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Protein

Adenylosuccinate lyase

Gene

Rsph17025_2272

Organism
Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
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 (Rsph17025_2272)
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), Phosphoribosylaminoimidazole-succinocarboxamide synthase (purC)
  2. Adenylosuccinate lyase (Rsph17025_2272)
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

BioCyciRSPH349102:GHE1-3599-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:Rsph17025_2272Imported
OrganismiRhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)Imported
Taxonomic identifieri349102 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
Proteomesi
  • UP000000234 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi349102.Rsph17025_2272.

Structurei

3D structure databases

ProteinModelPortaliA4WUU8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini352 – 43281ADSL_CInterPro annotationAdd
BLAST

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.

A4WUU8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIPRYSRPDM VAIWSPETKF RIWFEIEAHA CDAQAALGVI PKANAEAVWK
60 70 80 90 100
AADATFDVAR IDEIEAVTKH DVIAFLTHLA EIVGADEARF VHQGMTSSDV
110 120 130 140 150
LDTTLNIQLV RAADLLLAGL DRVLAALKTR AYEHKDTVRI GRSHGIHAEP
160 170 180 190 200
TTMGLTFARF YAEMARNRTR LVNARAEVAT GAISGAVGTF ANIDPRVEEH
210 220 230 240 250
VCEKLGLLPE PISTQVIPRD RHAMFFATLG VIASSIENVA IEIRHMQRTE
260 270 280 290 300
VLEAEEFFSP GQKGSSAMPH KRNPVLTENL TGLARLVRMA VIPAMENVAL
310 320 330 340 350
WHERDISHSS VERAIGPDAT ITLDFALHRL AGVVEKLVVY PENMLKNMNK
360 370 380 390 400
FRGLVMSQRV LLALTQAGVS REDSYRLVQR NAMKVWEEGK DFKEELLADP
410 420 430
EVTAALSPAE IEEKFDLGYH LKHVDTIFAR VFGA
Length:434
Mass (Da):48,199
Last modified:May 29, 2007 - v1
Checksum:i87A8170E9DF49D4F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000661 Genomic DNA. Translation: ABP71162.1.
RefSeqiWP_011909233.1. NC_009428.1.

Genome annotation databases

EnsemblBacteriaiABP71162; ABP71162; Rsph17025_2272.
KEGGirsq:Rsph17025_2272.
PATRICi23162857. VBIRhoSph94549_2344.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000661 Genomic DNA. Translation: ABP71162.1.
RefSeqiWP_011909233.1. NC_009428.1.

3D structure databases

ProteinModelPortaliA4WUU8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi349102.Rsph17025_2272.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABP71162; ABP71162; Rsph17025_2272.
KEGGirsq:Rsph17025_2272.
PATRICi23162857. VBIRhoSph94549_2344.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciRSPH349102:GHE1-3599-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 nameiA4WUU8_RHOS5
AccessioniPrimary (citable) accession number: A4WUU8
Entry historyi
Integrated into UniProtKB/TrEMBL: May 29, 2007
Last sequence update: May 29, 2007
Last modified: September 7, 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 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.