Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Adenylosuccinate lyase

Gene

SSU05_0039

Organism
Streptococcus suis (strain 05ZYH33)
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 (SSU05_0039)
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 (SSU05_0039)
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

BioCyciSSUI391295:GHI8-105-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:SSU05_0039Imported
OrganismiStreptococcus suis (strain 05ZYH33)Imported
Taxonomic identifieri391295 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000000243 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi391295.SSU05_0039.

Structurei

3D structure databases

ProteinModelPortaliA4VSC2.
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.

A4VSC2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIERYSRPEM AAIWSEENKY EAWLEVEILA DEAWAELGEI PKEDVALIRE
60 70 80 90 100
KATFDIDRIL EIEEETRHDV VAFTRAVSES LGEERKWVHY GLTSTDVVDT
110 120 130 140 150
AYGYLYKQAN DIIRRDLENF TTIIADKARE HKYTIMMGRT HGVHAEPTTF
160 170 180 190 200
GLKLATWYSE MKRNMERFDV AAKGVEAGKI SGAVGNFANI PPFVEEYVCG
210 220 230 240 250
KLGIRPQEIS TQVLPRDLHA EYFSALALIA TSIERMATEI RGLQKSEQRE
260 270 280 290 300
VEEYFAKGQK GSSAMPHKRN PIGSENMTGL ARVVRGHLVT AFENVALWHE
310 320 330 340 350
RDISHSSAER IITPDTTILI NYMLNRFGNI VKNLTVFPEN MKRNMESTFG
360 370 380 390 400
LIYSQRVMLS LIEKGMTREE AYDLVQPKTA QSWDNQVDFK PLLEADERVT
410 420 430
AKLSQEEIDE LFNPDYYAKR VDDIFERLGL
Length:430
Mass (Da):49,334
Last modified:May 29, 2007 - v1
Checksum:i8793D1F300042979
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000407 Genomic DNA. Translation: ABP89011.1.

Genome annotation databases

EnsemblBacteriaiABP89011; ABP89011; SSU05_0039.
KEGGissu:SSU05_0039.
PATRICi19771784. VBIStrSui128929_0037.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000407 Genomic DNA. Translation: ABP89011.1.

3D structure databases

ProteinModelPortaliA4VSC2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi391295.SSU05_0039.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABP89011; ABP89011; SSU05_0039.
KEGGissu:SSU05_0039.
PATRICi19771784. VBIStrSui128929_0037.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciSSUI391295:GHI8-105-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. "A glimpse of streptococcal toxic shock syndrome from comparative genomics of S. suis 2 Chinese isolates."
    BGI
    Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X., Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J., Dong Y.
    , Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F., Yang R., Wang J., Yu J.
    PLoS ONE 2:E315-E315(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 05ZYH33Imported.

Entry informationi

Entry nameiA4VSC2_STRSY
AccessioniPrimary (citable) accession number: A4VSC2
Entry historyi
Integrated into UniProtKB/TrEMBL: May 29, 2007
Last sequence update: May 29, 2007
Last modified: July 6, 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.