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Protein

Adenylosuccinate lyase

Gene

Hhal_0026

Organism
Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira halophila (strain DSM 244 / SL1))
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 (Hhal_0026)
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 (Hhal_0026)
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

BioCyciHHAL349124:GI3I-28-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:Hhal_0026Imported
OrganismiHalorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira halophila (strain DSM 244 / SL1))Imported
Taxonomic identifieri349124 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeHalorhodospira
Proteomesi
  • UP000000647 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi349124.Hhal_0026.

Structurei

3D structure databases

ProteinModelPortaliA1WT09.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 312Lyase_1InterPro annotationAdd BLAST299
Domaini331 – 445ASL_CInterPro annotationAdd BLAST115

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4107QTF. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000252916.
KOiK01756.
OMAiTQVNPCD.
OrthoDBiPOG091H01RB.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
InterProiIPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR004769. Pur_lyase.
IPR013539. PurB_C.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF08328. ASL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00928. purB. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A1WT09-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELDTLTALA PIDGRYADKT DDLRPLLSEY GLIRHRVVVE VRWLQALAKE
60 70 80 90 100
PGITEVPPLS TDATAFLEQL LAGFDTQQAR RVKAIEATTN HDVKAVEYYL
110 120 130 140 150
KERLAEHEEL AARAEFVHFA CTSEDINNLA WACMLRGARD EVLLPALDGI
160 170 180 190 200
IEQLRQLAHA QAEQPMLSRT HGQTASPTTL GKEIANVVHR LREQRQRLAD
210 220 230 240 250
VQPLGKINGA VGNFNAHLIA YPEVDWPALG RRYVQGLGLG WNPYTTQIEP
260 270 280 290 300
HDWIAELFDA ISRVNTVLLD LSRDVWGYIS LGYFGQRVVA GEVGSSTMPH
310 320 330 340 350
KVNPIDFENA EGNLGVSSAL LEHLARKLPV SRWQRDLSDS TALRTVSLGI
360 370 380 390 400
AHTLIALKSL EKGVGKLEAN PHRLDDDLEA AWEVLAEAIQ TVMRRYGADE
410 420 430 440 450
PYEQLKKLTR GRKIDEQAVR AFIEGLDLPE EAKAQLRGLT PRTYLGNAAS

QARAV
Length:455
Mass (Da):50,611
Last modified:February 6, 2007 - v1
Checksum:i918BD390F3463867
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000544 Genomic DNA. Translation: ABM60821.1.
RefSeqiWP_011812844.1. NC_008789.1.

Genome annotation databases

EnsemblBacteriaiABM60821; ABM60821; Hhal_0026.
KEGGihha:Hhal_0026.
PATRICi22094305. VBIHalHal112047_0026.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000544 Genomic DNA. Translation: ABM60821.1.
RefSeqiWP_011812844.1. NC_008789.1.

3D structure databases

ProteinModelPortaliA1WT09.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi349124.Hhal_0026.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABM60821; ABM60821; Hhal_0026.
KEGGihha:Hhal_0026.
PATRICi22094305. VBIHalHal112047_0026.

Phylogenomic databases

eggNOGiENOG4107QTF. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000252916.
KOiK01756.
OMAiTQVNPCD.
OrthoDBiPOG091H01RB.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciHHAL349124:GI3I-28-MONOMER.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
InterProiIPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR004769. Pur_lyase.
IPR013539. PurB_C.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF08328. ASL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00928. purB. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiA1WT09_HALHL
AccessioniPrimary (citable) accession number: A1WT09
Entry historyi
Integrated into UniProtKB/TrEMBL: February 6, 2007
Last sequence update: February 6, 2007
Last modified: October 5, 2016
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference 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.