Q9X2A1 (ASSY_THEMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Argininosuccinate synthase
EC=6.3.4.5

Alternative name(s):
Citrulline--aspartate ligase

Gene names

Name:	argG
Ordered Locus Names:	TM_1780

Organism

Thermotoga maritima

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	409 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate. HAMAP MF_00005
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. HAMAP MF_00005
Subunit structure	Homotetramer. Ref.2
Subcellular location	Cytoplasm Probable HAMAP MF_00005.
Sequence similarities	Belongs to the argininosuccinate synthase family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW argininosuccinate synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 409

409

Argininosuccinate synthase HAMAP MF_00005

PRO_0000148656

Regions

Nucleotide binding

8 – 16

9

ATP By similarity

Sites

Binding site

34

1

ATP; via amide nitrogen and carbonyl oxygen By similarity

Binding site

85

1

Citrulline By similarity

Binding site

115

1

ATP; via amide nitrogen By similarity

Binding site

117

1

Aspartate By similarity

Binding site

121

1

Aspartate By similarity

Binding site

121

1

Citrulline By similarity

Binding site

122

1

Aspartate By similarity

Binding site

125

1

Citrulline By similarity

Binding site

178

1

Citrulline By similarity

Binding site

187

1

Citrulline By similarity

Binding site

268

1

Citrulline By similarity

Binding site

280

1

Citrulline By similarity

Secondary structure

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409

Helix Strand Turn

Details...

Beta strand

4 – 8

5

Helix

13 – 24

12

Beta strand

28 – 37

10

Helix

42 – 52

11

Beta strand

55 – 61

7

Helix

63 – 69

7

Helix

71 – 75

5

Turn

76 – 78

3

Turn

82 – 84

3

Helix

88 – 107

20

Beta strand

110 – 113

4

Helix

122 – 133

12

Beta strand

137 – 140

4

Helix

142 – 144

3

Helix

146 – 151

6

Helix

157 – 165

9

Beta strand

176 – 181

6

Beta strand

186 – 190

5

Helix

191 – 194

4

Helix

202 – 204

3

Turn

211 – 213

3

Beta strand

219 – 226

8

Beta strand

229 – 235

7

Turn

236 – 238

3

Helix

245 – 258

14

Beta strand

263 – 269

7

Beta strand

271 – 281

11

Helix

283 – 299

17

Helix

302 – 321

20

Helix

327 – 340

14

Beta strand

345 – 352

8

Beta strand

355 – 362

8

Beta strand

364 – 366

3

Helix

383 – 404

22

Sequences

	Sequence		Length	Mass (Da)
	Q9X2A1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: ECCDC8575E962482	FASTA	409	46,054
	10 20 30 40 50 60 MKEKVVLAYS GGLDTSVILK WLCEKGFDVI AYVANVGQKD DFVAIKEKAL KTGASKVYVE 70 80 90 100 110 120 DLRREFVTDY IFTALLGNAM YEGRYLLGTA IARPLIAKRQ VEIAEKEGAQ YVAHGATGKG 130 140 150 160 170 180 NDQVRFELTY AALNPNLKVI SPWKDPEFLA KFKGRTDLIN YAMEKGIPIK VSKKRPYSED 190 200 210 220 230 240 ENLMHISHEA GKLEDPAHIP DEDVFTWTVS PKDAPDEETL LEIHFENGIP VKVVNLKDGT 250 260 270 280 290 300 EKTDPLELFE YLNEVGAKNG VGRLDMVENR FIGIKSRGVY ETPGATILWI AHRDLEGITM 310 320 330 340 350 360 DKEVMHLRDM LAPKFAELIY NGFWFSPEME FLLAAFRKAQ ENVTGKVTVS IYKGNVMPVA 370 380 390 400 RYSPYSLYNP ELSSMDVEGG FDATDSKGFI NIHALRLKVH QLVKKGYQR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]	"Crystal structure of argininosuccinate synthase (TM1780) from Thermotoga maritima at 1.65 A resolution." Joint center for structural genomics (JCSG) Submitted (MAR-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000512 Genomic DNA. Translation: AAD36844.1.

PIR

H72210.

RefSeq

NP_229577.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VL2	X-ray	1.65	A/B/C/D	1-409	[»]

ProteinModelPortal

Q9X2A1.

SMR

Q9X2A1. Positions 2-409.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

897844.

GenomeReviews

Gene locus TM_1780 in contig AE000512_GR.

KEGG

tma:TM1780.

NMPDR

fig|243274.1.peg.1761.

PATRIC

23938542. VBITheMar51294_1799.

TIGR

TM_1780.

Phylogenomic databases

HOGENOM

HBG335267.

OMA

RANAIYE.

PhylomeDB

Q9X2A1.

ProtClustDB

PRK00509.

Enzyme and pathway databases

BioCyc

TMAR243274:TM_1780-MONOMER.

Family and domain databases

HAMAP

MF_00005. Arg_succ_synth_type1.
[Tree]

InterPro

IPR001518. Arginosuc_synth.
IPR018223. Arginosuc_synth_CS.
IPR023434. Arginosuc_synth_type_1_subfam.
IPR024074. AS_cat/multimer_dom_body.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]

Gene3D

G3DSA:3.90.1260.10. G3DSA:3.90.1260.10. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.

KO

K01940.

PANTHER

PTHR11587. Arginosuc_synth. 1 hit.

Pfam

PF00764. Arginosuc_synth. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00032. ArgG. 1 hit.

PROSITE

PS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ASSY_THEMA

Accession

Primary (citable) accession number: Q9X2A1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2002
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program