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Protein

Adenylosuccinate lyase

Gene

Pmob_0219

Organism
Petrotoga mobilis (strain DSM 10674 / SJ95)
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 (Pmob_0219)
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 (Pmob_0219)
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

BioCyciPMOB403833:GH51-219-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:Pmob_0219Imported
OrganismiPetrotoga mobilis (strain DSM 10674 / SJ95)Imported
Taxonomic identifieri403833 [NCBI]
Taxonomic lineageiBacteriaThermotogaePetrotogalesPetrotogaceaePetrotoga
Proteomesi
  • UP000000789 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi403833.Pmob_0219.

Structurei

3D structure databases

ProteinModelPortaliA9BJ20.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini350 – 431ADSL_CInterPro annotationAdd BLAST82

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C83. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000033912.
KOiK01756.
OMAiVQENAMK.
OrthoDBiPOG091H0168.

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.

A9BJ20-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLIERYSLSP IKDIWTLDAQ YKRWLEVEIA VIEAFEELNL APKGTSQNIR
60 70 80 90 100
QKAKLDVQKI LDTEKIVDHD VIAFIKVVTE DMGDEARYFH KGLTSSDVVD
110 120 130 140 150
TALSLAIKRA EEIILDELTQ YIANLKKLAV DHKYTIIVGR THGVHAEPTS
160 170 180 190 200
FGLKILGFVA EEERNKERLE KAIDNISQGK LSGAVGNYAN IEPKVEEIAL
210 220 230 240 250
KKLNLRPCKV STQVLPRDLH AEFFSVLAMI GSSIERLAIE IRHLQKTEVL
260 270 280 290 300
EVEEPFKKEQ RGSSAMPHKK NPILCERLTG MSRMLRSYLS SAYENISLWH
310 320 330 340 350
ERDISHSSVE RVFIPDATML TYYMLNKANY LVENLVVHKD RMKENIEKSY
360 370 380 390 400
NLIYSQRVLL KLVELGVSRE EAYKIVQENA MKAWNERRDF KAILLEDNRV
410 420 430
KAKLSDKEAF EDIFSPDYYL KNINEIYERF EL
Length:432
Mass (Da):49,936
Last modified:January 15, 2008 - v1
Checksum:i62CED7D974EE6419
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000879 Genomic DNA. Translation: ABX30965.1.

Genome annotation databases

EnsemblBacteriaiABX30965; ABX30965; Pmob_0219.
KEGGipmo:Pmob_0219.
PATRICi22917948. VBIPetMob40494_0228.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000879 Genomic DNA. Translation: ABX30965.1.

3D structure databases

ProteinModelPortaliA9BJ20.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi403833.Pmob_0219.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABX30965; ABX30965; Pmob_0219.
KEGGipmo:Pmob_0219.
PATRICi22917948. VBIPetMob40494_0228.

Phylogenomic databases

eggNOGiENOG4105C83. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000033912.
KOiK01756.
OMAiVQENAMK.
OrthoDBiPOG091H0168.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciPMOB403833:GH51-219-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...

Entry informationi

Entry nameiA9BJ20_PETMO
AccessioniPrimary (citable) accession number: A9BJ20
Entry historyi
Integrated into UniProtKB/TrEMBL: January 15, 2008
Last sequence update: January 15, 2008
Last modified: November 2, 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.