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Protein

Adenylosuccinate lyase

Gene

Sfri_2262

Organism
Shewanella frigidimarina (strain NCIMB 400)
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 (Sfri_2262)
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 (Sfri_2262)
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

BioCyciSFRI318167:GIXS-2345-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:Sfri_2262Imported
OrganismiShewanella frigidimarina (strain NCIMB 400)Imported
Taxonomic identifieri318167 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000000684 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi318167.Sfri_2262.

Structurei

3D structure databases

ProteinModelPortaliQ081F7.
SMRiQ081F7. Positions 1-456.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 312299Lyase_1InterPro annotationAdd
BLAST
Domaini331 – 445115ASL_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.

Q081F7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLSALTAIS PVDGRYGSKT ASLRGIFSEF GLTKYRVQVE INWLKLLSSC
60 70 80 90 100
PEIEEVPPFS ETALAVLDSI KDNFSEQDAL RVKTIESTTN HDVKAVEYFI
110 120 130 140 150
KEQIANNAEL VAIDEFVHFA CTSEDINNLS HGLMLKEARE QVLVPHCQQI
160 170 180 190 200
IDAIKKLAHD NKSVPLMSRT HGQPASPSTL GKEMANVAVR LERQLNQINA
210 220 230 240 250
VEIMGKINGA VGNYNAHISA YPEVNWHELS QRFVTSLGIN WNAYTTQIEP
260 270 280 290 300
HDYIAELFDA IARFNTILID FDRDIWGYVA LGHFKQRTIA GEIGSSTMPH
310 320 330 340 350
KVNPIDFENS EGNLGIANAL MQHLAAKLPV SRWQRDLTDS TVLRNLGVGM
360 370 380 390 400
AHSLIAYQAT LKGISKLEVN EAQLLAELDK NWEVLAEPVQ TVMRRYGIEK
410 420 430 440 450
PYEKLKELTR GKRIDAAQLA VFIDGLELPE HVKIELKKMT PANYIGRAEA

FVDELK
Length:456
Mass (Da):51,029
Last modified:October 31, 2006 - v1
Checksum:i6817F6A017BE1459
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000447 Genomic DNA. Translation: ABI72108.1.
RefSeqiWP_011637717.1. NC_008345.1.

Genome annotation databases

EnsemblBacteriaiABI72108; ABI72108; Sfri_2262.
KEGGisfr:Sfri_2262.
PATRICi23498559. VBISheFri14343_2350.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000447 Genomic DNA. Translation: ABI72108.1.
RefSeqiWP_011637717.1. NC_008345.1.

3D structure databases

ProteinModelPortaliQ081F7.
SMRiQ081F7. Positions 1-456.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi318167.Sfri_2262.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABI72108; ABI72108; Sfri_2262.
KEGGisfr:Sfri_2262.
PATRICi23498559. VBISheFri14343_2350.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciSFRI318167:GIXS-2345-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 nameiQ081F7_SHEFN
AccessioniPrimary (citable) accession number: Q081F7
Entry historyi
Integrated into UniProtKB/TrEMBL: October 31, 2006
Last sequence update: October 31, 2006
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 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.