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Q8EPM7

- HEM1_OCEIH

UniProt

Q8EPM7 - HEM1_OCEIH

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Protein

Glutamyl-tRNA reductase

Gene
hemA, OB2070
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) 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 sitei50 – 501Nucleophile 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

BioCyciOIHE221109:GI2A-2150-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: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 reductaseUniRule annotationPRO_0000114049Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi221109.OB2070.

Structurei

3D structure databases

ProteinModelPortaliQ8EPM7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate 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.
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

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MHILKVGFNY KTTPVDIREK FTFSEDSLQD AMVELKNQKS ILEDVIISTC    50
NRTEIYAVVD QLHTGRYYIK QFLSNWFGIE KEEFSTYLRI TEDDGAMEHL 100
FRVSTGLDSM VLGETQILGQ VKQAFLNSQQ VNTTGTIFNE LFKQAITFGK 150
RAHKETAIGE HAVSISYAAV ELAKKIFGDL QEKHVAILGA GKMGELAAKN 200
IQGSGATKIT VVNRTLENAN EMAEKFNADV ESIDQLPVIL QQADILISST 250
GADSIVVTKE MMEKVQKQRK GRALFLVDIA VPRDMDPAIS ELENVFLYDI 300
DNLQHIVDDN LESRKQAAEK IELLIEEEIV TFKEWLKTLG VIPVISALRQ 350
KALTIQAETM QSIERKIPNL TDRERKVLNK HTKSIINQLL KEPVTQAKEF 400
AGKDNAEDSL QLFINIFGIE EEVKEELVKH AKKNETLMKI AKEEPSSFPI 450
IEKITTA 457
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: September 3, 2014
This is version 88 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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