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Protein

Adenylosuccinate lyase

Gene

Tpet_1648

Organism
Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotation
N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP.UniRule annotation

Pathwayi: AMP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes AMP from IMP.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Adenylosuccinate synthetase (purA)
  2. Adenylosuccinate lyase (Tpet_1648)
This subpathway is part of the pathway AMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from IMP, the pathway AMP biosynthesis via de novo pathway and in Purine metabolism.

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Phosphoribosylaminoimidazole-succinocarboxamide synthase (purC)
  2. Adenylosuccinate lyase (Tpet_1648)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationImported

Keywords - Biological processi

Purine biosynthesisUniRule annotation

Enzyme and pathway databases

BioCyciTPET390874:GHJI-1699-MONOMER.
UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylosuccinate lyaseUniRule annotation (EC:4.3.2.2UniRule annotation)
Short name:
ASLUniRule annotation
Alternative name(s):
AdenylosuccinaseUniRule annotation
Gene namesi
Ordered Locus Names:Tpet_1648Imported
OrganismiThermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)Imported
Taxonomic identifieri390874 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000006558 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi390874.Tpet_1648.

Structurei

3D structure databases

ProteinModelPortaliA5IN80.
SMRiA5IN80. Positions 2-430.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini349 – 42981ADSL_CInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C83. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000033912.
KOiK01756.
OMAiVQENAMK.
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.

A5IN80-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVERYSLSPM KDLWTEEAKY RRWLEVELAV TKAYEELGMI PKGVTERIRN
60 70 80 90 100
KAKIDVELFK KIEERTNHDV VAFVEGIGSM IGEDSRFFHY GLTSSDVLDT
110 120 130 140 150
ANSLALVEAG KILLESLREF CDVLWEVANR YKHTPTIGRT HGVHAEPTSF
160 170 180 190 200
GLKVLGWYSE MKRNIQRLER AIEEVSYGKI SGAVGNYANV PPEVEEKALS
210 220 230 240 250
YLGLKPEPVS TQVVPRDRHA FYLSTLAIVA AGIERIAVEI RHLQRTEVLE
260 270 280 290 300
VEEPFREGQR GSSAMPHKKN PITCERLTGL SRMMRAYVDP SLENIALWHE
310 320 330 340 350
RDISHSSVER YVFPDATQTL YYMIVTATNV VKNMKVNEER MKKNIDRTKG
360 370 380 390 400
LVFSQRVLLK LIEKGLTRKE AYDIVQRNAL KTWNSEKHFL EYLLEDEDVK
410 420 430
KLVTKEELEE LFDASYYLKH VDHIFERFEK E
Length:431
Mass (Da):49,889
Last modified:June 26, 2007 - v1
Checksum:i384AB44B29237026
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000702 Genomic DNA. Translation: ABQ47653.1.
RefSeqiWP_011944062.1. NC_009486.1.

Genome annotation databases

EnsemblBacteriaiABQ47653; ABQ47653; Tpet_1648.
KEGGitpt:Tpet_1648.
PATRICi23946147. VBIThePet65348_1666.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000702 Genomic DNA. Translation: ABQ47653.1.
RefSeqiWP_011944062.1. NC_009486.1.

3D structure databases

ProteinModelPortaliA5IN80.
SMRiA5IN80. Positions 2-430.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi390874.Tpet_1648.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABQ47653; ABQ47653; Tpet_1648.
KEGGitpt:Tpet_1648.
PATRICi23946147. VBIThePet65348_1666.

Phylogenomic databases

eggNOGiENOG4105C83. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000033912.
KOiK01756.
OMAiVQENAMK.
OrthoDBiEOG686NDB.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciTPET390874:GHJI-1699-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RKU-1 / ATCC BAA-488 / DSM 13995Imported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RKU-1 / ATCC BAA-488 / DSM 13995Imported.

Entry informationi

Entry nameiA5IN80_THEP1
AccessioniPrimary (citable) accession number: A5IN80
Entry historyi
Integrated into UniProtKB/TrEMBL: June 26, 2007
Last sequence update: June 26, 2007
Last modified: July 6, 2016
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

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.