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Protein

Quinolinate synthase A

Gene

nadA

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.UniRule annotation

Catalytic activityi

Glycerone phosphate + iminosuccinate = pyridine-2,3-dicarboxylate + 2 H2O + phosphate.UniRule annotation

Cofactori

[4Fe-4S] clusterUniRule annotationNote: Binds 1 [4Fe-4S] cluster per subunit.UniRule annotation

Pathwayi: NAD(+) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes quinolinate from iminoaspartate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Quinolinate synthase A (nadA)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes quinolinate from iminoaspartate, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei25IminoaspartateUniRule annotation1
Binding sitei42Iminoaspartate; via amide nitrogenUniRule annotation1
Binding sitei113IminoaspartateUniRule annotation1
Binding sitei130IminoaspartateUniRule annotation1
Binding sitei200IminoaspartateUniRule annotation1
Binding sitei217IminoaspartateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BRENDAi2.5.1.72. 5243.
UniPathwayiUPA00253; UER00327.

Names & Taxonomyi

Protein namesi
Recommended name:
Quinolinate synthase AUniRule annotation (EC:2.5.1.72UniRule annotation)
Gene namesi
Name:nadAUniRule annotation
Ordered Locus Names:PF1977
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000001013 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001558091 – 303Quinolinate synthase AAdd BLAST303

Interactioni

Protein-protein interaction databases

STRINGi186497.PF1977.

Structurei

Secondary structure

1303
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 18Combined sources17
Beta strandi20 – 25Combined sources6
Helixi30 – 35Combined sources6
Beta strandi37 – 40Combined sources4
Helixi42 – 48Combined sources7
Beta strandi54 – 61Combined sources8
Helixi63 – 72Combined sources10
Beta strandi76 – 79Combined sources4
Helixi95 – 104Combined sources10
Beta strandi110 – 116Combined sources7
Helixi118 – 121Combined sources4
Beta strandi125 – 128Combined sources4
Turni130 – 132Combined sources3
Helixi133 – 139Combined sources7
Beta strandi143 – 149Combined sources7
Helixi151 – 161Combined sources11
Beta strandi164 – 169Combined sources6
Beta strandi171 – 173Combined sources3
Helixi177 – 179Combined sources3
Helixi182 – 190Combined sources9
Beta strandi197 – 199Combined sources3
Helixi205 – 209Combined sources5
Beta strandi212 – 214Combined sources3
Helixi217 – 220Combined sources4
Beta strandi226 – 229Combined sources4
Beta strandi231 – 234Combined sources4
Helixi237 – 245Combined sources9
Beta strandi252 – 255Combined sources4
Beta strandi257 – 260Combined sources4
Helixi268 – 277Combined sources10
Helixi286 – 302Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4HHEX-ray2.80A1-303[»]
ProteinModelPortaliQ8TZL3.
SMRiQ8TZL3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8TZL3.

Family & Domainsi

Sequence similaritiesi

Belongs to the quinolinate synthase A family. Type 2 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiarCOG04459. Archaea.
COG0379. LUCA.
HOGENOMiHOG000222770.
KOiK03517.
OMAiIAHPECE.

Family and domain databases

HAMAPiMF_00568. NadA_type2. 1 hit.
InterProiIPR003473. NadA.
IPR023066. Quinolinate_synth_type2.
[Graphical view]
PfamiPF02445. NadA. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00550. nadA. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8TZL3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKVEELKKE IERLKKERNA IILAHNYQLP EVQDVADFVG DSLELARKAT
60 70 80 90 100
KVDADVIVFA GVDFMAETAK ILNPDKIVLI PNKRATCAMA NMLKVKHILE
110 120 130 140 150
AKKKYPNAPV VLYVNSTAET KAYADVTVTS ANAVDIIRKL DSDVIIFGPD
160 170 180 190 200
KNLAHYVAKV TGKTIIPIPP EGHCYVHKKF TIEDVERAKK LHPNAKLMVH
210 220 230 240 250
PECNPEVQEH ADIIVSTGGM IRRACEWDEW VVFTEREMVY RLSKLYPNKK
260 270 280 290 300
FYPAKEDAVC VGMKAITLQH VYESLRDMKY EVTVPEEIAE KARKAIERML

EMS
Length:303
Mass (Da):34,405
Last modified:June 1, 2002 - v1
Checksum:i488B122FD4F1271F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009950 Genomic DNA. Translation: AAL82101.1.
RefSeqiWP_011013119.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL82101; AAL82101; PF1977.
GeneIDi1469859.
KEGGipfu:PF1977.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009950 Genomic DNA. Translation: AAL82101.1.
RefSeqiWP_011013119.1. NC_003413.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4HHEX-ray2.80A1-303[»]
ProteinModelPortaliQ8TZL3.
SMRiQ8TZL3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi186497.PF1977.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL82101; AAL82101; PF1977.
GeneIDi1469859.
KEGGipfu:PF1977.

Phylogenomic databases

eggNOGiarCOG04459. Archaea.
COG0379. LUCA.
HOGENOMiHOG000222770.
KOiK03517.
OMAiIAHPECE.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00327.
BRENDAi2.5.1.72. 5243.

Miscellaneous databases

EvolutionaryTraceiQ8TZL3.

Family and domain databases

HAMAPiMF_00568. NadA_type2. 1 hit.
InterProiIPR003473. NadA.
IPR023066. Quinolinate_synth_type2.
[Graphical view]
PfamiPF02445. NadA. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00550. nadA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNADA_PYRFU
AccessioniPrimary (citable) accession number: Q8TZL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: June 1, 2002
Last modified: November 2, 2016
This is version 83 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.