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Protein

Adenylosuccinate lyase

Gene

Shew_1558

Organism
Shewanella loihica (strain ATCC BAA-1088 / PV-4)
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 (Shew_1558)
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 (Shew_1558)
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

BioCyciSLOI323850:GHQJ-1608-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:Shew_1558Imported
OrganismiShewanella loihica (strain ATCC BAA-1088 / PV-4)Imported
Taxonomic identifieri323850 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000001558 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi323850.Shew_1558.

Structurei

3D structure databases

ProteinModelPortaliA3QD77.
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.

A3QD77-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELSALTAIS PVDGRYGSKT ASLRGIFSEY GLTKYRVQVE INWLKLLSSC
60 70 80 90 100
PEIEEVPPFS EVALALLDQI KDNFSEEDAL RVKTIEATTN HDVKAVEYFI
110 120 130 140 150
KEKIADNSEL TSIGEFVHFA CTSEDINNLS HGLMLSEARE QVLVPYCQQI
160 170 180 190 200
VDGVKKLASE YRSVPLMSRT HGQPASPSTL GKEMANVAVR LERQLKQIQA
210 220 230 240 250
VEIMGKINGA VGNYNAHLSA YPEVDWHTLS ERFVTSLGLN WNPYTTQIEP
260 270 280 290 300
HDYIAELFDA VARFNTVLID FDRDIWGYIA LGHFKQKTIA GEIGSSTMPH
310 320 330 340 350
KVNPIDFENS EGNLGIANAL MQHLAAKLPV SRWQRDLTDS TVLRNLGVGM
360 370 380 390 400
AHSLIAYQAT LKGICKLEVN EAHLREELDQ NWEVLAEPVQ TVMRRYGIEK
410 420 430 440 450
PYEKLKELTR GKRIDGEQLA QFIDTLELPS DVKLELKKMT PANYIGRAEA

FVDDLK
Length:456
Mass (Da):51,209
Last modified:April 17, 2007 - v1
Checksum:i24F4EFF3ED57D87A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000606 Genomic DNA. Translation: ABO23425.1.
RefSeqiWP_011865357.1. NC_009092.1.

Genome annotation databases

EnsemblBacteriaiABO23425; ABO23425; Shew_1558.
KEGGislo:Shew_1558.
PATRICi23514951. VBISheLoi132094_1562.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000606 Genomic DNA. Translation: ABO23425.1.
RefSeqiWP_011865357.1. NC_009092.1.

3D structure databases

ProteinModelPortaliA3QD77.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi323850.Shew_1558.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABO23425; ABO23425; Shew_1558.
KEGGislo:Shew_1558.
PATRICi23514951. VBISheLoi132094_1562.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciSLOI323850:GHQJ-1608-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 nameiA3QD77_SHELP
AccessioniPrimary (citable) accession number: A3QD77
Entry historyi
Integrated into UniProtKB/TrEMBL: April 17, 2007
Last sequence update: April 17, 2007
Last modified: November 2, 2016
This is version 61 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.