Q8TZL3 (NADA_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Quinolinate synthase A
EC=2.5.1.72

Gene names

Name:	nadA
Ordered Locus Names:	PF1977

Organism

Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP]

Taxonomic identifier

186497 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus › Pyrococcus furiosus

Protein attributes

Sequence length	303 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate By similarity. HAMAP-Rule MF_00568
Catalytic activity	Glycerone phosphate + iminosuccinate = pyridine-2,3-dicarboxylate + 2 H2O + phosphate. HAMAP-Rule MF_00568
Cofactor	Binds 1 4Fe-4S cluster per subunit By similarity.
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1. HAMAP-Rule MF_00568
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the quinolinate synthase A family. Type 2 subfamily.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Cytoplasm
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	NAD biosynthetic process Inferred from electronic annotation. Source: HAMAP quinolinate biosynthetic process Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW quinolinate synthetase A activity Inferred from electronic annotation. Source: HAMAP transferase activity, transferring alkyl or aryl (other than methyl) groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 303

303

Quinolinate synthase A HAMAP-Rule MF_00568

PRO_0000155809

Sites

Binding site

25

1

Iminoaspartate By similarity

Binding site

42

1

Iminoaspartate; via amide nitrogen By similarity

Binding site

113

1

Iminoaspartate By similarity

Binding site

130

1

Iminoaspartate By similarity

Binding site

200

1

Iminoaspartate By similarity

Binding site

217

1

Iminoaspartate By similarity

Secondary structure

1

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303

Helix Strand Turn

Details...

Helix

2 – 18

17

Beta strand

20 – 25

6

Helix

30 – 35

6

Beta strand

37 – 40

4

Helix

42 – 48

7

Beta strand

54 – 61

8

Helix

63 – 72

10

Beta strand

76 – 79

4

Helix

95 – 104

10

Beta strand

110 – 116

7

Helix

118 – 121

4

Beta strand

125 – 128

4

Turn

130 – 132

3

Helix

133 – 139

7

Beta strand

143 – 149

7

Helix

151 – 161

11

Beta strand

164 – 169

6

Beta strand

171 – 173

3

Helix

177 – 179

3

Helix

182 – 189

8

Beta strand

190 – 192

3

Beta strand

197 – 199

3

Helix

205 – 208

4

Helix

217 – 222

6

Beta strand

231 – 234

4

Helix

236 – 242

7

Helix

243 – 245

3

Beta strand

252 – 255

4

Beta strand

257 – 260

4

Helix

268 – 277

10

Helix

286 – 302

17

Sequences

	Sequence		Length	Mass (Da)
	Q8TZL3 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 488B122FD4F1271F	FASTA	303	34,405
	10 20 30 40 50 60 MEKVEELKKE IERLKKERNA IILAHNYQLP EVQDVADFVG DSLELARKAT KVDADVIVFA 70 80 90 100 110 120 GVDFMAETAK ILNPDKIVLI PNKRATCAMA NMLKVKHILE AKKKYPNAPV VLYVNSTAET 130 140 150 160 170 180 KAYADVTVTS ANAVDIIRKL DSDVIIFGPD KNLAHYVAKV TGKTIIPIPP EGHCYVHKKF 190 200 210 220 230 240 TIEDVERAKK LHPNAKLMVH PECNPEVQEH ADIIVSTGGM IRRACEWDEW VVFTEREMVY 250 260 270 280 290 300 RLSKLYPNKK FYPAKEDAVC VGMKAITLQH VYESLRDMKY EVTVPEEIAE KARKAIERML EMS

References

[1]

"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences." Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T. Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE009950 Genomic DNA. Translation: AAL82101.1.

RefSeq

NP_579706.1. NC_003413.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2QS0	X-ray	2.80	A	1-303	[»]

ProteinModelPortal

Q8TZL3.

ModBase

Search...

Protein-protein interaction databases

STRING

186497.PF1977.

Proteomic databases

PRIDE

Q8TZL3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAL82101; AAL82101; PF1977.

GeneID

1469859.

KEGG

pfu:PF1977.

Phylogenomic databases

eggNOG

COG0379.

HOGENOM

HOG000222770.

KO

K03517.

OMA

GCPADEF.

ProtClustDB

PRK09375.

Enzyme and pathway databases

UniPathway

UPA00253; UER00327.

Family and domain databases

HAMAP

MF_00568. NadA_type2.

InterPro

IPR003473. NadA.
IPR023066. Quinolinate_synth_type2.
[Graphical view]

Pfam

PF02445. NadA. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00550. nadA. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q8TZL3.

Entry information

Entry name

NADA_PYRFU

Accession

Primary (citable) accession number: Q8TZL3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2002
Last sequence update:	June 1, 2002
Last modified:	May 1, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program