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Protein

Adenylosuccinate lyase

Gene

Msm_1151

Organism
Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)
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 (Msm_1151)
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 (Msm_1151)
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

BioCyciMSMI420247:GHWZ-1185-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:Msm_1151Imported
OrganismiMethanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)Imported
Taxonomic identifieri420247 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanobrevibacter
Proteomesi
  • UP000001992 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi420247.Msm_1151.

Structurei

3D structure databases

ProteinModelPortaliA5UMC8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini362 – 442ADSL_CInterPro annotationAdd BLAST81

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiarCOG01747. Archaea.
COG0015. LUCA.
HOGENOMiHOG000033912.
KOiK01756.
OMAiAVHPIDY.

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.

A5UMC8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIHPIEYRY GTPEMKSIWE TENKLQRKLD VESALAQAEG KLGIIPQEVA
60 70 80 90 100
DEIAAKANTK YVKLERVDEI EAQTKHDIAA LVKAIGEVCD NDAGEYVHFG
110 120 130 140 150
ATSNDVVDSS NSLLLNDSIE VLKEKVERLT KIMLDLTKEN IDKVCIGRTH
160 170 180 190 200
GQHALPTTYG MKFGIWADEL HRQYERLENA QKNVCVAMMD GAVGTTAALG
210 220 230 240 250
EDGWKIHKEV ANILGLPAAT ITNQVVQRDN HVEFISTLAN IASTLDKIAL
260 270 280 290 300
EIRSLQRTEL MELGEYFDPE KQVGSSTMPH KMNPITAERI CGVARIVKSF
310 320 330 340 350
VNAALDNNPL WHERDLTNSS CERIMFPESC ILTDYILSLT IKLMSNLVFY
360 370 380 390 400
DENIERNLNL TNGLIMAERL MAELTRSGMG KQTAYGIVRR NAIKANKEGG
410 420 430 440 450
LLGELILEEE DVQKYLTPED VEKIMNPHTY IGSSKTIINE LLEQSKEWFK
Length:450
Mass (Da):50,492
Last modified:July 10, 2007 - v1
Checksum:i91BC5A274B0FA748
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000678 Genomic DNA. Translation: ABQ87356.1.
RefSeqiWP_004032787.1. NC_009515.1.

Genome annotation databases

EnsemblBacteriaiABQ87356; ABQ87356; Msm_1151.
GeneIDi5216889.
KEGGimsi:Msm_1151.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000678 Genomic DNA. Translation: ABQ87356.1.
RefSeqiWP_004032787.1. NC_009515.1.

3D structure databases

ProteinModelPortaliA5UMC8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi420247.Msm_1151.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABQ87356; ABQ87356; Msm_1151.
GeneIDi5216889.
KEGGimsi:Msm_1151.

Phylogenomic databases

eggNOGiarCOG01747. Archaea.
COG0015. LUCA.
HOGENOMiHOG000033912.
KOiK01756.
OMAiAVHPIDY.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciMSMI420247:GHWZ-1185-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 nameiA5UMC8_METS3
AccessioniPrimary (citable) accession number: A5UMC8
Entry historyi
Integrated into UniProtKB/TrEMBL: July 10, 2007
Last sequence update: July 10, 2007
Last modified: September 7, 2016
This is version 51 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.