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Q75D66 (CARB_ASHGO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Carbamoyl-phosphate synthase arginine-specific large chain

EC=6.3.5.5
Alternative name(s):
Arginine-specific carbamoyl-phosphate synthetase, ammonia chain
Gene names
Name:CPA2
Ordered Locus Names:ABR157W
OrganismAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Complete proteome]
Taxonomic identifier284811 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium

Protein attributes

Sequence length1113 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 3 manganese ions per subunit By similarity.

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.

Subunit structure

Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate By similarity.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

In eukaryotes this enzyme is synthesized by two pathway-specific (arginine and pyrimidine) under separate control.

Sequence similarities

Belongs to the CarB family.

Contains 2 ATP-grasp domains.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
   Cellular componentCytoplasm
   DomainRepeat
   LigandATP-binding
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarginine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11131113Carbamoyl-phosphate synthase arginine-specific large chain
PRO_0000145088

Regions

Domain154 – 346193ATP-grasp 1
Domain693 – 888196ATP-grasp 2
Nucleotide binding174 – 22956ATP Potential
Nucleotide binding321 – 37151ATP Potential

Sites

Metal binding3031Manganese 1 By similarity
Metal binding3171Manganese 1 By similarity
Metal binding3171Manganese 2 By similarity
Metal binding3191Manganese 2 By similarity
Metal binding8431Manganese 3 By similarity
Metal binding8591Manganese 3 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q75D66 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: FE979E5C405A507D

FASTA1,113121,650
        10         20         30         40         50         60 
MSTAGISDEA SASAFTTAGY CPQLIKGIDS VLIIGSGGLS IGQAGEFDYS GSQAIKALKE 

        70         80         90        100        110        120 
TGKRTILINP NIATNQTSYS LADEVYFLPV TPEFITHVIK RERPDGILLT FGGQTGLNCG 

       130        140        150        160        170        180 
VALQRAVTLE KYGVTVLGTP ISVLETTEDR ELFARALKEI NMPIAESVAC STVEDAVAAA 

       190        200        210        220        230        240 
NDIGYPVIVR SAYALGGLGS GFADDDLQLR QLCAQSLALS PQVLVEKSLK GWKEIEYEVV 

       250        260        270        280        290        300 
RDRVGNCITV CNMENFDPLG IHTGDSIVLA PSQTLSDEEF HMLRTAAIEI IRHLGVVGEC 

       310        320        330        340        350        360 
NVQYALQPDG LAFKVIEVNA RLSRSSALAS KATGYPLAYT AAKIALGYTL PELPNPVTKS 

       370        380        390        400        410        420 
TVANFEPSLD YIVAKVPRWD LSKFQHVDKT IGSAMKSVGE VMAIGRNFEE AFQKAFRQVD 

       430        440        450        460        470        480 
PSLLGFQGSD EFADLDEALQ FPTDRRWLAV GEALMNRGYS VERVHELTKI DRFFLHKCMN 

       490        500        510        520        530        540 
IVRMQKQLET LGSINRLDEV LLRKAKKLGF CDKQIARAIS DDLSELDIRA LRKSFGILPF 

       550        560        570        580        590        600 
VKRIDTMAAE VPAVTNYLYV TYNAVKDDVT FGDNGIMVLG SGVYRIGSSV EFDWCAVNTV 

       610        620        630        640        650        660 
QALRKEGHKT IMINYNPETV STDFDEVDRL YFEELSFERV MDIYEAECAS GCVISMGGQQ 

       670        680        690        700        710        720 
PQNIASQLYE QGANILGTSP EDIDKAEDRH KFSTILDTLG LDQPRWSELK SLSEVKHFLD 

       730        740        750        760        770        780 
DVGYPVLVRP SYVLSGAAMS TVYNSEDLEG VFESAVAVSP EHPVVISKFI EGAQELDIDA 

       790        800        810        820        830        840 
VAYKGSLLVH AISEHVENAG VHSGDATLVL PPQSLKEEEK TRLKQLAAQV AAAWNITGPF 

       850        860        870        880        890        900 
NMQIIKTAEG GHTCLKIIEC NIRASRSFPF VSKVLGVNFV EIAVKAFLGG DLVPPSCDLM 

       910        920        930        940        950        960 
ARSYNYVATK CPQFSFTRLP GADPFLGVEM ASVGEVAAFG SNALESYWVA LQGLMSFCVP 

       970        980        990       1000       1010       1020 
LPPSGILLGG DLSKEHLGRV AALLAPHGFT LLALSEATCE YLSRYLPAES SVTVLQMPET 

      1030       1040       1050       1060       1070       1080 
GREVRALFEQ HNVQCVVNLA ARRASSPIDP DYRIRRSAID FAVPLFNEPQ TTMLFARALS 

      1090       1100       1110 
AYLPAELEMR QSDGPETPSY VLPWREYLGF KPT 

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References

[1]"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed: 15001715] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016815 Genomic DNA. Translation: AAS50929.1.
RefSeqNP_983105.2. NM_208458.2.

3D structure databases

ProteinModelPortalQ75D66.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ75D66.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4619215.
GenomeReviewsGene locus ABR157W in contig AE016815_GR.
KEGGago:AGOS_ABR157W.
NMPDRfig|33169.1.peg.750.

Organism-specific databases

AGDABR157W.

Phylogenomic databases

eggNOGfuNOG06096.
HOGENOMHBG405439.
OMAEGIEVAN.
OrthoDBEOG4T7CBC.
PhylomeDBQ75D66.

Family and domain databases

InterProIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
IPR005479. CarbamoylP_synth_lsu_ATP-bd.
IPR005483. CarbamoylP_synth_lsu_CPS-dom.
IPR005481. CarbamoylP_synth_lsu_N.
IPR005480. CarbamoylP_synth_lsu_oligo.
IPR011607. MGS-like_dom.
IPR013817. Pre-ATP_grasp.
IPR016185. PreATP-grasp-like.
[Graphical view]
Gene3DG3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 2 hits.
G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 2 hits.
G3DSA:1.10.1030.10. CarbamoylP_synth_lsu_oligo. 1 hit.
G3DSA:3.40.50.1380. MGS-like_dom. 1 hit.
G3DSA:3.40.50.20. Pre-ATP_grasp. 2 hits.
KOK01955.
PfamPF00289. CPSase_L_chain. 2 hits.
PF02786. CPSase_L_D2. 2 hits.
PF02787. CPSase_L_D3. 1 hit.
[Graphical view]
PRINTSPR00098. CPSASE.
SMARTSM01096. CPSase_L_D3. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF48108. CarbamoylP_synth_lsu_oligo. 1 hit.
SSF52335. MGS-like_dom. 1 hit.
SSF52440. PreATP-grasp-like. 2 hits.
TIGRFAMsTIGR01369. CPSaseII_lrg. 1 hit.
PROSITEPS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCARB_ASHGO
AccessionPrimary (citable) accession number: Q75D66
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families