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Protein

Adenylosuccinate lyase

Gene

Sden_1826

Organism
Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013)
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 (Sden_1826)
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 (Sden_1826)
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

BioCyciSDEN318161:GHKQ-1893-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:Sden_1826Imported
OrganismiShewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013)Imported
Taxonomic identifieri318161 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000001982 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi318161.Sden_1826.

Structurei

3D structure databases

ProteinModelPortaliQ12N66.
SMRiQ12N66. Positions 1-455.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 312299Lyase_1InterPro annotationAdd
BLAST
Domaini331 – 445115ASL_CInterPro annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4107QTF. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000252916.
KOiK01756.
OMAiTFGKEMA.
OrthoDBiEOG686NDB.

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.

Q12N66-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLSALTAIS PVDGRYGSKT ASLRGIFSEF GLTKYRVQVE INWLKLLSSC
60 70 80 90 100
PEIEEVPPFS ETALALLDSI KDNFSEQDAL RVKAIESTTN HDVKAVEYFI
110 120 130 140 150
KEQIASSPEL VAIDEFVHFA CTSEDINNLS HALMLKEARE QVLVPHCQQI
160 170 180 190 200
IDGIKKLARD NKSVPLMSRT HGQPASPSTL GKEMANVAVR LERQLKQIES
210 220 230 240 250
VEIMGKINGA VGNYNAHISA YPEVNWHELS QRFVTSLGVV WNAYTTQIEP
260 270 280 290 300
HDYIAELFDA VTRFNTILLD FDRDIWGYIA LGHFKQRTIA GEIGSSTMPH
310 320 330 340 350
KVNPIDFENS EGNLGIANAI LQHLSAKLPV SRWQRDLTDS TVLRNLGVGL
360 370 380 390 400
AHSLIAYQST LKGISKLEVN EAQLLAELDK NWEVLAEPVQ TVMRRYGIEK
410 420 430 440 450
PYEKLKELTR GKRIDAQQLA VFIDGLALPD DVKTELKKMT PANYIGRAEA

FVDELN
Length:456
Mass (Da):50,983
Last modified:August 22, 2006 - v1
Checksum:i9411FAABE6B72D8A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000302 Genomic DNA. Translation: ABE55110.1.
RefSeqiWP_011496267.1. NC_007954.1.

Genome annotation databases

EnsemblBacteriaiABE55110; ABE55110; Sden_1826.
KEGGisdn:Sden_1826.
PATRICi23489545. VBISheDen79529_1941.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000302 Genomic DNA. Translation: ABE55110.1.
RefSeqiWP_011496267.1. NC_007954.1.

3D structure databases

ProteinModelPortaliQ12N66.
SMRiQ12N66. Positions 1-455.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi318161.Sden_1826.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE55110; ABE55110; Sden_1826.
KEGGisdn:Sden_1826.
PATRICi23489545. VBISheDen79529_1941.

Phylogenomic databases

eggNOGiENOG4107QTF. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000252916.
KOiK01756.
OMAiTFGKEMA.
OrthoDBiEOG686NDB.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciSDEN318161:GHKQ-1893-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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: OS217 / ATCC BAA-1090 / DSM 15013Imported.

Entry informationi

Entry nameiQ12N66_SHEDO
AccessioniPrimary (citable) accession number: Q12N66
Entry historyi
Integrated into UniProtKB/TrEMBL: August 22, 2006
Last sequence update: August 22, 2006
Last modified: July 6, 2016
This is version 64 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.