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A8H7A6

- HEM1_SHEPA

UniProt

A8H7A6 - HEM1_SHEPA

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Spea_3127
Organism
Shewanella pealeana (strain ATCC 700345 / ANG-SQ1)
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
Sitei95 – 951Important for activity By similarity
Binding sitei105 – 1051Substrate By similarity
Binding sitei116 – 1161Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi185 – 1906NADP By similarity

GO - Molecular functioni

  1. NADP binding Source: InterPro
  2. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP

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

BioCyciSPEA398579:GHG5-3272-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:Spea_3127
OrganismiShewanella pealeana (strain ATCC 700345 / ANG-SQ1)
Taxonomic identifieri398579 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000002608: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 416416Glutamyl-tRNA reductaseUniRule annotation
PRO_1000075427Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi398579.Spea_3127.

Structurei

3D structure databases

ProteinModelPortaliA8H7A6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni110 – 1123Substrate 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.
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.

A8H7A6-1 [UniParc]FASTAAdd to Basket

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MSLVAIGINH KTATVDLREK VAFGPDKIHD AMKSLAASTQ SGEAVIISTC    50
NRTELYCNNC EAADVVAWLE DYHQLSHEDV EPCLYQYKGQ EAVKHLMRVS 100
AGLDSLILGE PQILGQVKQS FVKAKEAGTV AATMDRMFQN TFSVAKKIRT 150
ETEIGAAAVS VAFAAVSMAK HIFSSISTTQ VLLVGAGETI ELVARHLKDN 200
GVTTMVVANR TISRAEAMCE EFGATAITLE QIPDFLPKAD IVISSTASPL 250
PILGKGMVEK ALKQRRHQPM LLVDIAVPRD IEAEVADLDD AFLYTVDDLQ 300
SIIEQNMASR REAAEQAELI AEDQAYQFME WIRSLESVDS IREYRTKSMA 350
IKDELVERAV NKLAQGGNSE QVLLELANKL TNKLIHAPTQ ALTAASRQGD 400
LNSLGQLRAL LGLDKD 416
Length:416
Mass (Da):45,425
Last modified:November 13, 2007 - v1
Checksum:i44788E8E2BD4E69A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000851 Genomic DNA. Translation: ABV88443.1.
RefSeqiYP_001502978.1. NC_009901.1.

Genome annotation databases

EnsemblBacteriaiABV88443; ABV88443; Spea_3127.
GeneIDi5663516.
KEGGispl:Spea_3127.
PATRICi23536345. VBIShePea72822_3270.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000851 Genomic DNA. Translation: ABV88443.1 .
RefSeqi YP_001502978.1. NC_009901.1.

3D structure databases

ProteinModelPortali A8H7A6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 398579.Spea_3127.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABV88443 ; ABV88443 ; Spea_3127 .
GeneIDi 5663516.
KEGGi spl:Spea_3127.
PATRICi 23536345. VBIShePea72822_3270.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci SPEA398579:GHG5-3272-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 700345 / ANG-SQ1.

Entry informationi

Entry nameiHEM1_SHEPA
AccessioniPrimary (citable) accession number: A8H7A6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 13, 2007
Last modified: September 3, 2014
This is version 57 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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