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Protein

Adenylosuccinate lyase

Gene

LVIS_0228

Organism
Lactobacillus brevis (strain ATCC 367 / JCM 1170)
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 (LVIS_0228)
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. no protein annotated in this organism
  2. Adenylosuccinate lyase (LVIS_0228)
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

BioCyciLBRE387344:GJ8S-228-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:LVIS_0228Imported
OrganismiLactobacillus brevis (strain ATCC 367 / JCM 1170)Imported
Taxonomic identifieri387344 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus
Proteomesi
  • UP000001652 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi387344.LVIS_0228.

Structurei

3D structure databases

ProteinModelPortaliQ03TS8.
SMRiQ03TS8. Positions 2-430.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini349 – 42981ADSL_CInterPro annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C83. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000033912.
KOiK01756.
OMAiVQENAMK.
OrthoDBiEOG686NDB.

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.

Q03TS8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLERYTRPEM GQIWSLENQY ASWLAVEIAI DEAWAKLGEV PVADAQKIRA
60 70 80 90 100
NARFDVERIA DIEAVTHHDM VAFTRNVSES LGAERKWIHF GVTSTDVVDT
110 120 130 140 150
AQGYRLKQAN AVLRADIVTL IATLKNLALT YKETVMIGRT HGVQAEPTTF
160 170 180 190 200
GLKIARWYAE MQRNLERFDR AAAGVETGKI SGAVGTFANV PPEVEAAVCE
210 220 230 240 250
QLGISAQPIA SQVLPRDLHA DYVATLALIG TSIEEFATEI RSLQRSEIHE
260 270 280 290 300
VEEHFNPGQK GSSAMPHKRN PIGSENVTGL ARVLRGTVVT AYENVSLWHE
310 320 330 340 350
RDISHSSAER MILPESTTLL DYMLSRFNRI LTNLDVFPEM MKANMNRTYG
360 370 380 390 400
LIYSQRLLLK LIESGLSREA AYDLVQPLTA QAWDEQRQFR PLVEANTEIT
410 420 430
ARLTPAQIAD AFDYHYHLRR VDEIFKRLGL LD
Length:432
Mass (Da):48,590
Last modified:November 14, 2006 - v1
Checksum:i7B65804BE35D3DC7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000416 Genomic DNA. Translation: ABJ63394.1.
RefSeqiWP_011667022.1. NC_008497.1.

Genome annotation databases

EnsemblBacteriaiABJ63394; ABJ63394; LVIS_0228.
GeneIDi4413050.
KEGGilbr:LVIS_0228.
PATRICi22199424. VBILacBre134470_0224.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000416 Genomic DNA. Translation: ABJ63394.1.
RefSeqiWP_011667022.1. NC_008497.1.

3D structure databases

ProteinModelPortaliQ03TS8.
SMRiQ03TS8. Positions 2-430.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi387344.LVIS_0228.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABJ63394; ABJ63394; LVIS_0228.
GeneIDi4413050.
KEGGilbr:LVIS_0228.
PATRICi22199424. VBILacBre134470_0224.

Phylogenomic databases

eggNOGiENOG4105C83. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000033912.
KOiK01756.
OMAiVQENAMK.
OrthoDBiEOG686NDB.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciLBRE387344:GJ8S-228-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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 367 / JCM 1170Imported.

Entry informationi

Entry nameiQ03TS8_LACBA
AccessioniPrimary (citable) accession number: Q03TS8
Entry historyi
Integrated into UniProtKB/TrEMBL: November 14, 2006
Last sequence update: November 14, 2006
Last modified: July 6, 2016
This is version 66 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.