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Protein

Adenylosuccinate lyase

Gene

Swit_4474

Organism
Sphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273)
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 (Swit_4474)
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 (Swit_4474)
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

BioCyciSWIT392499:GHZK-4491-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:Swit_4474Imported
OrganismiSphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273)Imported
Taxonomic identifieri392499 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeSphingomonas
Proteomesi
  • UP000001989 Componenti: Chromosome

PTM / Processingi

Proteomic databases

PRIDEiA5VEU6.

Interactioni

Protein-protein interaction databases

STRINGi392499.Swit_4474.

Structurei

3D structure databases

ProteinModelPortaliA5VEU6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini349 – 431ADSL_CInterPro annotationAdd BLAST83

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.

A5VEU6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIPRYSRPEM VKIWEPETRF RIWFEIEAHA TDALAELGVV PKEAAKAIWE
60 70 80 90 100
KGAFEVDRID AIEAEVKHDV IAFLTNVAEH VGEPARFMHQ GMTSSDVLDT
110 120 130 140 150
CLAVQLARAS DILIADLDKL LDVIKRRAFE HKMTPTIGRS HGIHAEPVTF
160 170 180 190 200
GLKLAQAYAE FARNRERLIA ARKDVATCAI SGAVGTFANI DPRVEAHVAE
210 220 230 240 250
KMGLTVEPVS TQVIPRDRHA MFFATLGVIA SSVERLATEV RHLQRTEVLE
260 270 280 290 300
AEEYFSPGQK GSSAMPHKRN PVLTENLTGL ARLVRGYVTP ALENVALWHE
310 320 330 340 350
RDISHSSVER MIGPDATVTL DFALARLTGV IDKLLVYPAR MQKNLDRMGG
360 370 380 390 400
LVHSQRVLLA LTQAGISRED AYRIVQRNAM KVWESDGALS LLDLLKADPQ
410 420 430
VTAAISEKEL EEKFDLDYHL KHVDTIFARV FG
Length:432
Mass (Da):48,176
Last modified:July 10, 2007 - v1
Checksum:i9C501C4BF4E7743B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000699 Genomic DNA. Translation: ABQ70812.1.
RefSeqiWP_012050648.1. NC_009511.1.

Genome annotation databases

EnsemblBacteriaiABQ70812; ABQ70812; Swit_4474.
KEGGiswi:Swit_4474.
PATRICi23688231. VBISphWit55028_5042.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000699 Genomic DNA. Translation: ABQ70812.1.
RefSeqiWP_012050648.1. NC_009511.1.

3D structure databases

ProteinModelPortaliA5VEU6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi392499.Swit_4474.

Proteomic databases

PRIDEiA5VEU6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABQ70812; ABQ70812; Swit_4474.
KEGGiswi:Swit_4474.
PATRICi23688231. VBISphWit55028_5042.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciSWIT392499:GHZK-4491-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 nameiA5VEU6_SPHWW
AccessioniPrimary (citable) accession number: A5VEU6
Entry historyi
Integrated into UniProtKB/TrEMBL: July 10, 2007
Last sequence update: July 10, 2007
Last modified: November 2, 2016
This is version 62 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.