Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q91293 (CPSM_LITCT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carbamoyl-phosphate synthase [ammonia], mitochondrial

EC=6.3.4.16
Alternative name(s):
Carbamoyl-phosphate synthetase I
Short name=CPSase I
OrganismLithobates catesbeiana (American bullfrog) (Rana catesbeiana)
Taxonomic identifier8400 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaRanoideaRanidaeRanaAquarana

Protein attributes

Sequence length1496 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell By similarity. HAMAP-Rule MF_01209

Catalytic activity

2 ATP + NH3 + CO2 + H2O = 2 ADP + phosphate + carbamoyl phosphate. HAMAP-Rule MF_01209

Enzyme regulation

Requires N-acetyl-L-glutamate (NAG) as an allosteric activator By similarity. HAMAP-Rule MF_01209

Subcellular location

Mitochondrion HAMAP-Rule MF_01209.

Sequence similarities

Contains 2 ATP-grasp domains.

Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Keywords
   Biological processUrea cycle
   Cellular componentMitochondrion
   DomainRepeat
Transit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termAllosteric enzyme
Gene Ontology (GO)
   Biological_processcarbamoyl phosphate biosynthetic process

Inferred from electronic annotation. Source: InterPro

glutamine catabolic process

Inferred from electronic annotation. Source: InterPro

urea cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

carbamoyl-phosphate synthase (ammonia) activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3333Mitochondrion By similarity
Chain34 – 14961463Carbamoyl-phosphate synthase [ammonia], mitochondrial HAMAP-Rule MF_01209
PRO_0000029900

Regions

Domain215 – 401187Glutamine amidotransferase type-1
Domain548 – 740193ATP-grasp 1
Domain1090 – 1281192ATP-grasp 2
Region34 – 214181Anthranilate phosphoribosyltransferase homolog HAMAP-Rule MF_01209

Sites

Active site2901For GATase activity By similarity
Binding site13881Allosteric activator By similarity
Binding site13911Allosteric activator By similarity
Binding site14071Allosteric activator By similarity
Binding site14331Allosteric activator By similarity
Binding site14361Allosteric activator By similarity
Binding site14451Allosteric activator By similarity

Sequences

Sequence LengthMass (Da)Tools
Q91293 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 2360BF05D21B059E

FASTA1,496163,767
        10         20         30         40         50         60 
MTRILSVFKT AKTGVLNAAA HRYRGFSKAG VRLMSVKAQT ANLVLEDGTK IKGYSFGHPA 

        70         80         90        100        110        120 
SVAGEVIFNT GLGGYVEAVT DPSYHGQILT LTNPIIGNGG APDTKARDAY GLMKYIESEN 

       130        140        150        160        170        180 
IQASGLLVLD YSHEYSHWGA VKSLSEWLHE EKVPALCGID TRMLAKKIRD NKGAVLGKIE 

       190        200        210        220        230        240 
FEGQPVEFID PNKRNLIAEV STKETKVFGK GNPVRIVAVD CGVKHNIIRQ LVKRGAEVHL 

       250        260        270        280        290        300 
VPWNHDFSQM EYDGLLITSG PGNPELAKPL IQNLKKVFQS DRPEPIFGIC KGNEIAALAA 

       310        320        330        340        350        360 
GGKTYRLPMA NRGQNQPVMI TLNGQAFITA QNHAYAVDNN SLPAGWKPLF VNINDQSNEG 

       370        380        390        400        410        420 
IMHETKPIFT SQFHPEANPG PVDTEFLFDV YMSLIKKGKG TTLTSVMPKP ALQSKRIDVA 

       430        440        450        460        470        480 
KVLILGSGGL SIGQAGEFDY SGSQAVKAMK EENVKTVLMN PNIASVQTNE VGLKQADTVY 

       490        500        510        520        530        540 
FLPITPQFVT EVIKAEKTDG IILGMGGQTA LNCGVELFKR GVLKEYGVRV LGTSVESIMF 

       550        560        570        580        590        600 
TEDRQLFSDK LNEIKEPIAP SFAVESVKDA LEAADKIGYP VMIRSAYALG GLGSGLCPDK 

       610        620        630        640        650        660 
ETLTDLATKA LAMTNQILVE RSVVGWKEIE YEVVRDAADN CVTVCNMENV DAMGVHTGDS 

