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Protein

Adenylosuccinate lyase

Gene

Mlab_1121

Organism
Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)
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 (Mlab_1121)
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. no protein annotated in this organism
  2. Adenylosuccinate lyase (Mlab_1121)
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

BioCyciMLAB410358:GH7C-1157-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:Mlab_1121Imported
OrganismiMethanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)Imported
Taxonomic identifieri410358 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanocorpusculaceaeMethanocorpusculum
Proteomesi
  • UP000000365 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi410358.Mlab_1121.

Structurei

3D structure databases

ProteinModelPortaliA2SSI4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini358 – 43881ADSL_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.

A2SSI4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIHPIDFRY GTPEMKRVWS EDNRFTCIVR AEVALAHAQG VVGMIPAEDA
60 70 80 90 100
AIIEKNALSA SRVRAKEIEA EISHDTMAIT RAISEVCGDA GRWIHYGATS
110 120 130 140 150
NDILDTATGL QLKEAYDLLE KKLSTLMGVL LKRAEETKNL ICIARTHGQQ
160 170 180 190 200
GVPTTYGLRF AIWASEVSRH LIRLRESRPR VVVGQMTGAV GTMAAMGEHG
210 220 230 240 250
IEVQAEMMKY LGIGSVDVSS QVISRDRYAE YIFLLANIAT TLDKVGIEVR
260 270 280 290 300
TLQRTEIGEV EESFSKKQVG SSTMPHKRNP IKSEQVCGLA RIVRSMVEPA
310 320 330 340 350
LLNNTLWDER DLTNSSAERI TFLETSILCD HCLQVMTGVI ENLTINTEAV
360 370 380 390 400
ERNLRYLHGI NLAESVMIEL TKRGMKREDA HETIREASME ALSAKMPLAE
410 420 430 440
ILAAKPEVTE YVSAEEIAKL LKPESYAGLA GVQVENLIRK LAPYCTL
Length:447
Mass (Da):49,538
Last modified:March 6, 2007 - v1
Checksum:iA5DAA233896ECAA5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000559 Genomic DNA. Translation: ABN07290.1.
RefSeqiWP_011833493.1. NC_008942.1.

Genome annotation databases

EnsemblBacteriaiABN07290; ABN07290; Mlab_1121.
GeneIDi4795529.
KEGGimla:Mlab_1121.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000559 Genomic DNA. Translation: ABN07290.1.
RefSeqiWP_011833493.1. NC_008942.1.

3D structure databases

ProteinModelPortaliA2SSI4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi410358.Mlab_1121.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABN07290; ABN07290; Mlab_1121.
GeneIDi4795529.
KEGGimla:Mlab_1121.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciMLAB410358:GH7C-1157-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: ATCC 43576 / DSM 4855 / ZImported.

Entry informationi

Entry nameiA2SSI4_METLZ
AccessioniPrimary (citable) accession number: A2SSI4
Entry historyi
Integrated into UniProtKB/TrEMBL: March 6, 2007
Last sequence update: March 6, 2007
Last modified: July 6, 2016
This is version 60 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.