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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei70 – 701Proton donor/acceptorUniRule annotationBy similarity
Binding sitei147 – 1471SubstrateCombined sources1 Publication
Active sitei178 – 1781Proton donor/acceptorUniRule annotationBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 71D → S: Strongly reduced catalytic activity. 1 Publication
Mutagenesisi147 – 1471E → N: Strongly reduced catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 254254Glutamate racemasePRO_0000095449Add
BLAST

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1
254
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 109Combined sources
Helixi11 – 133Combined sources
Helixi15 – 228Combined sources
Beta strandi23 – 253Combined sources
Beta strandi27 – 326Combined sources
Turni34 – 363Combined sources
Helixi39 – 413Combined sources
Helixi44 – 5916Combined sources
Turni60 – 623Combined sources
Beta strandi64 – 685Combined sources
Helixi71 – 744Combined sources
Helixi78 – 847Combined sources
Beta strandi85 – 873Combined sources
Beta strandi89 – 924Combined sources
Helixi93 – 10311Combined sources
Beta strandi108 – 1136Combined sources
Helixi115 – 1206Combined sources
Helixi122 – 1287Combined sources
Beta strandi133 – 1386Combined sources
Turni143 – 1453Combined sources
Helixi148 – 1514Combined sources
Helixi153 – 1553Combined sources
Helixi156 – 1638Combined sources
Turni165 – 1706Combined sources
Beta strandi172 – 1765Combined sources
Helixi185 – 1917Combined sources
Beta strandi196 – 1983Combined sources
Helixi200 – 2067Combined sources
Turni207 – 2115Combined sources
Beta strandi220 – 2267Combined sources
Helixi231 – 2399Combined sources
Beta strandi245 – 2473Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B73X-ray2.30A1-254[»]
1B74X-ray2.30A1-254[»]
ProteinModelPortaliP56868.
SMRiP56868. Positions 1-252.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56868.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 82Substrate bindingUniRule annotationBy similarity
Regioni39 – 402Substrate bindingUniRule annotationBy similarity
Regioni71 – 722Substrate bindingUniRule annotationCombined sources1 Publication
Regioni179 – 1802Substrate bindingUniRule annotationBy similarity

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.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1B73X-ray2.30A1-254[»]
1B74X-ray2.30A1-254[»]
ProteinModelPortaliP56868.
SMRiP56868. Positions 1-252.
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.
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...

Publicationsi

  1. "Molecular cloning, expression, and characterization of a thermostable glutamate racemase from a hyperthermophilic bacterium, Aquifex pyrophilus."
    Kim S.S., Choi I.G., Kim S.H., Yu Y.G.
    Extremophiles 3:175-183(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, SUBUNIT, CATALYTIC ACTIVITY.
  2. "Structure and mechanism of glutamate racemase from Aquifex pyrophilus."
    Hwang K.Y., Cho C.-S., Kim S.S., Sung H.-C., Yu Y.G., Cho Y.
    Nat. Struct. Biol. 6:422-426(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GLUTAMATE, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF ASP-7 AND GLU-147.

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: March 16, 2016
This is version 82 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.