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Q8EPM7

- HEM1_OCEIH

UniProt

Q8EPM7 - HEM1_OCEIH

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Oceanobacillus iheyensis (strain DSM 14371 / JCM 11309 / KCTC 3954 / HTE831)
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

BioCyciOIHE221109:GI2A-2150-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:OB2070
OrganismiOceanobacillus iheyensis (strain DSM 14371 / JCM 11309 / KCTC 3954 / HTE831)
Taxonomic identifieri221109 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeOceanobacillus
ProteomesiUP000000822: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 457457Glutamyl-tRNA reductasePRO_0000114049Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi221109.OB2070.

Structurei

3D structure databases

ProteinModelPortaliQ8EPM7.
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.
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.

Q8EPM7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHILKVGFNY KTTPVDIREK FTFSEDSLQD AMVELKNQKS ILEDVIISTC
60 70 80 90 100
NRTEIYAVVD QLHTGRYYIK QFLSNWFGIE KEEFSTYLRI TEDDGAMEHL
110 120 130 140 150
FRVSTGLDSM VLGETQILGQ VKQAFLNSQQ VNTTGTIFNE LFKQAITFGK
160 170 180 190 200
RAHKETAIGE HAVSISYAAV ELAKKIFGDL QEKHVAILGA GKMGELAAKN
210 220 230 240 250
IQGSGATKIT VVNRTLENAN EMAEKFNADV ESIDQLPVIL QQADILISST
260 270 280 290 300
GADSIVVTKE MMEKVQKQRK GRALFLVDIA VPRDMDPAIS ELENVFLYDI
310 320 330 340 350
DNLQHIVDDN LESRKQAAEK IELLIEEEIV TFKEWLKTLG VIPVISALRQ
360 370 380 390 400
KALTIQAETM QSIERKIPNL TDRERKVLNK HTKSIINQLL KEPVTQAKEF
410 420 430 440 450
AGKDNAEDSL QLFINIFGIE EEVKEELVKH AKKNETLMKI AKEEPSSFPI

IEKITTA
Length:457
Mass (Da):51,544
Last modified:March 1, 2003 - v1
Checksum:i2D936FCD7D9DFF4A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000028 Genomic DNA. Translation: BAC14026.1.
RefSeqiNP_692991.1. NC_004193.1.
WP_011066465.1. NC_004193.1.

Genome annotation databases

EnsemblBacteriaiBAC14026; BAC14026; BAC14026.
GeneIDi1017794.
KEGGioih:OB2070.
PATRICi22795180. VBIOceIhe82024_2100.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000028 Genomic DNA. Translation: BAC14026.1 .
RefSeqi NP_692991.1. NC_004193.1.
WP_011066465.1. NC_004193.1.

3D structure databases

ProteinModelPortali Q8EPM7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 221109.OB2070.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC14026 ; BAC14026 ; BAC14026 .
GeneIDi 1017794.
KEGGi oih:OB2070.
PATRICi 22795180. VBIOceIhe82024_2100.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci OIHE221109:GI2A-2150-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. "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments."
    Takami H., Takaki Y., Uchiyama I.
    Nucleic Acids Res. 30:3927-3935(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 14371 / JCM 11309 / KCTC 3954 / HTE831.

Entry informationi

Entry nameiHEM1_OCEIH
AccessioniPrimary (citable) accession number: Q8EPM7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: March 1, 2003
Last modified: October 1, 2014
This is version 89 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