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Protein

Glutamate racemase

Gene

murI

Organism
Aquifex pyrophilus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Provides the (R)-glutamate required for cell wall biosynthesis. Converts L- or D-glutamate to D- or L-glutamate, respectively, but not other amino acids such as alanine, aspartate, and glutamine.

Catalytic activityi

L-glutamate = D-glutamate.UniRule annotation2 Publications

Temperature dependencei

Thermostable.

Pathwayi: peptidoglycan biosynthesis

This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei70Proton donor/acceptorUniRule annotationBy similarity1
Binding sitei147SubstrateCombined sources1 Publication1
Active sitei178Proton donor/acceptorUniRule annotationBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

BRENDAi5.1.1.3. 397.
SABIO-RKP56868.
UniPathwayiUPA00219.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate racemase1 PublicationUniRule annotation (EC:5.1.1.3UniRule annotation2 Publications)
Gene namesi
Name:murIUniRule annotation
OrganismiAquifex pyrophilus
Taxonomic identifieri2714 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi7D → S: Strongly reduced catalytic activity. 1 Publication1
Mutagenesisi147E → N: Strongly reduced catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000954491 – 254Glutamate racemaseAdd BLAST254

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1254
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 10Combined sources9
Helixi11 – 13Combined sources3
Helixi15 – 22Combined sources8
Beta strandi23 – 25Combined sources3
Beta strandi27 – 32Combined sources6
Turni34 – 36Combined sources3
Helixi39 – 41Combined sources3
Helixi44 – 59Combined sources16
Turni60 – 62Combined sources3
Beta strandi64 – 68Combined sources5
Helixi71 – 74Combined sources4
Helixi78 – 84Combined sources7
Beta strandi85 – 87Combined sources3
Beta strandi89 – 92Combined sources4
Helixi93 – 103Combined sources11
Beta strandi108 – 113Combined sources6
Helixi115 – 120Combined sources6
Helixi122 – 128Combined sources7
Beta strandi133 – 138Combined sources6
Turni143 – 145Combined sources3
Helixi148 – 151Combined sources4
Helixi153 – 155Combined sources3
Helixi156 – 163Combined sources8
Turni165 – 170Combined sources6
Beta strandi172 – 176Combined sources5
Helixi185 – 191Combined sources7
Beta strandi196 – 198Combined sources3
Helixi200 – 206Combined sources7
Turni207 – 211Combined sources5
Beta strandi220 – 226Combined sources7
Helixi231 – 239Combined sources9
Beta strandi245 – 247Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B73X-ray2.30A1-254[»]
1B74X-ray2.30A1-254[»]
ProteinModelPortaliP56868.
SMRiP56868.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56868.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni7 – 8Substrate bindingUniRule annotationBy similarity2
Regioni39 – 40Substrate bindingUniRule annotationBy similarity2
Regioni71 – 72Substrate bindingUniRule annotationCombined sources1 Publication2
Regioni179 – 180Substrate bindingUniRule annotationBy similarity2

Sequence similaritiesi

Belongs to the aspartate/glutamate racemases family.UniRule annotation

Family and domain databases

Gene3Di3.40.50.1860. 1 hit.
HAMAPiMF_00258. Glu_racemase. 1 hit.
InterProiIPR015942. Asp/Glu/hydantoin_racemase.
IPR001920. Asp/Glu_race.
IPR018187. Asp/Glu_racemase_AS_1.
IPR033134. Asp/Glu_racemase_AS_2.
IPR004391. Glu_race.
[Graphical view]
PfamiPF01177. Asp_Glu_race. 1 hit.
[Graphical view]
SUPFAMiSSF53681. SSF53681. 2 hits.
TIGRFAMsiTIGR00067. glut_race. 1 hit.
PROSITEiPS00923. ASP_GLU_RACEMASE_1. 1 hit.
PS00924. ASP_GLU_RACEMASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P56868-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIGIFDSGV GGLTVLKAIR NRYRKVDIVY LGDTARVPYG IRSKDTIIRY
60 70 80 90 100
SLECAGFLKD KGVDIIVVAC NTASAYALER LKKEINVPVF GVIEPGVKEA
110 120 130 140 150
LKKSRNKKIG VIGTPATVKS GAYQRKLEEG GADVFAKACP LFVPLAEEGL
160 170 180 190 200
LEGEITRKVV EHYLKEFKGK IDTLILGCTH YPLLKKEIKK FLGDVEVVDS
210 220 230 240 250
SEALSLSLHN FIKDDGSSSL ELFFTDLSPN LQFLIKLILG RDYPVKLAEG

VFTH
Length:254
Mass (Da):27,993
Last modified:May 30, 2000 - v1
Checksum:iD9E7B16F33A90711
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF212972 Genomic DNA. Translation: AAF25672.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF212972 Genomic DNA. Translation: AAF25672.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B73X-ray2.30A1-254[»]
1B74X-ray2.30A1-254[»]
ProteinModelPortaliP56868.
SMRiP56868.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00219.
BRENDAi5.1.1.3. 397.
SABIO-RKP56868.

Miscellaneous databases

EvolutionaryTraceiP56868.

Family and domain databases

Gene3Di3.40.50.1860. 1 hit.
HAMAPiMF_00258. Glu_racemase. 1 hit.
InterProiIPR015942. Asp/Glu/hydantoin_racemase.
IPR001920. Asp/Glu_race.
IPR018187. Asp/Glu_racemase_AS_1.
IPR033134. Asp/Glu_racemase_AS_2.
IPR004391. Glu_race.
[Graphical view]
PfamiPF01177. Asp_Glu_race. 1 hit.
[Graphical view]
SUPFAMiSSF53681. SSF53681. 2 hits.
TIGRFAMsiTIGR00067. glut_race. 1 hit.
PROSITEiPS00923. ASP_GLU_RACEMASE_1. 1 hit.
PS00924. ASP_GLU_RACEMASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMURI_AQUPY
AccessioniPrimary (citable) accession number: P56868
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: November 2, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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.