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Reviewed, UniProtKB/Swiss-Prot Q91437 (PYR1_SQUAC)

Last modified June 16, 2009. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    CAD protein
Including the following 3 domains:
    1- Recommended name:
            Glutamine-dependent carbamoyl-phosphate synthase
              EC=6.3.5.5
    2- Recommended name:
            Aspartate carbamoyltransferase
              EC=2.1.3.2
    3- Recommended name:
            Dihydroorotase
              EC=3.5.2.3
Gene names
Name: CAD
OrganismSqualus acanthias (Spiny dogfish)
Taxonomic identifier7797 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Chondrichthyes › Elasmobranchii › Squalea › Hypnosqualea › Squaliformes › Squaloidei › Squalidae › Squalus

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Protein attributes

Sequence length2242 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).

Catalytic activity

2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.

Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate.

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate.

Cofactor

Binds 1 zinc ion per subunit (for dihydroorotase activity) Potential.

Enzyme regulation

Allosterically regulated and controlled by phosphorylation. 5-phosphoribose 1-diphosphate is an activator while UMP is an inhibitor of the CPSase reaction.

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.

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 3/6.

Subunit structure

Homohexamer.

Subcellular location

Cytoplasm.

Tissue specificity

Present in the testis but not in the liver.

Miscellaneous

GATase (glutamine amidotransferase) and CPSase (carbamoyl phosphate synthase) form together the glutamine-dependent CPSase (GD-CPSase) (EC 6.3.5.5).

Sequence similarities

In the central section; belongs to the DHOase family.

Contains 2 ATP-grasp domains.

Contains 1 glutamine amidotransferase type-1 domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 22422242CAD protein
PRO_0000199508

Regions

Domain177 – 363187Glutamine amidotransferase type-1
Domain522 – 714193ATP-grasp 1
Domain1057 – 1248192ATP-grasp 2
Region1 – 365365GATase (Glutamine amidotransferase)
Region366 – 39732Linker
Region398 – 14621065CPSase (Carbamoyl-phosphate synthase)
Region398 – 937540CPSase A
Region938 – 1462525CPSase B
Region1463 – 1796334DHOase (dihydroorotase)
Region1797 – 1934138Linker
Region1935 – 2242308ATCase (Aspartate transcarbamylase)

Sites

Active site2521For GATase activity By similarity
Active site3361For GATase activity By similarity
Active site3381For GATase activity By similarity
Metal binding14781Zinc Potential
Metal binding14801Zinc Potential

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Sequences

Sequence LengthMass (Da)Tools
Q91437-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 99F1986BA41244EA

FASTA2,242249,393
        10         20         30         40         50         60 
MATLFLDDGS SFKGRLFGAS STVSGEVVFQ TGMVGYPEAL TDPSYLSQIL VLTYPLIGNY 

        70         80         90        100        110        120 
GIPKDEEDEH GLSKWFESAK IHAAALVIGE NSQNPSHWSS VRSLDQRLKE HGIPALEGID 

       130        140        150        160        170        180 
TRSLTKKIRE KGTLLGKLVI DGTDENSLPY DDPNKRHLVK EVSIKEPKVY HPSGNVKIMA 

       190        200        210        220        230        240 
VDCGMKYNQI RSLCKRGAAV TVVPWDYLFD SNEFDGLFIS NGPGDPEYCQ QTINNVKKAI 

       250        260        270        280        290        300 
SEEKPKPLFG ICLGHQILSL AIGAKTYKMK YGNRGHNQPC IHEGTQRCFY TSQNHGFAVE 

       310        320        330        340        350        360 
PCSLPRDWSV LFTNANDQSN EGIIHNSKPL FSVQFHPEHK AGPTDLVDLF DIFLECARDV 

       370        380        390        400        410        420 
KLGVNLDKTV KGRVISHYSF KNGTENSKTP PGRIQPHKVL ILGSGGLSIG QAGEFDYSGS 

       430        440        450        460        470        480 
QAIKALKEEN VQSVLINPNI ATVQTSKGLA DKVYFLPITP EYVTQVIMNE RPDGILLTFG 

