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Protein

Adenylosuccinate lyase

Gene

MmarC7_0216

Organism
Methanococcus maripaludis (strain C7 / ATCC BAA-1331)
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 (MmarC7_0216)
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 (MmarC7_0216)
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

BioCyciMMAR426368:GHHL-217-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:MmarC7_0216Imported
OrganismiMethanococcus maripaludis (strain C7 / ATCC BAA-1331)Imported
Taxonomic identifieri426368 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus
Proteomesi
  • UP000002298 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi426368.MmarC7_0216.

Structurei

3D structure databases

ProteinModelPortaliA6VFR0.
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.
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.

A6VFR0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIHPIDFRY GTPEMKKVWE EETKLQKMLE VEAALAMAEA ELGMIPKEAA
60 70 80 90 100
EEINRKKSTE FVKLERVKEI EMATRHDVVS VVKAFAEQCE GDAGEYIHFG
110 120 130 140 150
STSNDIIDTA QSLQFKDAFE VLEEKLKTLR GELLKKAEEH KNTVCIGRTH
160 170 180 190 200
GQHAVPTTYG MKFALWATEI QRHVERLESS KKRLCVSMIT GAVGTMAAIG
210 220 230 240 250
ENGILVHNRV GEILELDPVL ISNQVVQRDR HGEFMATLAL IAQTLNKIGV
260 270 280 290 300
TVRSMQRSEI KELEEEFDAS KQTGSSTMPH KRNPITFEQI CGLSRIVKAN
310 320 330 340 350
ALAEFDNIPL WEERDLTNSS SERCLFPESC VILDHILNLS IKGMRKLSVN
360 370 380 390 400
LENVNKNLEM TKGLIMAERV MMFLANSGMG RQTGHETVRR CAMKAHDEGR
410 420 430 440
HLKEVLLEEP EVMKYVSLEE IEKMFDYKTY IGLAPEIVEN VLNEAKNWE
Length:449
Mass (Da):50,889
Last modified:August 21, 2007 - v1
Checksum:i884FF32F4EF7038E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000745 Genomic DNA. Translation: ABR65286.1.
RefSeqiWP_011976623.1. NC_009637.1.

Genome annotation databases

EnsemblBacteriaiABR65286; ABR65286; MmarC7_0216.
GeneIDi5328958.
KEGGimmz:MmarC7_0216.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000745 Genomic DNA. Translation: ABR65286.1.
RefSeqiWP_011976623.1. NC_009637.1.

3D structure databases

ProteinModelPortaliA6VFR0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi426368.MmarC7_0216.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABR65286; ABR65286; MmarC7_0216.
GeneIDi5328958.
KEGGimmz:MmarC7_0216.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciMMAR426368:GHHL-217-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 nameiA6VFR0_METM7
AccessioniPrimary (citable) accession number: A6VFR0
Entry historyi
Integrated into UniProtKB/TrEMBL: August 21, 2007
Last sequence update: August 21, 2007
Last modified: July 6, 2016
This is version 52 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.