509
Regions
	Domain	265 – 453	189	Glutamine amidotransferase type-1
	Domain	604 – 796	193	ATP-grasp 1
	Domain	1139 – 1330	192	ATP-grasp 2
	Region	1 – 440	440	GATase (Glutamine amidotransferase) By similarity
	Region	441 – 482	42	Linker By similarity
	Region	483 – 1522	1040	CPSase (Carbamoyl-phosphate synthase) By similarity
	Region	1523 – 1532	10	Linker By similarity
	Region	1533 – 1862	330	Defective DHOase domain By similarity
	Region	1863 – 1953	91	Linker By similarity
	Region	1954 – 2258	305	ATCase (Aspartate transcarbamylase) By similarity
Sites
	Active site	342	1	For GATase activity By similarity
	Active site	426	1	For GATase activity By similarity
	Active site	428	1	For GATase activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	O93937-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 27BA9C1FA751436A	FASTA	2,275	249,741
	10 20 30 40 50 60 MPETVGHEEP ALPSSPQARG AVAYNAISKE LQPLPPTETA NGGIIPPASS RIEGSTGRLC 70 80 90 100 110 120 ALELEDGTVY QGYNFGAEKS VAGELVFQTG MVGYPESITD PSYRGQILVI TFPLVGNYGV 130 140 150 160 170 180 PSRETMDELL KTLPKHFEST EIHIAALVVA TYAGENYSHF LAESSLGQCV KEQGVPAIHG 190 200 210 220 230 240 VDTRALTKRI RQKGSMLGRL LLHKADVAET DAALAQDTWK SSFEQIDWVD PNTKNLVSEV 250 260 270 280 290 300 SIREPKLFSP PENVALKHPS SRPIRVLCLD VGLKFNQLRC LVARGVEVLV VPWDYDFPTL 310 320 330 340 350 360 AGKDYDGLFV SNGPGDPATM TTTVNNLAKT MQEARTPIFG ICLGHQLIAR SVGAQTLKMK 370 380 390 400 410 420 FGNRGHNIPC TSLVTGKCHI TSQNHGYAVD SSTLPSDWQE LFDNANDGSN EGIRHVSRPY 430 440 450 460 470 480 FSVQFHPEST PGPRDTEYLF DVFINAIKDT IASAEALQKP VNFPGGAVAE NIKASPRVSV 490 500 510 520 530 540 KKVLILGSGG LSIGQAGEFD YSGSQAIKAL KEEGIYTILI NPNIATIQTS KGLADKVYFL 550 560 570 580 590 600 PVNADFVRKV IKHERPDAIY VTFGGQTALQ VGIQLKDEFE SLGVKVLGTP IDTIITTEDR 610 620 630 640 650 660 ELFARSMDSI GEKCAKSASA SSLEEALQVV ESIGFPVIVR AAYALGGLGS GFADNLDELK 670 680 690 700 710 720 DLCAKAFAAS PQVLIERSMK GWKEIEYEVV RDARDNCITV CNMENFDPLG IHTGDSIVVA 730 740 750 760 770 780 PSQTLSDEDY NMLRTTAVNV IRHLGVVGEC NIQYALNPYS KEYCIIEVNA RLSRSSALAS 790 800 810 820 830 840 KATGYPLAFI AAKLGLNIPL NEIKNSVTKV TCACFEPSLD YCVVKIPRWD LKKFTRVSTQ 850 860 870 880 890 900 LGSSMKSVGE VMAIGRTFEE AIQKAIRSVD FHNLGFNETN ALMSIKTELQ TPSDQRLFAI 910 920 930 940 950 960 ANAMAAGYRL DDIWKLTNID KWFLTRLKGL SDFGKLMTNY NASTVTAPLL RQAKQLGFSD 970 980 990 1000 1010 1020 RQLAKFLSSN ELAIRRLRVE AGIIPIVKQI DTVAAEFPSV TNYLYLAYNA SEHDVRFDDN 1030 1040 1050 1060 1070 1080 GIMVLGSGVY RIGSSVEFDW CSVRTIRTLR EQGHKTVMVN YNPETVSTDY DEADRLYFEN 1090 1100 1110 1120 1130 1140 INLETVLDIY QLESSSGVIM SMGGQTPNNI ALPLHRLNVR ILGTSPEMID GAENRYKFSR 1150 1160 1170 1180 1190 1200 MLDRIGVDQP AWKELTSIEE AREFCDKVGY PVLVRPSYVL SGAAMNTVYS EHDLASYLNQ 1210 1220 1230 1240 1250 1260 AADVSREHPV VITKYIENAK EIEMDAVARN GVMVGHFISE HVENAGVHSG DATLILPPQD 1270 1280 1290 1300 1310 1320 LDPETVRRIE EATRKIGNAL NVTGPFNIQF IAKDNDIKVI ECNVRASRSF PFVSKVMGVD 1330 1340 1350 1360 1370 1380 LIEMATKAMI GAPFAEYPPV TIPKDYVGVK VPQFSFSRLA GADPVLGVEM ASTGEVASFG 1390 1400 1410 1420 1430 1440 RDKYEAYLKA LLSTGFKLPK RNILLSIGSY KEKMEMLPSI IKLRDVGFEL FATSGTADFL 1450 1460 1470 1480 1490 1500 KENGVPVKYL EILPGEDEDI KSEYSLTQHL ANNLIDLYIN LPSSNRFRRP ANYMSKGYRT 1510 1520 1530 1540 1550 1560 RRMAVDYQTP LVTNVKNAKI LIEAIARHYA LNVQTIDYQT SHRSIILPGL INVGAFVPGL 1570 1580 1590 1600 1610 1620 GSADSKDFEA VTKASIAAGF SMIRVMPVGV DSSITDARTL KLVQQNAGKA SFCDYNFSVV 1630 1640 1650 1660 1670 1680 ATSSNSAEVG QLTGEVGSLF IPFNHLSGNI SKVAAVTSHF GAWPSSKPII TDAKSTDLAS 1690 1700 1710 1720 1730 1740 VLLLASLHSR NIHVMSVTSK EDIGLIALSK EKGLKVTCDV SIYCLFLSRD DYPEAAFLPT 1750 1760 1770 1780 1790 1800 REDQKALWEH LSTIDIFSIG SIPYQLAGEK GSPAAGIAEA LPLLFTAVSE GRLTVEDIIA 1810 1820 1830 1840 1850 1860 RLYENPKKIF ELHDQSDSSV EVEIDRPYLF QSAQAWSPFS GKSVKGLVQR VIFQGKTSCL 1870 1880 1890 1900 1910 1920 DSEITPDAPK GSDMSGHRIV PASPSLKAMS PRVDGALDRR QSISIAGTPA RLGRKPVDHF 1930 1940 1950 1960 1970 1980 PAATGAELGP PLYTPVPRAS SPLLQMLSRS PFKQKHVLSV NQFNRADLHL LFTVAQEMRL 1990 2000 2010 2020 2030 2040 GVQREGVLDI LKGRLLCTLF YEPSTRTSAS FDVAMQRLGG RTIAISTEHS STKKGETLQD 2050 2060 2070 2080 2090 2100 TLRTLGCYGD AVVLRHPEPS STEVAAKFSP VPVINGGNGS VEHPTQAFLD LFTIREELGT 2110 2120 2130 2140 2150 2160 VGGLTITFTG DLKYGRPVHS LIKLLQFYDV RVQLVAPKDL SLPADIRQQL LATGQLLTES 2170 2180 2190 2200 2210 2220 EELTPEIVAR SDVLYSTRVQ KERFADLEQY ERLKNSFIID NALLKHAKSH MVVMHPLPRN 2230 2240 2250 2260 2270 AEVSEEVDFD QRAAYFRLVS LQSRGPSSEF DMLMWMQMRY GLYCRMALIE LIMAP

