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Protein

Adenylosuccinate lyase

Gene

purB

Organism
Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)
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 (purB)
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 (purB)
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

BioCyciNMEN272831:GJDX-290-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
Name:purBImported
Ordered Locus Names:NMC0290Imported
OrganismiNeisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)Imported
Taxonomic identifieri272831 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
Proteomesi
  • UP000002286 Componenti: Chromosome

Structurei

3D structure databases

ProteinModelPortaliA1KRX3.
SMRiA1KRX3. Positions 2-449.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 312300Lyase_1InterPro annotationAdd
BLAST
Domaini331 – 446116ASL_CInterPro annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000252916.
KOiK01756.
OMAiTQVNPCD.

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.

A1KRX3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MINPIASLSP LDGRYAQSVE ALRPIFSEYG LMKARVKVEL NWLKALAAEP
60 70 80 90 100
KIVEVPPFSA ETLAEIDTVI ENFSLEDAAA VKAIEATTNH DVKAIEYWLK
110 120 130 140 150
ERFSGVPEVA AASEFIHFAC TSEDINNLSH ALMLQEAREA VLLPKLAEII
160 170 180 190 200
EKLTGMAHEL AAVPMMSRTH GQPATPSTLG KEIANVVYRL QRQFKNLQAQ
210 220 230 240 250
EFLGKINGAV GNYNAHMVAY PDVDWETHCR NFVEISLGLT FNPYTIQIEP
260 270 280 290 300
HDYMAEFFQA ISRVNTILID FNRDVWGYIS LGYFKQKVKA GEVGSSTMPH
310 320 330 340 350
KVNPIDFENS EGNLGMANAV LGFLSEKLPI SRWQRDLTDS TVLRNMGVGV
360 370 380 390 400
GYAVLGFAAH LRGLNKLEPN PAALAADLDA TWELLAEPIQ TVMRRYGVAN
410 420 430 440 450
PYEKLKDLTR GKDGITPEVL KLFIESLEIP AEAKAKLLEL TPALYVGKAE

ALAKRI
Length:456
Mass (Da):50,494
Last modified:February 6, 2007 - v1
Checksum:i873486506D3D0B75
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM421808 Genomic DNA. Translation: CAM09602.1.
RefSeqiWP_002240245.1. NC_008767.1.

Genome annotation databases

EnsemblBacteriaiCAM09602; CAM09602; NMC0290.
KEGGinmc:NMC0290.
PATRICi20350159. VBINeiMen17609_0339.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM421808 Genomic DNA. Translation: CAM09602.1.
RefSeqiWP_002240245.1. NC_008767.1.

3D structure databases

ProteinModelPortaliA1KRX3.
SMRiA1KRX3. Positions 2-449.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAM09602; CAM09602; NMC0290.
KEGGinmc:NMC0290.
PATRICi20350159. VBINeiMen17609_0339.

Phylogenomic databases

HOGENOMiHOG000252916.
KOiK01756.
OMAiTQVNPCD.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciNMEN272831:GJDX-290-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 nameiA1KRX3_NEIMF
AccessioniPrimary (citable) accession number: A1KRX3
Entry historyi
Integrated into UniProtKB/TrEMBL: February 6, 2007
Last sequence update: February 6, 2007
Last modified: September 7, 2016
This is version 63 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.