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A5GCW3

- HEM1_GEOUR

UniProt

A5GCW3 - HEM1_GEOUR

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Geobacter uraniireducens (strain Rf4) (Geobacter uraniumreducens)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).UniRule annotation

Catalytic activityi

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei50 – 501NucleophileUniRule annotation
Sitei99 – 991Important for activityUniRule annotation
Binding sitei109 – 1091SubstrateUniRule annotation
Binding sitei120 – 1201SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 1946NADPUniRule annotation

GO - Molecular functioni

  1. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
  2. NADP binding Source: InterPro

GO - Biological processi

  1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciGURA351605:GI6A-367-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTRUniRule annotation
Gene namesi
Name:hemAUniRule annotation
Ordered Locus Names:Gura_0360
OrganismiGeobacter uraniireducens (strain Rf4) (Geobacter uraniumreducens)
Taxonomic identifieri351605 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter
ProteomesiUP000006695: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434Glutamyl-tRNA reductasePRO_1000075410Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi351605.Gura_0360.

Structurei

3D structure databases

ProteinModelPortaliA5GCW3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni114 – 1163Substrate bindingUniRule annotation

Domaini

Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.UniRule annotation

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109651.
KOiK02492.
OMAiKMLHGTM.
OrthoDBiEOG6MWNBM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMiSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A5GCW3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNIIVVGLSH KTATVEIREK VAFAPTQMEK PLHALVSLPD ITEAVIVSTC
60 70 80 90 100
NRVEIYATTR DIAGGVARLK RFLADYHNIS LETLEPHLYS YHGEAATRHV
110 120 130 140 150
FRVASSLDSM VVGEPQILGQ IKTSYGYAAE YKSSGIILNR FLHKAFSVAK
160 170 180 190 200
RVRTETKIAS SAVSVAFAAV ELAKKIFGDL SDKTVMLIGA GEMCELAAKH
210 220 230 240 250
FINTGVRGVM VTNRTFERAV KLAEEFDGKA VNYEELFDHL HKADIVLSST
260 270 280 290 300
GAPHFIIGPK NVEEVIRRRK MKPMFFIDIA VPRDIDPKVN DVENIYLYTV
310 320 330 340 350
DDLNGVVATN LEQRNKEAEK AEAIVEQEIG QFFKWLSSLE VTPTIVALRS
360 370 380 390 400
KFDEIRRAEL AKTLANWKEL PPDAEKRLEA LTSAIMNKLL HQPTSVLKRA
410 420 430
EQGNRNDLYI DALRNLFELE TTRPEVEELG ELEE
Length:434
Mass (Da):48,621
Last modified:June 12, 2007 - v1
Checksum:iC73AE46A08C845D0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000698 Genomic DNA. Translation: ABQ24576.1.
RefSeqiWP_011937302.1. NC_009483.1.
YP_001229149.1. NC_009483.1.

Genome annotation databases

EnsemblBacteriaiABQ24576; ABQ24576; Gura_0360.
GeneIDi5164597.
KEGGigur:Gura_0360.
PATRICi22030564. VBIGeoUra13052_0377.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000698 Genomic DNA. Translation: ABQ24576.1 .
RefSeqi WP_011937302.1. NC_009483.1.
YP_001229149.1. NC_009483.1.

3D structure databases

ProteinModelPortali A5GCW3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 351605.Gura_0360.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABQ24576 ; ABQ24576 ; Gura_0360 .
GeneIDi 5164597.
KEGGi gur:Gura_0360.
PATRICi 22030564. VBIGeoUra13052_0377.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
KOi K02492.
OMAi KMLHGTM.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci GURA351605:GI6A-367-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00087. Glu_tRNA_reductase.
InterProi IPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view ]
Pfami PF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMi SSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsi TIGR01035. hemA. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Rf4.

Entry informationi

Entry nameiHEM1_GEOUR
AccessioniPrimary (citable) accession number: A5GCW3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: October 29, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA.UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3