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Q9X0I0

- PUR8_THEMA

UniProt

Q9X0I0 - PUR8_THEMA

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Protein
Adenylosuccinate lyase
Gene
purB, TM_1095
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei95 – 951Substrate By similarity
Active sitei141 – 1411Proton acceptor1 Publication
Active sitei141 – 1411Proton donor/acceptor By similarity
Binding sitei212 – 2121Substrate By similarity
Active sitei262 – 2621Proton donor/acceptor By similarity
Binding sitei301 – 3011Substrate By similarity
Binding sitei306 – 3061Substrate By similarity
Binding sitei310 – 3101Substrate By similarity

GO - Molecular functioni

  1. (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity Source: UniProtKB-EC
  2. N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. 'de novo' AMP biosynthetic process Source: UniProtKB-UniPathway
  2. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylosuccinate lyase (EC:4.3.2.2)
Short name:
ASL
Alternative name(s):
Adenylosuccinase
Short name:
ASase
Gene namesi
Name:purB
Ordered Locus Names:TM_1095
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000008183: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 431431Adenylosuccinate lyase
PRO_0000137886Add
BLAST

Interactioni

Subunit structurei

Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site.1 Publication

Protein-protein interaction databases

STRINGi243274.TM1095.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53
Helixi10 – 134
Helixi16 – 3621
Helixi44 – 518
Helixi56 – 6611
Helixi69 – 8113
Helixi82 – 876
Turni88 – 914
Helixi94 – 13037
Turni131 – 1333
Beta strandi135 – 1406
Beta strandi143 – 1497
Helixi150 – 17425
Beta strandi188 – 1903
Helixi192 – 20110
Beta strandi211 – 2133
Helixi217 – 24327
Turni246 – 2483
Beta strandi250 – 2523
Helixi272 – 28615
Helixi288 – 2936
Helixi304 – 33330
Helixi338 – 3458
Turni346 – 3505
Helixi351 – 3533
Helixi354 – 36310
Helixi368 – 38316
Beta strandi385 – 3873
Helixi389 – 3946
Helixi397 – 4004
Helixi405 – 4106
Helixi415 – 4184
Helixi421 – 4266

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C3CX-ray1.80A/B2-430[»]
1C3UX-ray2.30A/B1-431[»]
ProteinModelPortaliQ9X0I0.
SMRiQ9X0I0. Positions 2-430.

Miscellaneous databases

EvolutionaryTraceiQ9X0I0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4 – 52Substrate binding By similarity
Regioni67 – 693Substrate binding By similarity
Regioni68 – 692Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0015.
KOiK01756.
OMAiRNMGSTF.
OrthoDBiEOG686NDB.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
InterProiIPR019468. AdenyloSucc_lyase_C.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR004769. Pur_lyase.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10397. ADSL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SMARTiSM00998. ADSL_C. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00928. purB. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9X0I0-1 [UniParc]FASTAAdd to Basket

« Hide

MVERYSLSPM KDLWTEEAKY RRWLEVELAV TRAYEELGMI PKGVTERIRN    50
NAKIDVELFK KIEEKTNHDV VAFVEGIGSM IGEDSRFFHY GLTSSDVLDT 100
ANSLALVEAG KILLESLKEF CDVLWEVANR YKHTPTIGRT HGVHAEPTSF 150
GLKVLGWYSE MKRNVQRLER AIEEVSYGKI SGAVGNYANV PPEVEEKALS 200
YLGLKPEPVS TQVVPRDRHA FYLSTLAIVA AGIERIAVEI RHLQRTEVLE 250
VEEPFRKGQR GSSAMPHKKN PITCERLTGL SRMMRAYVDP SLENIALWHE 300
RDISHSSVER YVFPDATQTL YYMIVTATNV VRNMKVNEER MKKNIDLTKG 350
LVFSQRVLLK LIEKGLTRKE AYDIVQRNAL KTWNSEKHFL EYLLEDEEVK 400
KLVTKEELEE LFDISYYLKH VDHIFERFEK E 431
Length:431
Mass (Da):49,873
Last modified:November 1, 1999 - v1
Checksum:iD3ACB25D87582869
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000512 Genomic DNA. Translation: AAD36171.1.
PIRiA72294.
RefSeqiNP_228901.1. NC_000853.1.
WP_004080360.1. NC_023151.1.
YP_007977450.1. NC_021214.1.
YP_008991807.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD36171; AAD36171; TM_1095.
GeneIDi898670.
KEGGitma:TM1095.
tmi:THEMA_08870.
tmm:Tmari_1101.
PATRICi23937125. VBITheMar51294_1111.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000512 Genomic DNA. Translation: AAD36171.1 .
PIRi A72294.
RefSeqi NP_228901.1. NC_000853.1.
WP_004080360.1. NC_023151.1.
YP_007977450.1. NC_021214.1.
YP_008991807.1. NC_023151.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q9X0I0.
SMRi Q9X0I0. Positions 2-430.
ModBasei Search...

Protein-protein interaction databases

STRINGi 243274.TM1095.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD36171 ; AAD36171 ; TM_1095 .
GeneIDi 898670.
KEGGi tma:TM1095.
tmi:THEMA_08870.
tmm:Tmari_1101.
PATRICi 23937125. VBITheMar51294_1111.

Phylogenomic databases

eggNOGi COG0015.
KOi K01756.
OMAi RNMGSTF.
OrthoDBi EOG686NDB.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00132 .
UPA00075 ; UER00336 .

Miscellaneous databases

EvolutionaryTracei Q9X0I0.

Family and domain databases

Gene3Di 1.10.275.10. 1 hit.
InterProi IPR019468. AdenyloSucc_lyase_C.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR004769. Pur_lyase.
[Graphical view ]
PANTHERi PTHR11444. PTHR11444. 1 hit.
Pfami PF10397. ADSL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view ]
PRINTSi PR00149. FUMRATELYASE.
SMARTi SM00998. ADSL_C. 1 hit.
[Graphical view ]
SUPFAMi SSF48557. SSF48557. 1 hit.
TIGRFAMsi TIGR00928. purB. 1 hit.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiPUR8_THEMA
AccessioniPrimary (citable) accession number: Q9X0I0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: September 3, 2014
This is version 112 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

External Data

Dasty 3

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