References

[1]

"Structural and transcriptional analysis of the pyrABCN, pyrD and pyrF genes in Aspergillus nidulans and the evolutionary origin of fungal dihydroorotases." Aleksenko A., Liu W., Gojkovic Z., Nielsen J., Piskur J. Mol. Microbiol. 33:599-611(1999) [PubMed: 10417650] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: FGSC 4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF112473 Genomic DNA. Translation: AAD09129.1.
3D structure databases
HSSP	HSSP built from PDB template 1M6V based on UniProtKB P00968.
ModBase	Search...
Family and domain databases
InterPro	IPR006220. Anth_synthII. IPR006130. Asp/Orn_carbamoyltranf. IPR006132. Asp/Orn_carbamoyltranf_P_bd. IPR006131. Asp_carbamoyltransf_Asp/Orn_bd. IPR002082. Aspartate_carbamoyltransf_euk. IPR011761. ATP-grasp. IPR013816. ATP_grasp_subdomain_2. IPR001317. CarbamoylP_synth_GATase. IPR005483. CarbamoylP_synth_lsu. IPR005479. CarbamoylP_synth_lsu_ATP-bd. IPR006275. CarbamoylP_synth_lsu_Gln-dep. IPR005481. CarbamoylP_synth_lsu_N. IPR005480. CarbamoylP_synth_lsu_oligo. IPR006274. CarbamoylP_synth_ssu. IPR002474. CarbamoylP_synth_ssu_N. IPR011702. GATASE. IPR012998. GATase_1_AS. IPR000991. GATase_class1_C. IPR011607. MGS. IPR013817. Pre-ATP_grasp. [Graphical view]
Gene3D	G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 2 hits. G3DSA:3.40.50.20. Pre-ATP_grasp. 2 hits.
Pfam	PF00289. CPSase_L_chain. 2 hits. PF02786. CPSase_L_D2. 2 hits. PF02787. CPSase_L_D3. 1 hit. PF00988. CPSase_sm_chain. 1 hit. PF00117. GATase. 1 hit. PF02142. MGS. 1 hit. PF00185. OTCace. 1 hit. PF02729. OTCace_N. 1 hit. [Graphical view]
PRINTS	PR00097. ANTSNTHASEII. PR00100. AOTCASE. PR00101. ATCASE. PR00098. CPSASE. PR00099. CPSGATASE. PR00096. GATASE.
TIGRFAMs	TIGR00670. asp_carb_tr. 1 hit. TIGR01369. CPSaseII_lrg. 1 hit. TIGR01368. CPSaseIIsmall. 1 hit.
PROSITE	PS50975. ATP_GRASP. 2 hits. PS00097. CARBAMOYLTRANSFERASE. 1 hit. PS00866. CPSASE_1. 2 hits. PS00867. CPSASE_2. 2 hits. PS51273. GATASE_TYPE_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYR1_EMENI

Accession

Primary (citable) accession number: O93937

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	May 1, 1999
Last modified:	November 25, 2008
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)