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Protein

Adenylosuccinate lyase

Gene

Bpro_4662

Organism
Polaromonas sp. (strain JS666 / ATCC BAA-500)
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 (Bpro_4662)
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 (Bpro_4662)
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

BioCyciPSP296591:GHI4-5380-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:Bpro_4662Imported
OrganismiPolaromonas sp. (strain JS666 / ATCC BAA-500)Imported
Taxonomic identifieri296591 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaePolaromonas
Proteomesi
  • UP000001983 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi296591.Bpro_4662.

Structurei

3D structure databases

ProteinModelPortaliQ122J7.
SMRiQ122J7. Positions 1-459.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 316303Lyase_1InterPro annotationAdd
BLAST
Domaini335 – 449115ASL_CInterPro annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4107QTF. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000252916.
KOiK01756.
OMAiTFGKEMA.
OrthoDBiEOG686NDB.

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.

Q122J7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFSTINALS PLDGRYAGKL SQLRPLMSEQ GYMHRRVQVE VAWFIALSDA
60 70 80 90 100
KFAEFKPLSP GARTYLLGLV KNFSENDAVA IKEIEKTTNH DVKAVEYWIK
110 120 130 140 150
SKFEARPELQ AAGEFVHFAC TSEDINNTSH ALQLKSSREL VLLPALDKVI
160 170 180 190 200
AQMRKMAHTY AAEPMLSRTH GQTASPTTVG KEIANVVVRL QAAREKIAGI
210 220 230 240 250
RLMAKMNGAV GNYNAHLSAW PDFDWEAFSR NVIETPEPLG LGLTFQPYSI
260 270 280 290 300
QIEPHDYMAE LFDAVARTNT ILIDFARDVW GYVSVGYFKQ RLKEGEIGSS
310 320 330 340 350
TMPHKVNPID FENAEGNLGL ANALLRHLSE KLPVSRWQRD LTDSTVLRNM
360 370 380 390 400
GVALGYAVLA YNSLGVGLGK LELNREALQE DLDSSWEVLA EPIQTVMRRY
410 420 430 440 450
GVQGAYEKLK EVTRGKTVKA EDLHALIRSL QIPDAEKQRL LAMTPASYVG

LAATLARRV
Length:459
Mass (Da):51,132
Last modified:August 22, 2006 - v1
Checksum:i590F22FA09086585
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000316 Genomic DNA. Translation: ABE46545.1.
RefSeqiWP_011485532.1. NC_007948.1.

Genome annotation databases

EnsemblBacteriaiABE46545; ABE46545; Bpro_4662.
KEGGipol:Bpro_4662.
PATRICi22962636. VBIPolSp102244_4763.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000316 Genomic DNA. Translation: ABE46545.1.
RefSeqiWP_011485532.1. NC_007948.1.

3D structure databases

ProteinModelPortaliQ122J7.
SMRiQ122J7. Positions 1-459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi296591.Bpro_4662.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE46545; ABE46545; Bpro_4662.
KEGGipol:Bpro_4662.
PATRICi22962636. VBIPolSp102244_4763.

Phylogenomic databases

eggNOGiENOG4107QTF. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000252916.
KOiK01756.
OMAiTFGKEMA.
OrthoDBiEOG686NDB.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciPSP296591:GHI4-5380-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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JS666 / ATCC BAA-500Imported.

Entry informationi

Entry nameiQ122J7_POLSJ
AccessioniPrimary (citable) accession number: Q122J7
Entry historyi
Integrated into UniProtKB/TrEMBL: August 22, 2006
Last sequence update: August 22, 2006
Last modified: July 6, 2016
This is version 65 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.