Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A3QH31

- HEM1_SHELP

UniProt

A3QH31 - HEM1_SHELP

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Shewanella loihica (strain ATCC BAA-1088 / PV-4)
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
Sitei95 – 951Important for activityUniRule annotation
Binding sitei105 – 1051SubstrateUniRule annotation
Binding sitei116 – 1161SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi185 – 1906NADPUniRule 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

BioCyciSLOI323850:GHQJ-3005-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:Shew_2913
OrganismiShewanella loihica (strain ATCC BAA-1088 / PV-4)
Taxonomic identifieri323850 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000001558: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 416416Glutamyl-tRNA reductasePRO_1000004690Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi323850.Shew_2913.

Structurei

3D structure databases

ProteinModelPortaliA3QH31.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni110 – 1123Substrate 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.
HOGENOMiHOG000109650.
KOiK02492.
OMAiLAHKLTN.
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.

A3QH31-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSLVAIGINH KTATVDLREK VAFAPDKIHE AMKSLASRTK TGEAVIVSTC
60 70 80 90 100
NRTELYCNTG DEADVISWLE SYHQLSHDDV LPCLYKYQGQ QVVQHLMRVS
110 120 130 140 150
SGLDSLILGE PQILGQVKQS FVKAKEAGTV AVTMDRLFQN TFSVAKKVRT
160 170 180 190 200
ETEIGAAAVS VAFAAVSMAK HIFSALSATK VLLIGAGETI ELVARHLKDN
210 220 230 240 250
GVDSMIVANR TISRAEAMCE EFGATAITLE QIPDFLPKAD IVISSTASPL
260 270 280 290 300
PILGKGMVEK ALKQRRHQPM LLVDIAVPRD IEAEVADLDD AFLYTVDDLQ
310 320 330 340 350
SIIEQNMASR REAAEKAELI VEEESHHFME WIRSLESVDS IREYRSQSMA
360 370 380 390 400
IRDELVERAI NKLAQGGDSE QLILELANKL TNKLIHAPTQ ALTQASRRGD
410
LNSLGQLRAA LGLDKD
Length:416
Mass (Da):45,644
Last modified:April 17, 2007 - v1
Checksum:i9E56664DF922EEAF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000606 Genomic DNA. Translation: ABO24779.1.
RefSeqiYP_001095038.1. NC_009092.1.

Genome annotation databases

EnsemblBacteriaiABO24779; ABO24779; Shew_2913.
GeneIDi4921173.
KEGGislo:Shew_2913.
PATRICi23517721. VBISheLoi132094_2913.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000606 Genomic DNA. Translation: ABO24779.1 .
RefSeqi YP_001095038.1. NC_009092.1.

3D structure databases

ProteinModelPortali A3QH31.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 323850.Shew_2913.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABO24779 ; ABO24779 ; Shew_2913 .
GeneIDi 4921173.
KEGGi slo:Shew_2913.
PATRICi 23517721. VBISheLoi132094_2913.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci SLOI323850:GHQJ-3005-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: ATCC BAA-1088 / PV-4.

Entry informationi

Entry nameiHEM1_SHELP
AccessioniPrimary (citable) accession number: A3QH31
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 17, 2007
Last modified: October 1, 2014
This is version 61 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