A0A023F583 · A0A023F583_TRIIF

  • Protein
    Putative multifunctional pyrimidine synthesis protein cad includes carbamoyl-phosphate synthetase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    4/5

Function

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site252Nucleophile
Active site336
Active site338

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionamino acid binding
Molecular Functionaspartate carbamoyltransferase activity
Molecular FunctionATP binding
Molecular Functioncarbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
Molecular Functiondihydroorotase activity
Molecular Functionmetal ion binding
Biological Process'de novo' pyrimidine nucleobase biosynthetic process
Biological Process'de novo' UMP biosynthetic process
Biological Processcitrulline biosynthetic process
Biological Processglutamine metabolic process
Biological ProcessUTP biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Submitted names
    • Putative multifunctional pyrimidine synthesis protein cad includes carbamoyl-phosphate synthetase

Organism names

  • Taxonomic identifier
  • Strain
    • Chile
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Paraneoptera > Hemiptera > Heteroptera > Panheteroptera > Cimicomorpha > Reduviidae > Triatominae > Triatoma

Accessions

  • Primary accession
    A0A023F583

Subcellular Location

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain517-709ATP-grasp
Domain1049-1240ATP-grasp
Domain1305-1461MGS-like

Sequence similarities

In the 2nd section; belongs to the CarB family.
In the 3rd section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily.
In the C-terminal section; belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
In the N-terminal section; belongs to the CarA family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    2,202
  • Mass (Da)
    244,558
  • Last updated
    2014-06-11 v1
  • Checksum
    D5AB3D294A663C9B
CILVLEDGTIYKGYNFGASSSINGEVVFQTGMVGYVESLTDPSYHAQILVLTYPLIGNYGVPSDEYDEYNLPKWFESHKIWAAGLVVGEVCETPSHWQSDRTLSQWLEANNVPGIAGIDTRDLTKKIRHKGSILGKIITDTLISPKNLHFLDPNVRNLVSEVSVKERKLYTPKTPSNLRICVVDCGMKYNQLRCFLKRGATVEVVPWDHHLDPTTYDGLFLSNGPGNPLMCAATVTNIKKAIENKKPIFGICLGHQLLAIAAGCTTYKMKYGNRGHNQPCIHFSTKRCYMTSQNHGFAVDSKSIPEGWIEFFVNANDNSNEGIIHENLPFFSVQFHPEHCAGPQDLEILFDIFLSAVELYKNNSACISLVDKVTEALHFKQAVHTPLAHKRNKVLLLGSGGLSIGQAGEFDYSGSQAIKALQEENIRTVLINPNIATVQTSKGLADKVYFLPLLPNYVEQVICSERPDGVLLTFGGQTGLNCGVELQKNGVFDKYNVKILGTPIQSIIETEDRKLFADRINEIEEKVAPSAAVYSVNEALDAAMRLGYPVLARSAFSLGGLGSGFANNDDELRKLAQHAFAHSNQLIIDKSLKGWKEVEYEVVRDAFDNCITVCNMENVDPLGIHTGESIVVAPSQTLSNAEYNRLRTTAIKVIRHFGIVGECNIQYALSPTSGEFYIIEVNARLSRSSALASKATGFPLAYVAAKLALGYSLVDIRNSVTMTTTSCFEPSLDYCVVKIPRWDLSKFSRVSTKIGSSMKSVGEVMAIGRKFEEAFQKAMRMVDENVIGFDPYAKSPCDVELEQPTDKRMFVLAAAIKDGYTIDRLYELTKIDRWFLYKMANIVKMQMHLEEQTHVTLEQLLEAKKLGFSDKQIASFVKSTELAIRNKREENGILPFVKQIDTVAAEWPATTNYLYLTYNGRSHDLTFPGGYTMVIGSGVYRIGSSVEFDWCAVGCLRELKKLGKKTIMVNYNPETVSTDYDMSDRLYFEEISFEVVMDIYNVENPEGIILSMGGQLPNNIAMDLHRQQARILGTSPESVDGAENRFKFSRMLDRIGILQPRWKELTNLKSAMDFCEEVGYPCLVRPSYVLSGAAMSVVHSERDLEEYLALASDVSKEHPVVISKFLQEAKEIDVDAVACDGVILCMAVSEHVENAGVHSGDATLVTPPQDINAETLAKILAISRAVASSLEVTGPFNMQLIAKDNVLKVIECNVRVSRSFPFVSKTLDHDFVATATRVIVGEKVEPVDVLMGCGKVGVKVAVFSFSRLAGADVMLGVEMASTGEVACFGDNRYEAYLKAMLSTGFHIPQKAILLSIGSFKHKKELLPSMKSLQKMGYKLYASMGTADFYNEHGVRVEPVQWTFENIGEATTTSGELNNLADFLARKDFDLVINLPMRNRGARRVSSFMTYGYRTRRLAVDFSVPLVTDVKCAKLLVEAMLGTKECPVMKTHTDCLTSRRIIRLPGLIDVHVHAREPGAEYKEDIASCTAAAIAGGITLVCLMPNTDPPCIDQTTFSLVKELAAEKARCDYGIFLGATEENYNIIPELASDAVGLKMYLNETFNTLRLRDLTFWIKHFDNWPKKSPLCVHAEGQTTAAVLLLATLHNRPIHVCHVARKEEIQIIRAAKEKGLHVTCEVCPHHLFLTEKAKEFLGENKSQVRPVLCTEEDRQALWDNLDVIDCFATDHAPHTVEEKTGDKPPPGFPGLETILPLLLTAVNEGKLTIEDVIDKMHRNPRRIFNLPEQRDTYVEVDMDMEGVIPDCPPFSKARWTPFAGMPVKGGVHRVVLRGEVAFIEGQVVLNPGFGRDVREMKASKIIQIMAGETVHSRPGSSLETTCPHDKLYHVEEHVSEVQLKVPVDLTGRPVSPLAILPKIKSDITRENVLHVPQPLTSPTHSLAHQHVLTVDMFSKDQLNELFNLAQTLRIFVLKERPIDHILKGKVMASIFYEVSTRTSCSFSAAMQRLGGKVIHVDETSSSVKKGETLEDTVAVMASYADVVVLRHPEPGAVNRASQHCRKPLVNAGDGTGEHPTQALLDVFTIREEIGTVNGLTITMVGDLKHGRTVHSLARLLTLYNVQLRYVSPPSLGMPKHITDFVAGRGIAQQEMSSLEEALPDSDIVYMTRIQRERFSSQMEYDKACGLLILSPQLMTKAKRKMVVMHPLPRVFEISPELDSDPRAAYFRQAECGMYVRMALLAMLLGKC

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GBBI01002464
EMBL· GenBank· DDBJ
JAC16248.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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