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Protein

Adenylosuccinate lyase

Gene

Ppro_1145

Organism
Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1)
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 (Ppro_1145)
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 (Ppro_1145)
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

BioCyciPPRO338966:GHL0-1142-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:Ppro_1145Imported
OrganismiPelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1)Imported
Taxonomic identifieri338966 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesDesulfuromonadaceaePelobacter
Proteomesi
  • UP000006732 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi338966.Ppro_1145.

Structurei

3D structure databases

ProteinModelPortaliA1AN49.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini349 – 429ADSL_CInterPro annotationAdd BLAST81

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4107QTF. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000033912.
KOiK01756.
OMAiVQENAMK.
OrthoDBiPOG091H0168.

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.

A1AN49-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIERYSRPEM AHIWTAQNRF KIWLEIETLA CEAQAELGVI PKDVVPVIRE
60 70 80 90 100
KGNFDIARID AIEAEVKHDV IAFLTSVSEY VGPEARFIHQ GMTSSDVLDT
110 120 130 140 150
CLSVQLTQAA DQLLVDLDMV LASIRKRALE HRDTVCIGRS HGIHAEPVTF
160 170 180 190 200
GLKLATWYAE MQRNRDRLAA SRETIATGAI SGAVGTFANI DPFVEEYVCQ
210 220 230 240 250
RMGLKAEPVS TQVIPRDRHA EYFCTLALIA SSMERIAVEI RHLQRTEVLE
260 270 280 290 300
AEEFFSKGQK GSSAMPHKRN PVLSENLTGQ ARYIRSLCIP ALENVALWHE
310 320 330 340 350
RDISHSSVER YIGPDATVAL DFSLRRLNGL IENLVVYPEN MLRNLNQMKG
360 370 380 390 400
LVFSQKILLD LTQAGVSRED SYRLVQRNAM KVWEQGKDFL TELLNDQEVV
410 420 430
GALGEAKIRE SFDLNYHLKH VNTIFKRVFG E
Length:431
Mass (Da):48,762
Last modified:January 23, 2007 - v1
Checksum:i78A1C32E5BABBE50
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000482 Genomic DNA. Translation: ABK98769.1.
RefSeqiWP_011735071.1. NC_008609.1.

Genome annotation databases

EnsemblBacteriaiABK98769; ABK98769; Ppro_1145.
KEGGippd:Ppro_1145.
PATRICi22895333. VBIPelPro64470_1296.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000482 Genomic DNA. Translation: ABK98769.1.
RefSeqiWP_011735071.1. NC_008609.1.

3D structure databases

ProteinModelPortaliA1AN49.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi338966.Ppro_1145.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK98769; ABK98769; Ppro_1145.
KEGGippd:Ppro_1145.
PATRICi22895333. VBIPelPro64470_1296.

Phylogenomic databases

eggNOGiENOG4107QTF. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000033912.
KOiK01756.
OMAiVQENAMK.
OrthoDBiPOG091H0168.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciPPRO338966:GHL0-1142-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 nameiA1AN49_PELPD
AccessioniPrimary (citable) accession number: A1AN49
Entry historyi
Integrated into UniProtKB/TrEMBL: January 23, 2007
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 59 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.