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Protein

Adenylosuccinate lyase

Gene

Patl_2381

Organism
Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087)
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 (Patl_2381)
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 (Patl_2381)
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

BioCyciPATL342610:GHGT-2421-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:Patl_2381Imported
OrganismiPseudoalteromonas atlantica (strain T6c / ATCC BAA-1087)Imported
Taxonomic identifieri342610 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas
Proteomesi
  • UP000001981 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi342610.Patl_2381.

Structurei

3D structure databases

ProteinModelPortaliQ15T91.
SMRiQ15T91. 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.
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.

Q15T91-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQLSALTAVS PIDGRYAEKT AELRSIFSEF GLLKYRVQVE VRWLQKLAST
60 70 80 90 100
ASIEQVPAFS AEANTLLDNI VATFDESHAG RIKEIERTTN HDVKAVEYFL
110 120 130 140 150
KEQVADNAEL NAVNEFIHFA CTSEDINNMS HALMLKEARD SIILPYSDKL
160 170 180 190 200
ISELKRLAKE YQNIPMMART HGQPASPTTM GKEMANVAYR LERQRNQIAN
210 220 230 240 250
VAVLGKVNGA VGNYNAHLSA YPSLDWAQFA EEFVASLGVT LNPFTTQIEP
260 270 280 290 300
HDYIAELFDA IARFNTILID FNRDVWGYIA LGHFKQRTIA GEIGSSTMPH
310 320 330 340 350
KVNPIDFENS EGNLGLANAL FGHLATKLPV SRWQRDLTDS TVLRNLGVGV
360 370 380 390 400
GYAIIAYQAT LKGISKLQVN EQSLLDELDN NWELLAEPIQ TVMRRYGIEK
410 420 430 440 450
PYEKLKELTR GKKVNQQIMA EFIDGLELPD EAKTQLKALT PSNYIGQAVE

LVNQI
Length:455
Mass (Da):50,932
Last modified:July 25, 2006 - v1
Checksum:i83F3C4817C912BCC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000388 Genomic DNA. Translation: ABG40897.1.
RefSeqiWP_011575175.1. NC_008228.1.

Genome annotation databases

EnsemblBacteriaiABG40897; ABG40897; Patl_2381.
KEGGipat:Patl_2381.
PATRICi23049920. VBIPseAtl25434_2543.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000388 Genomic DNA. Translation: ABG40897.1.
RefSeqiWP_011575175.1. NC_008228.1.

3D structure databases

ProteinModelPortaliQ15T91.
SMRiQ15T91. Positions 1-455.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi342610.Patl_2381.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABG40897; ABG40897; Patl_2381.
KEGGipat:Patl_2381.
PATRICi23049920. VBIPseAtl25434_2543.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciPATL342610:GHGT-2421-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 nameiQ15T91_PSEA6
AccessioniPrimary (citable) accession number: Q15T91
Entry historyi
Integrated into UniProtKB/TrEMBL: July 25, 2006
Last sequence update: July 25, 2006
Last modified: September 7, 2016
This is version 69 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.