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Protein

Adenylosuccinate lyase

Gene

purB

Organism
Aeromonas salmonicida (strain A449)
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 (purB)
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 (purB)
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

BioCyciASAL382245:GJJN-1383-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
Name:purBImported
Ordered Locus Names:ASA_1389Imported
OrganismiAeromonas salmonicida (strain A449)Imported
Taxonomic identifieri382245 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas
Proteomesi
  • UP000000225 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi382245.ASA_1389.

Structurei

3D structure databases

ProteinModelPortaliA4SKR8.
SMRiA4SKR8. Positions 1-456.
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.

A4SKR8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELSALTAVS PIDGRYGDKA DALRPIFSEF GLLRFRVEVE VRWLQKLASH
60 70 80 90 100
VGIPEVPALS AAANALLDGI VSNFNESDAA RIKQIERTTN HDVKAVEYFL
110 120 130 140 150
KEKVEVNPEL AAVSEFIHFA CTSEDINNNS HGLMLKTARD EVIKPYCEKL
160 170 180 190 200
IRELKRLAHE YRDMPLLSRT HGQPATPSTM GKEMANVAYR LERQFKQIMA
210 220 230 240 250
VEILGKINGA VGNYNAHVSA YPEVDWHQFS EEFVTSLGLN WNPYTTQIEP
260 270 280 290 300
HDYIAELFYA MARFNTILID FDRDVWGYIS LGHFKQRTVA GEIGSSTMPH
310 320 330 340 350
KVNPIDFENS EGNLGLANAV FQHLASKLPI SRWQRDLTDS TVLRNLGVAV
360 370 380 390 400
GYSLIAYQAT LKGISKLEAN AGAMAADLDA NWEVLAEPIQ TVMRRYGIEK
410 420 430 440 450
PYEKLKELTR GRRVDAEGMR TFIDTLELPE HVKVELKKLT PANYIGQAQR

LVDLLK
Length:456
Mass (Da):51,346
Last modified:May 15, 2007 - v1
Checksum:iEAB0A6EBEC5134B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000644 Genomic DNA. Translation: ABO89490.1.
RefSeqiWP_005319182.1. NC_009348.1.

Genome annotation databases

EnsemblBacteriaiABO89490; ABO89490; ASA_1389.
GeneIDi4997330.
KEGGiasa:ASA_1389.
PATRICi20789158. VBIAerSal2987_1384.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000644 Genomic DNA. Translation: ABO89490.1.
RefSeqiWP_005319182.1. NC_009348.1.

3D structure databases

ProteinModelPortaliA4SKR8.
SMRiA4SKR8. Positions 1-456.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi382245.ASA_1389.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABO89490; ABO89490; ASA_1389.
GeneIDi4997330.
KEGGiasa:ASA_1389.
PATRICi20789158. VBIAerSal2987_1384.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciASAL382245:GJJN-1383-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. "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into the evolution of a fish pathogen."
    Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J., Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C., Brown L.L.
    BMC Genomics 9:427-427(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: A449Imported.

Entry informationi

Entry nameiA4SKR8_AERS4
AccessioniPrimary (citable) accession number: A4SKR8
Entry historyi
Integrated into UniProtKB/TrEMBL: May 15, 2007
Last sequence update: May 15, 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.