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Protein

Adenylosuccinate lyase

Gene

Pnap_3914

Organism
Polaromonas naphthalenivorans (strain CJ2)
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 (Pnap_3914)
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 (Pnap_3914)
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

BioCyciPNAP365044:GJ8X-3969-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:Pnap_3914Imported
OrganismiPolaromonas naphthalenivorans (strain CJ2)Imported
Taxonomic identifieri365044 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaePolaromonas
Proteomesi
  • UP000000644 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi365044.Pnap_3914.

Structurei

3D structure databases

ProteinModelPortaliA1VU82.
SMRiA1VU82. Positions 25-483.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 340302Lyase_1InterPro annotationAdd
BLAST
Domaini359 – 473115ASL_CInterPro annotationAdd
BLAST

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.

A1VU82-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIAVFHPLN RRQAPGQCRL QSHPMSFSPI NALSPLDGRY VAKLATLRPL
60 70 80 90 100
MSEQGYMHRR VQVEIAWFIA LSDAKFAEFK PLSPGARTYL LGLVKNFSEA
110 120 130 140 150
DACAIKTIEK TTNHDVKAVE YWIKSKFEAR PELQAASEFV HFACTSEDIN
160 170 180 190 200
NTSQALQLKS SREQVVLPAL DKVIDKLRQL AHAHADVPML SRTHGQTASP
210 220 230 240 250
TTVGKEIANV VVRLVNTREK IAGIKLMAKM NGAVGNFNAH LAAWPDFDWE
260 270 280 290 300
AFSRHVIETP EPLGLGLTFQ PYSIQIEPHD YMAELFDAVA RTNTILIDLA
310 320 330 340 350
RDIWGYVSVG YFKQRLKEGE IGSSTMPHKV NPIDFENAEG NLGLANALLR
360 370 380 390 400
HMSEKLPISR WQRDLTDSTV LRNMGVALGY AVLAYNSLCI GLNKLELNNE
410 420 430 440 450
ALADDLDNSW EVLAEPIQTV MRRYAVAGAY EKLKEVTRGK TVRPEDLHGL
460 470 480
IRSLEIPDAA KERLLAMTPG SYVGMAAELA KRV
Length:483
Mass (Da):53,824
Last modified:February 6, 2007 - v1
Checksum:i5BC7FC376F6FCB8D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000529 Genomic DNA. Translation: ABM39210.1.

Genome annotation databases

EnsemblBacteriaiABM39210; ABM39210; Pnap_3914.
KEGGipna:Pnap_3914.
PATRICi22952609. VBIPolNap76733_4820.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000529 Genomic DNA. Translation: ABM39210.1.

3D structure databases

ProteinModelPortaliA1VU82.
SMRiA1VU82. Positions 25-483.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi365044.Pnap_3914.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABM39210; ABM39210; Pnap_3914.
KEGGipna:Pnap_3914.
PATRICi22952609. VBIPolNap76733_4820.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciPNAP365044:GJ8X-3969-MONOMER.

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 nameiA1VU82_POLNA
AccessioniPrimary (citable) accession number: A1VU82
Entry historyi
Integrated into UniProtKB/TrEMBL: February 6, 2007
Last sequence update: February 6, 2007
Last modified: September 7, 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.