       670        680        690        700        710        720 
IVVAPCQTLS NEECQMLRAV SIKVVRHLGI VGECNIQFAL HPTSLEYVII EVNARLSRSS 

       730        740        750        760        770        780 
ALASKATGYP LAFIAAKIAL GIPLPEIKNV VSGKTTACFE PSLDYMVTKI PRWDLDRFHG 

       790        800        810        820        830        840 
ASGLIGSSMK SVGEVMAIGR TFEESFQKAL RMCHPSVDGF TSNLPMNKAW SSDVNLRKEM 

       850        860        870        880        890        900 
AEPTSTRMYS MAKAIQSGIS LDEINKLTAI DKWFLYKMQG ILNMEKTLKG SRSESVPEET 

       910        920        930        940        950        960 
LRRAKQIGFS DRYIGKCLGL SETQTRELRL NKNVKPWVKQ IDTLAAEYPA ITNYLYLTYN 

       970        980        990       1000       1010       1020 
GQEHDIKFDD HGMMVLGCGP YHIGSSVEFD WCAVSSIRTL RHVGKKTVVV NCNPETVSTD 

      1030       1040       1050       1060       1070       1080 
FDECDKLYFE ELSQERIMDV FQLEQCDGCI ISVGGQIPNN LAVPLYKNGV KIMGTSPMQI 

      1090       1100       1110       1120       1130       1140 
DRAEDRSIFS AVLDELQIAQ APWKAVNSLD DALQFTKTVG YPCLLRPSYV LSGSAMNVVY 

      1150       1160       1170       1180       1190       1200 
GEEELKTFLA EATRVSQEHP VVITKFIEGA REVEMDAVGK EGRVISHAIS EHVEDAGVHS 

      1210       1220       1230       1240       1250       1260 
GDATLMIPTQ SISQGAIEKV KIATKKIATA FAISGPFNVQ FLVRGNDVLV IECNLRASRS 

      1270       1280       1290       1300       1310       1320 
FPFVSKTLGV DFIDVATKVM IGEKIDESSL PTLERPVIPA DYVGIKAPMF SWPRLRGADP 

      1330       1340       1350       1360       1370       1380 
VLKCEMASTG EVACFGQNVY SAFLKAMIST GFKLPQKGIL IGIQHSFRPH FLGTAQTLKD 

      1390       1400       1410       1420       1430       1440 
EGFKLYATEA TADWLNANDI TATPVAWPSQ EGQSGPSSIY KLIKEGNIDM VINLPNNNTK 

      1450       1460       1470       1480       1490 
YVRDNFAIRR TAVDTGTALL TNFQVVKMFA EAIKYSGDLD AKSLFHYRQF GGAKPS 

« Hide

References

[1]"3,5,3'-Triiodothyronine-induced carbamyl-phosphate synthetase gene expression is stabilized in the liver of Rana catesbeiana tadpoles during heat shock."
Helbing C.C., Atkinson B.G.
J. Biol. Chem. 269:11743-11750(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U05193 mRNA. Translation: AAA19016.1.
PIRI51170.

3D structure databases

ProteinModelPortalQ91293.
SMRQ91293. Positions 1340-1474.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG000279.

Family and domain databases

Gene3D1.10.1030.10. 1 hit.
3.30.1490.20. 2 hits.
3.30.470.20. 2 hits.
3.40.50.1380. 1 hit.
3.40.50.20. 2 hits.
3.50.30.20. 1 hit.
HAMAPMF_01209. CPSase_S_chain.
InterProIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
IPR005481. CarbamoylP_synth_lsu_N.
IPR005480. CarbamoylP_synth_lsu_oligo.
IPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR005483. CbamoylP_synth_lsu_CPSase_dom.
IPR017926. GATASE.
IPR011607. MGS-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamPF00289. 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.
[Graphical view]
PRINTSPR00098. CPSASE.
SMARTSM01096. CPSase_L_D3. 1 hit.
SM01097. CPSase_sm_chain. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF48108. SSF48108. 1 hit.
SSF52021. SSF52021. 1 hit.
SSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsTIGR01369. CPSaseII_lrg. 1 hit.
TIGR01368. CPSaseIIsmall. 1 hit.
PROSITEPS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCPSM_LITCT
AccessionPrimary (citable) accession number: Q91293
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families