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Protein

Adenylosuccinate lyase

Gene

Mevan_0294

Organism
Methanococcus vannielii (strain SB / ATCC 35089 / DSM 1224)
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 (Mevan_0294)
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 (Mevan_0294)
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

BioCyciMVAN406327:GI04-298-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:Mevan_0294Imported
OrganismiMethanococcus vannielii (strain SB / ATCC 35089 / DSM 1224)Imported
Taxonomic identifieri406327 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus
Proteomesi
  • UP000001107 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi406327.Mevan_0294.

Structurei

3D structure databases

ProteinModelPortaliA6UNY1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini362 – 44281ADSL_CInterPro annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiarCOG01747. Archaea.
COG0015. LUCA.
HOGENOMiHOG000033912.
KOiK01756.
OMAiVMWMANV.

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.

A6UNY1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIHPIDFRY GTLEMKRVWE EETKLQKMLE VEAALAMAEA ELEMIPMEAA
60 70 80 90 100
VEINKKKSTE FVKLERVKEI ESVTKHDVVS VVKAFAEQCE GNAGEYIHFG
110 120 130 140 150
STSNDIIDTA QSLQFKDACD IILEKLKTLR SELLKKAEGH KNTVCIGRTH
160 170 180 190 200
GQHAVPTTYG MKFALWATEI QRHVERLETC KKRLCVSMIT GAVGTMAAIG
210 220 230 240 250
ENGILVHNRV GEILELTPVL ISNQVVQRDR HGEFMSILAL IAQTLNKIGI
260 270 280 290 300
TVRSMQRSEI KELEEEFDAS KQTGSSTMPH KRNPITFEQI CGLSRIVKAN
310 320 330 340 350
ALAEFDNIPL WEERDLTNSS SERCLFPESC VIIDHILNLS IKGMRKLTVN
360 370 380 390 400
IENVNKNLEL TKGLIMAERV MMFLANSGMG RQTGHETVRR CAMKAHDEGR
410 420 430 440
HLKEVLLEEP EIMKYVSVAE IEKMFDYTTY IGLAPEIVEN VIIESKNWK
Length:449
Mass (Da):50,786
Last modified:August 21, 2007 - v1
Checksum:i2EE2D8F93D88709D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000742 Genomic DNA. Translation: ABR54203.1.
RefSeqiWP_011972106.1. NC_009634.1.

Genome annotation databases

EnsemblBacteriaiABR54203; ABR54203; Mevan_0294.
GeneIDi5325496.
KEGGimvn:Mevan_0294.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000742 Genomic DNA. Translation: ABR54203.1.
RefSeqiWP_011972106.1. NC_009634.1.

3D structure databases

ProteinModelPortaliA6UNY1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi406327.Mevan_0294.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABR54203; ABR54203; Mevan_0294.
GeneIDi5325496.
KEGGimvn:Mevan_0294.

Phylogenomic databases

eggNOGiarCOG01747. Archaea.
COG0015. LUCA.
HOGENOMiHOG000033912.
KOiK01756.
OMAiVMWMANV.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciMVAN406327:GI04-298-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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SB / ATCC 35089 / DSM 1224Imported.

Entry informationi

Entry nameiA6UNY1_METVS
AccessioniPrimary (citable) accession number: A6UNY1
Entry historyi
Integrated into UniProtKB/TrEMBL: August 21, 2007
Last sequence update: August 21, 2007
Last modified: July 6, 2016
This is version 48 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.