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Protein

Adenylosuccinate lyase

Gene

purB

Organism
Dichelobacter nodosus (strain VCS1703A)
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 (purB)
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 (purB)
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

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
Name:purBImported
Ordered Locus Names:DNO_0667Imported
OrganismiDichelobacter nodosus (strain VCS1703A)Imported
Taxonomic identifieri246195 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaCardiobacterialesCardiobacteriaceaeDichelobacter
Proteomesi
  • UP000000248 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi246195.DNO_0667.

Structurei

3D structure databases

ProteinModelPortaliA5EV77.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 313Lyase_1InterPro annotationAdd BLAST298
Domaini332 – 446ASL_CInterPro annotationAdd BLAST115

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4107QTF. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000252916.
KOiK01756.
OMAiTQVNPCD.
OrthoDBiPOG091H01RB.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
InterProiIPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR004769. Pur_lyase.
IPR013539. PurB_C.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF08328. ASL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00928. purB. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A5EV77-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAQNHALTA ISPIDGRYAE KTAVLRTIFS EYGLIKYRYR VELQWLRFLA
60 70 80 90 100
NHDGIPELQA LSPSAEQFLQ QLSEQFDEHK ALEIKAIEKT TNHDVKAVEY
110 120 130 140 150
QLKKDLATHD ELATKIEFVH FACTSEDINN LSYALMLKDG RDVLLQMYQE
160 170 180 190 200
ISNQIKQIAL AEQNTAFLAH THGQPASPTT LGKEFANVAF RIKRQLSLLD
210 220 230 240 250
SQEMLGKING AVGNFNAHHV AYPDVDWQRS AQQFVEQLGL TYNPLTTQIE
260 270 280 290 300
PHDYIAELLH TLSRINLILL DFCRDVWTYI SLNYFKQKVI SGEVGSSTMP
310 320 330 340 350
HKVNPIDFEN AEGNFGLANA LAEHLAHKLP ISRMQRDLTD STVLRSLGSV
360 370 380 390 400
FAYTVIALAS LKKGLTKLET NHAAIAADLA ANPEVLAEAV QTVMRRYAIP
410 420 430 440 450
EPYEKLKALT RGQKITPEIL VTFIDGLDLP EEVKARLRGL TPKDYVGLAQ

KLAQCVQ
Length:457
Mass (Da):51,335
Last modified:June 12, 2007 - v1
Checksum:i3A8FE2C5E36214A5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000513 Genomic DNA. Translation: ABQ13438.1.
RefSeqiWP_012031000.1. NC_009446.1.

Genome annotation databases

EnsemblBacteriaiABQ13438; ABQ13438; DNO_0667.
KEGGidno:DNO_0667.
PATRICi21785656. VBIDicNod48475_0671.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000513 Genomic DNA. Translation: ABQ13438.1.
RefSeqiWP_012031000.1. NC_009446.1.

3D structure databases

ProteinModelPortaliA5EV77.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246195.DNO_0667.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABQ13438; ABQ13438; DNO_0667.
KEGGidno:DNO_0667.
PATRICi21785656. VBIDicNod48475_0671.

Phylogenomic databases

eggNOGiENOG4107QTF. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000252916.
KOiK01756.
OMAiTQVNPCD.
OrthoDBiPOG091H01RB.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
InterProiIPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR004769. Pur_lyase.
IPR013539. PurB_C.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF08328. ASL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00928. purB. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiA5EV77_DICNV
AccessioniPrimary (citable) accession number: A5EV77
Entry historyi
Integrated into UniProtKB/TrEMBL: June 12, 2007
Last sequence update: June 12, 2007
Last modified: November 2, 2016
This is version 61 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.