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Protein

Aspartate carbamoyltransferase

Gene

pyrB

Organism
Pyrococcus abyssi (strain GE5 / Orsay)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Aspartate carbamoyltransferase (pyrB)
  3. Dihydroorotase (pyrC)
This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-dihydroorotate from bicarbonate, the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Pyrimidine biosynthesis

Enzyme and pathway databases

BRENDAi2.1.3.2. 5242.
UniPathwayiUPA00070; UER00116.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate carbamoyltransferase (EC:2.1.3.2)
Alternative name(s):
Aspartate transcarbamylase
Short name:
ATCase
Gene namesi
Name:pyrB
Ordered Locus Names:PYRAB13270
ORF Names:PAB1498
OrganismiPyrococcus abyssi (strain GE5 / Orsay)
Taxonomic identifieri272844 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000810 Componenti: Chromosome
  • UP000009139 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 308308Aspartate carbamoyltransferasePRO_0000113253Add
BLAST

Interactioni

Subunit structurei

Heterooligomer of catalytic and regulatory chains.1 Publication

Protein-protein interaction databases

STRINGi272844.PAB1498.

Structurei

Secondary structure

1
308
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 133Combined sources
Helixi16 – 3621Combined sources
Turni41 – 444Combined sources
Beta strandi46 – 538Combined sources
Helixi57 – 6812Combined sources
Beta strandi72 – 776Combined sources
Helixi79 – 813Combined sources
Helixi83 – 864Combined sources
Helixi90 – 978Combined sources
Turni98 – 1003Combined sources
Beta strandi102 – 1109Combined sources
Helixi113 – 1197Combined sources
Beta strandi125 – 1306Combined sources
Helixi136 – 14914Combined sources
Beta strandi153 – 16210Combined sources
Turni164 – 1663Combined sources
Helixi168 – 1769Combined sources
Helixi177 – 1793Combined sources
Beta strandi182 – 1876Combined sources
Helixi190 – 1923Combined sources
Helixi196 – 2049Combined sources
Beta strandi209 – 2135Combined sources
Helixi216 – 2194Combined sources
Beta strandi223 – 2275Combined sources
Helixi232 – 2343Combined sources
Beta strandi235 – 2373Combined sources
Helixi238 – 2425Combined sources
Turni243 – 2464Combined sources
Helixi254 – 2574Combined sources
Beta strandi263 – 2653Combined sources
Beta strandi271 – 2744Combined sources
Helixi276 – 2805Combined sources
Helixi286 – 2916Combined sources
Helixi293 – 30412Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML4X-ray1.80A1-308[»]
ProteinModelPortaliP77918.
SMRiP77918. Positions 2-308.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP77918.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATCase/OTCase family.Curated

Phylogenomic databases

eggNOGiarCOG00911. Archaea.
COG0540. LUCA.
HOGENOMiHOG000022685.
KOiK00609.
OMAiKQSFYGV.

Family and domain databases

Gene3Di3.40.50.1370. 2 hits.
HAMAPiMF_00001. Asp_carb_tr.
InterProiIPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR002082. Asp_carbamoyltransf.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
[Graphical view]
PfamiPF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
[Graphical view]
PRINTSiPR00100. AOTCASE.
PR00101. ATCASE.
SUPFAMiSSF53671. SSF53671. 1 hit.
TIGRFAMsiTIGR00670. asp_carb_tr. 1 hit.
PROSITEiPS00097. CARBAMOYLTRANSFERASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P77918-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDWKGRDVIS IRDFSKEDIE TVLATAERLE RELKEKGQLE YAKGKILATL
60 70 80 90 100
FFEPSTRTRL SFESAMHRLG GAVIGFAEAS TSSVKKGESL RDTIKTVEQY
110 120 130 140 150
CDVIVIRHPK EGAARLAAEV AEVPVINAGD GSNQHPTQTL LDLYTIKKEF
160 170 180 190 200
GRIDGLKIGL LGDLKYGRTV HSLAEALTFY DVELYLISPE LLRMPRHIVE
210 220 230 240 250
ELREKGMKVV ETTTLEDVIG KLDVLYVTRI QKERFPDEQE YLKVKGSYQV
260 270 280 290 300
NLKVLEKAKD ELRIMHPLPR VDEIHPEVDN TKHAIYFRQV FNGVPVRMAL

LALVLGVI
Length:308
Mass (Da):34,901
Last modified:February 1, 1997 - v1
Checksum:iD36961E7749C012E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U61765 Genomic DNA. Translation: AAB62984.1.
AJ248287 Genomic DNA. Translation: CAB50232.1.
HE613800 Genomic DNA. Translation: CCE70769.1.
PIRiC75042.
RefSeqiWP_010868442.1. NC_000868.1.

Genome annotation databases

EnsemblBacteriaiCAB50232; CAB50232; PAB1498.
GeneIDi1496715.
KEGGipab:PAB1498.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U61765 Genomic DNA. Translation: AAB62984.1.
AJ248287 Genomic DNA. Translation: CAB50232.1.
HE613800 Genomic DNA. Translation: CCE70769.1.
PIRiC75042.
RefSeqiWP_010868442.1. NC_000868.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML4X-ray1.80A1-308[»]
ProteinModelPortaliP77918.
SMRiP77918. Positions 2-308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272844.PAB1498.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB50232; CAB50232; PAB1498.
GeneIDi1496715.
KEGGipab:PAB1498.

Phylogenomic databases

eggNOGiarCOG00911. Archaea.
COG0540. LUCA.
HOGENOMiHOG000022685.
KOiK00609.
OMAiKQSFYGV.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00116.
BRENDAi2.1.3.2. 5242.

Miscellaneous databases

EvolutionaryTraceiP77918.

Family and domain databases

Gene3Di3.40.50.1370. 2 hits.
HAMAPiMF_00001. Asp_carb_tr.
InterProiIPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR002082. Asp_carbamoyltransf.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
[Graphical view]
PfamiPF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
[Graphical view]
PRINTSiPR00100. AOTCASE.
PR00101. ATCASE.
SUPFAMiSSF53671. SSF53671. 1 hit.
TIGRFAMsiTIGR00670. asp_carb_tr. 1 hit.
PROSITEiPS00097. CARBAMOYLTRANSFERASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Aspartate transcarbamylase from the deep-sea hyperthermophilic archaeon Pyrococcus abyssi: genetic organization, structure, and expression in Escherichia coli."
    Purcarea C., Herve G., Ladjimi M.M., Cunin R.
    J. Bacteriol. 179:4143-4157(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT.
    Strain: GE5 / Orsay.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: GE5 / Orsay.
  3. "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638."
    Gao J., Wang J.
    Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: GE5 / Orsay.

Entry informationi

Entry nameiPYRB_PYRAB
AccessioniPrimary (citable) accession number: P77918
Secondary accession number(s): G8ZHD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: November 11, 2015
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.