       490        500        510        520        530        540 
GQTALNCGVE LQKRGVLEKY HVRVLGTPVS SIEMTEDRKI FVEKMAEINE YVVPSEAAFT 

       550        560        570        580        590        600 
LEQAQGAAER LGYPVLVRAA FALGGLGSGF AQNKEELVTL VTQAFAHTSQ ILVDKSLKGW 

       610        620        630        640        650        660 
KEIEYEVVRD AYDNCITVCN MENVDPLGIH TGESIVVAPS QTLNDKEYNL LRTTAIKVIR 

       670        680        690        700        710        720 
HLGVVGECNI QYALSPESEQ YFIIEVNARL SRSSALASKA TGYPLAYVAA KLALGIPLPV 

       730        740        750        760        770        780 
LRNSVTNSTT ANYEPSLDYC VVKVPRWDLS KFLRLSTKIG SSMKSVGEVM AIGRNFEEAF 

       790        800        810        820        830        840 
QKALRMVDEN CVGFDHTLKP ASDEELETPT DKRIFVLAAA LRAGYEIDRL YELTKIDKWF 

       850        860        870        880        890        900 
LHKMKNIVEY SLKLSELYMK DEVPRHDLLK VKRLGFSDKQ IAMAIQSTEL AVRRLRQEWK 

       910        920        930        940        950        960 
ILPVVKQIDT VAAEWPAQTN YLYLTYNGEG HDLDFTKPHV MVIGSGVYRI GSSVEFDWCA 

       970        980        990       1000       1010       1020 
VRCIQQLRKM GYKTRMVNYN PETVSTDYDM CDRLYFDEIS FEVVMDIYEL ENPEGIILSM 

      1030       1040       1050       1060       1070       1080 
GGQLPNNIAM DLHRQQCRIL GTSPESIDTA ENRFKFSRML DTIGISQPRW KELSDTESSK 

      1090       1100       1110       1120       1130       1140 
QFCTKVGYPC LIRPSYVLSG VAMNVAYSDN DLEKFLSSAV AVSKEHPVVI SKFIQEAKEI 

      1150       1160       1170       1180       1190       1200 
DVDAVACDGV VIAVAISEHV ENAGVHSGDA TLVTPPQDLN QKTTERIKAI VHAIGQELQA 

      1210       1220       1230       1240       1250       1260 
TGPFNLQLIA KDDQLKVIEC NVRVSRSFPF VSKTLGVDMI ALATKVIMGE EVEPVGLMTG 

      1270       1280       1290       1300       1310       1320 
TGVVGVKVPQ FSFSRLAGAD VVLGVEMTST GEVACFGENR YEAYLKAMLS TGFKIPKKNI 

      1330       1340       1350       1360       1370       1380 
LLSIGSYKNK SELLSTVQSL EQLGYNLYAS LGTADFYTEH GVKIKAVDWP FEDTDNGCPL 

      1390       1400       1410       1420       1430       1440 
KERHRNIMDY LEENHFDLVI NLSMRNSGGR RLSSFVTKGY RTRRLAVDYS VPLIIDIKCT 

      1450       1460       1470       1480       1490       1500 
KLFVEALRLV GDTPPVKTHI DSMSSHKLIR LPGLIDVHVH LREPGGTHKE DFASGTAAAL 

      1510       1520       1530       1540       1550       1560 
AGGVTMVCAM PNTNPAITDQ TSFALVQKLA TAGARCDFAL FLGASSDNAD VLPLISNSAA 

      1570       1580       1590       1600       1610       1620 
GLKMYLNDTF STLKMDNVSL WMEHFEKWPK HLPIVVHAER QTVAAILMVA QLYQRPVHIC 

      1630       1640       1650       1660       1670       1680 
HVARKEEIQI IRAAKQKGVQ VTCEVAPHHL FLNEEDLESI GHGKGQVRPM LSTKEDVNAL 

