Skip Header

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

A3D0G0

- HEM1_SHEB5

UniProt

A3D0G0 - HEM1_SHEB5

(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 baltica (strain OS155 / ATCC BAA-1091)
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

BioCyciSBAL325240:GCTA-713-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:Sbal_0695
OrganismiShewanella baltica (strain OS155 / ATCC BAA-1091)
Taxonomic identifieri325240 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000001557: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 416416Glutamyl-tRNA reductasePRO_1000004686Add
BLAST

Proteomic databases

PRIDEiA3D0G0.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi325240.Sbal_0695.

Structurei

3D structure databases

ProteinModelPortaliA3D0G0.
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.

A3D0G0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSLVAIGINH KTATVDLREK VAFSPDKIHD AMKSLASRTR SGEAVIVSTC
60 70 80 90 100
NRTELYCNNG DEADIIAWLE EYHGLDHKDV APCLYNYHGQ DAVRHLMRVA
110 120 130 140 150
SGLDSLILGE PQILGQVKQA FVKAKEAGTV ALTIDRLFQN TFSVAKKVRT
160 170 180 190 200
DTEIGAAAVS VAFAAVSMAK HIFSSISTTK VLLIGAGETI ELVAKHLKDN
210 220 230 240 250
GVASMVVANR TLERAQGMCE EFGATAITLA QIPDYLPKAD IVISSTASPL
260 270 280 290 300
PILGKGMVEK ALKQRRHQPM LLVDIAVPRD IEPEVADLDD AFLYTVDDLH
310 320 330 340 350
SIIEQNMASR KEAAEQAEVI TEEQSFLFMD WIRSLESVDS IREYRSQSMA
360 370 380 390 400
VKDELVERAL NKLAQGSDTE QVLIELANRL TNKLIHAPTQ ALTAASRQGD
410
LNTLGQLRSA LGLDKN
Length:416
Mass (Da):45,444
Last modified:March 20, 2007 - v1
Checksum:i8AAE3737FF3B2778
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000563 Genomic DNA. Translation: ABN60223.1.
RefSeqiYP_001049092.1. NC_009052.1.

Genome annotation databases

EnsemblBacteriaiABN60223; ABN60223; Sbal_0695.
GeneIDi4843253.
KEGGisbl:Sbal_0695.
PATRICi37180123. VBISheBal55297_0920.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000563 Genomic DNA. Translation: ABN60223.1 .
RefSeqi YP_001049092.1. NC_009052.1.

3D structure databases

ProteinModelPortali A3D0G0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 325240.Sbal_0695.

Proteomic databases

PRIDEi A3D0G0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABN60223 ; ABN60223 ; Sbal_0695 .
GeneIDi 4843253.
KEGGi sbl:Sbal_0695.
PATRICi 37180123. VBISheBal55297_0920.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci SBAL325240:GCTA-713-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: OS155 / ATCC BAA-1091.

Entry informationi

Entry nameiHEM1_SHEB5
AccessioniPrimary (citable) accession number: A3D0G0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 20, 2007
Last modified: October 1, 2014
This is version 62 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

Documents

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

External Data

Dasty 3