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A1AX01

- HEM1_RUTMC

UniProt

A1AX01 - HEM1_RUTMC

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Protein

Glutamyl-tRNA reductase

Gene
hemA, Rmag_0730
Organism
Ruthia magnifica subsp. Calyptogena magnifica
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) By similarity.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 sitei51 – 511Nucleophile By similarity
Sitei99 – 991Important for activity By similarity
Binding sitei109 – 1091Substrate By similarity
Binding sitei120 – 1201Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 1946NADP By similarity

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

BioCyciCRUT413404:GHM7-756-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
Ordered Locus Names:Rmag_0730
OrganismiRuthia magnifica subsp. Calyptogena magnifica
Taxonomic identifieri413404 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriasulfur-oxidizing symbionts
ProteomesiUP000002587: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 416416Glutamyl-tRNA reductaseUniRule annotationPRO_0000335069Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi413404.Rmag_0730.

Structurei

3D structure databases

ProteinModelPortaliA1AX01.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 534Substrate binding By similarity
Regioni114 – 1163Substrate binding By similarity

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 By similarity.UniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109650.
KOiK02492.
OMAiAETEIQG.
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.

A1AX01-1 [UniParc]FASTAAdd to Basket

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MSQIAILSVN HQLVPVEVRE KVAFTPDKLI QALNNLHHID GIDACIILST    50
CNRVEIYVAS NHKNSEELLS NYLAKTHNIK RDIIDSYLNY FEGNEALTHL 100
CNVATGLDSL VLGEPQILGQ LKNAYHIAKE VKTLNKLLEK LFQHTFSTAK 150
KVRTNTQIGA SPVSIAYCAV KLSEKIFEQL SEQTVLLIGA GEMIELCAHY 200
LNQKGVNKMI VANRTIENAK KIAHLYQAQS IGLKQFSSFV YKADIIISST 250
AASMPIIGKG LIESALKKRK HKPIFMLDIA IPRDIEPEVG QLDDVYLYTI 300
DDLGQVVNDN IGNREKEKGL AQEIIVKQNQ VFNKWLDTIP NEQMVQSYQF 350
GANSIKNELL EKAIKQLKNG ANSEDTIRKL ADQLANKLLH LPFKNIKQTS 400
IENLSQCEGC IPYIKN 416
Length:416
Mass (Da):46,617
Last modified:January 23, 2007 - v1
Checksum:i10B27D8B37D46E6F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000488 Genomic DNA. Translation: ABL02458.1.
RefSeqiYP_903929.1. NC_008610.1.

Genome annotation databases

EnsemblBacteriaiABL02458; ABL02458; Rmag_0730.
GeneIDi4555590.
KEGGirma:Rmag_0730.
PATRICi32001185. VBICanRut45856_0805.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000488 Genomic DNA. Translation: ABL02458.1 .
RefSeqi YP_903929.1. NC_008610.1.

3D structure databases

ProteinModelPortali A1AX01.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 413404.Rmag_0730.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABL02458 ; ABL02458 ; Rmag_0730 .
GeneIDi 4555590.
KEGGi rma:Rmag_0730.
PATRICi 32001185. VBICanRut45856_0805.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109650.
KOi K02492.
OMAi AETEIQG.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CRUT413404:GHM7-756-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].

Entry informationi

Entry nameiHEM1_RUTMC
AccessioniPrimary (citable) accession number: A1AX01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: January 23, 2007
Last modified: September 3, 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 By similarity.

Keywords - Technical termi

Complete proteome

Documents

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

External Data

Dasty 3

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