      1690       1700       1710       1720       1730       1740 
WENLDVIDCF ATDHAPHSVE EKNSDSPPPG YPGLETMLPL LLTAVSEGRL TIDDLVKRLY 

      1750       1760       1770       1780       1790       1800 
ENPRKIFSLP VQENTYVEVD LEQEWIIPSY MQFTKSKWTP FEGKKVKGRV RRVVLRGEVA 

      1810       1820       1830       1840       1850       1860 
YIDGQVLVPP GYGQDVRAWP LGVPLPPPPT TVKTPEHSKP TQTETVRTRT ASPRRLASSG 

      1870       1880       1890       1900       1910       1920 
PAVDARFHLP PRIHRCSDPG LPNAEGEYKE KPVKKFIEQD TVSQDGYIYP PPVSRLLSPQ 

      1930       1940       1950       1960       1970       1980 
NLAAQAVPHP YSLLLHPFVG QHILSVKRFT KDQLSHLFNV AHNLRLTVQK DRSLDILKGK 

      1990       2000       2010       2020       2030       2040 
VMASMFYEVS TRTSSSFRAA MHRLGGSVIH FSEATSSVQK GESLLDSVQT MSCYVDVVVL 

      2050       2060       2070       2080       2090       2100 
RHPEPGAVEL AAKHSRKPII NAGDGVGEHP TQALLDIFTI REELGTVNGM TITMVGDLKH 

      2110       2120       2130       2140       2150       2160 
GRTVHSLAYL LTLYRVNLRY VTPRNLRMPP NIIRFLASRG IKQEEFDSLE EALPDTDVLY 

      2170       2180       2190       2200       2210       2220 
MTRIQKERFA SEEEYEACFG QFILTPHIMT KGKKKMVVMH PLPRVNEVSV EVDSDPRAAY 

      2230       2240 
FRQAENGMYV RMALLATVLG KF

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References

[1]"Nucleotide sequence and tissue-specific expression of the multifunctional protein carbamoyl-phosphate synthetase-aspartate transcarbamoylase-dihydroorotase (CAD) mRNA in Squalus acanthias."
Hong J., Salo W.L., Anderson P.M.
J. Biol. Chem. 270:14130-14139(1995) [PubMed: 7775474] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Spleen and Testis.

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Cross-references

Sequence databases

U18868 mRNA. Translation: AAA74569.1.
PIRA57541.

3D structure databases

HSSPHSSP built from PDB template 1ML4 based on UniProtKB P77918.
ModBaseSearch...

Phylogenomic databases

HOVERGENQ91437.

Enzyme and pathway databases

BRENDA2.1.3.2. 981.
3.5.2.3. 981.
6.3.5.5. 981.

Family and domain databases

InterProIPR006680. Amidohydro_1.
IPR006132. Asp/Orn_carbamoyltranf_P_bd.
IPR006130. Asp/Orn_carbamoylTrfase.
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.
IPR004722. DHOmult.
IPR002195. Dihydroorotase_CS.
IPR011702. GATASE.
IPR017926. GATASE_1.
IPR000991. GATase_class1_C.
IPR011607. MGS.
IPR013817. Pre-ATP_grasp.
[Graphical view]
Gene3DG3DSA:3.30.470.20. ATP_grasp_subdomain_2. 2 hits.
G3DSA:3.40.50.20. Pre-ATP_grasp. 2 hits.
PfamPF01979. Amidohydro_1. 1 hit.
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]
PRINTSPR00100. AOTCASE.
PR00101. ATCASE.
PR00098. CPSASE.
PR00099. CPSGATASE.
PR00096. GATASE.
TIGRFAMsTIGR00670. asp_carb_tr. 1 hit.
TIGR01369. CPSaseII_lrg. 1 hit.
TIGR01368. CPSaseIIsmall. 1 hit.
TIGR00857. pyrC_multi. 1 hit.
PROSITEPS50975. ATP_GRASP. 2 hits.
PS00097. CARBAMOYLTRANSFERASE. 1 hit.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
PS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePYR1_SQUAC
AccessionPrimary (citable) accession number: Q91437
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents