Q9X0I0 (PUR8_THEMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenylosuccinate lyase
Short name=ASL
EC=4.3.2.2

Alternative name(s):
Adenylosuccinase
Short name=ASase

Gene names

Name:	purB
Ordered Locus Names:	TM_1095

Organism

Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]

Taxonomic identifier

243274 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Thermotogae › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga › Thermotoga maritima

Protein attributes

Sequence length	431 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP. (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
Pathway	Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2. Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.
Subunit structure	Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site. Ref.2
Sequence similarities	Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.

Ontologies

Keywords
Biological process	Purine biosynthesis
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' AMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway 'de novo' IMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity Inferred from electronic annotation. Source: EC N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) 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 – 431

431

Adenylosuccinate lyase

PRO_0000137886

Regions

Region

4 – 5

2

Substrate binding By similarity

Region

67 – 69

3

Substrate binding By similarity

Region

68 – 69

2

Substrate binding By similarity

Sites

Active site

141

1

Proton acceptor Ref.2

Active site

141

1

Proton donor/acceptor By similarity

Active site

262

1

Proton donor/acceptor By similarity

Binding site

95

1

Substrate By similarity

Binding site

212

1

Substrate By similarity

Binding site

301

1

Substrate By similarity

Binding site

306

1

Substrate By similarity

Binding site

310

1

Substrate By similarity

Secondary structure

1

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431

Helix Strand Turn

Details...

Helix

3 – 5

3

Helix

10 – 13

4

Helix

16 – 36

21

Helix

44 – 51

8

Helix

56 – 66

11

Helix

69 – 81

13

Helix

82 – 87

6

Turn

88 – 91

4

Helix

94 – 130

37

Turn

131 – 133

3

Beta strand

135 – 140

6

Beta strand

143 – 149

7

Helix

150 – 174

25

Beta strand

188 – 190

3

Helix

192 – 201

10

Beta strand

211 – 213

3

Helix

217 – 243

27

Turn

246 – 248

3

Beta strand

250 – 252

3

Helix

272 – 286

15

Helix

288 – 293

6

Helix

304 – 333

30

Helix

338 – 345

8

Turn

346 – 350

5

Helix

351 – 353

3

Helix

354 – 363

10

Helix

368 – 383

16

Beta strand

385 – 387

3

Helix

389 – 394

6

Helix

397 – 400

4

Helix

405 – 410

6

Helix

415 – 418

4

Helix

421 – 426

6

Sequences

	Sequence		Length	Mass (Da)
	Q9X0I0 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: D3ACB25D87582869	FASTA	431	49,873
	10 20 30 40 50 60 MVERYSLSPM KDLWTEEAKY RRWLEVELAV TRAYEELGMI PKGVTERIRN NAKIDVELFK 70 80 90 100 110 120 KIEEKTNHDV VAFVEGIGSM IGEDSRFFHY GLTSSDVLDT ANSLALVEAG KILLESLKEF 130 140 150 160 170 180 CDVLWEVANR YKHTPTIGRT HGVHAEPTSF GLKVLGWYSE MKRNVQRLER AIEEVSYGKI 190 200 210 220 230 240 SGAVGNYANV PPEVEEKALS YLGLKPEPVS TQVVPRDRHA FYLSTLAIVA AGIERIAVEI 250 260 270 280 290 300 RHLQRTEVLE VEEPFRKGQR GSSAMPHKKN PITCERLTGL SRMMRAYVDP SLENIALWHE 310 320 330 340 350 360 RDISHSSVER YVFPDATQTL YYMIVTATNV VRNMKVNEER MKKNIDLTKG LVFSQRVLLK 370 380 390 400 410 420 LIEKGLTRKE AYDIVQRNAL KTWNSEKHFL EYLLEDEEVK KLVTKEELEE LFDISYYLKH 430 VDHIFERFEK E

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]	"The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway." Toth E.A., Yeates T.O. Structure 8:163-174(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SUBUNIT, ACTIVE SITE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000512 Genomic DNA. Translation: AAD36171.1.

PIR

A72294.

RefSeq

NP_228901.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C3C	X-ray	1.80	A/B	2-430	[»]
1C3U	X-ray	2.30	A/B	1-431	[»]

ProteinModelPortal

Q9X0I0.

SMR

Q9X0I0. Positions 2-430.

ModBase

Search...

Protein-protein interaction databases

STRING

243274.TM1095.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAD36171; AAD36171; TM_1095.

GeneID

898670.

KEGG

tma:TM1095.

PATRIC

23937125. VBITheMar51294_1111.

Phylogenomic databases

eggNOG

COG0015.

KO

K01756.

OMA

KIAVNIR.

ProtClustDB

CLSK875567.

Enzyme and pathway databases

UniPathway

UPA00074; UER00132.
UPA00075; UER00336.

Family and domain databases

Gene3D

1.10.275.10. 1 hit.

InterPro

IPR019468. AdenyloSucc_lyase_C.
IPR003031. D_crystallin.
IPR024083. Fumarase/histidase_N.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR004769. Pur_lyase.
[Graphical view]

PANTHER

PTHR11444:SF2. PTHR11444:SF2. 1 hit.

Pfam

PF10397. ADSL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]

PRINTS

PR00145. ARGSUCLYASE.
PR00149. FUMRATELYASE.

SMART

SM00998. ADSL_C. 1 hit.
[Graphical view]

SUPFAM

SSF48557. L-Aspartase-like. 1 hit.

TIGRFAMs

TIGR00928. purB. 1 hit.

PROSITE

PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9X0I0.

Entry information

Entry name

PUR8_THEMA

Accession

Primary (citable) accession number: Q9X0I0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program