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Protein

Adenylosuccinate lyase

Gene

Memar_0781

Organism
Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)
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
N6-(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 (Memar_0781)
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 (Memar_0781)
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

Keywordsi

Molecular functionLyaseUniRule annotationImported
Biological processPurine biosynthesisUniRule annotation

Enzyme and pathway databases

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:Memar_0781Imported
OrganismiMethanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)Imported
Taxonomic identifieri368407 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanomicrobiaceaeMethanoculleus
Proteomesi
  • UP000002146 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi368407.Memar_0781.

Structurei

3D structure databases

ProteinModelPortaliA3CTL4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini358 – 438ADSL_CInterPro annotationAdd BLAST81

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiarCOG01747. Archaea.
COG0015. LUCA.
HOGENOMiHOG000033912.
KOiK01756.
OMAiASSCEKI.
OrthoDBiPOG093Z04ZT.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
InterProiView protein in InterPro
IPR019468. 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.
PfamiView protein in Pfam
PF10397. ADSL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
PRINTSiPR00149. FUMRATELYASE.
SMARTiView protein in SMART
SM00998. ADSL_C. 1 hit.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00928. purB. 1 hit.
PROSITEiView protein in PROSITE
PS00163. FUMARATE_LYASES. 1 hit.

Sequencei

Sequence statusi: Complete.

A3CTL4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATHPIDYRY GTPEMRAVWS EENRFRAIVT AEVALARAEA AHGMIPREDA
60 70 80 90 100
ETIATRAPEA RLERAKEIEA EINHDMMAIV KAVTEVCGDA GRWIHYGATS
110 120 130 140 150
NDILDTATAL QVRESLMLIE EKLGKLLCVL LARSAETKTL VCAGRTHGQI
160 170 180 190 200
GVPTTYGLRF AIWASEVSRH IERLRQMRPR VVVGQLTGAV GTQAALGDAG
210 220 230 240 250
IEVQETMMEF LGIGAVDVSN QIIARDRYAE YFMLLANIAT TLDKIGLELR
260 270 280 290 300
LMQRSEIGEL AEAFGKKQVG SSTMPHKRNP IKSEQVCGLA RIVRSAVEPA
310 320 330 340 350
LQNNVLWDER DLTNSSPERA LFPEASVLAD HILNVMINVM EGLEFNKANI
360 370 380 390 400
RKNLMLLRGV NLAESVMIDL TRRGMSRQEA HEAMRTASMQ ALAEDRDLSQ
410 420 430 440
VLGERPEVTK FVTREELNAL LDPDAYIGTA VRQVERLIEK LTPLCR
Length:446
Mass (Da):49,564
Last modified:March 20, 2007 - v1
Checksum:iBE2343C0A097685A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000562 Genomic DNA. Translation: ABN56714.1.
RefSeqiWP_011843625.1. NC_009051.1.

Genome annotation databases

EnsemblBacteriaiABN56714; ABN56714; Memar_0781.
GeneIDi4846515.
KEGGimem:Memar_0781.

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.

Entry informationi

Entry nameiA3CTL4_METMJ
AccessioniPrimary (citable) accession number: A3CTL4
Entry historyiIntegrated into UniProtKB/TrEMBL: March 20, 2007
Last sequence update: March 20, 2007
Last modified: June 7, 2017
This is version 65 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported