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B6EHH4

- HEM1_ALISL

UniProt

B6EHH4 - HEM1_ALISL

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain LFI1238))
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
Sitei98 – 981Important for activityUniRule annotation
Binding sitei108 – 1081SubstrateUniRule annotation
Binding sitei119 – 1191SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi188 – 1936NADPUniRule 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

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:VSAL_I0789
OrganismiAliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain LFI1238))
Taxonomic identifieri316275 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio
ProteomesiUP000001730: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 418418Glutamyl-tRNA reductasePRO_1000093113Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi316275.VSAL_I0789.

Structurei

3D structure databases

ProteinModelPortaliB6EHH4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni113 – 1153Substrate 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.
OMAiMIICEEL.
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.

B6EHH4-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MSLLVIGINH TSATVDLREK VAFSPDKLTK ALDELKNSDA IKSGVILSTC
60 70 80 90 100
NRTEIYCEVK LGISSGYVIN WLAEFHHVAL DLLMPSIYIY EEQAAVKHLM
110 120 130 140 150
RVSCGLDSLV LGEPQILGQV KKAFADAREH NAVEGVVEKL FQSDFSVAKR
160 170 180 190 200
VRTETNIGGN AVSVAYAACT LARQIFESLA ESTVMLVGAG ETIELVAKHL
210 220 230 240 250
NDAGCKQLIV ANRTRERAMI LADQFNADVI SLPEIPEHLS KADIIISSTA
260 270 280 290 300
SPLPIIGKGM VESALKQRRH QPMLFVDIAV PRDIESEVAD LNDVYLYSVD
310 320 330 340 350
DLKSIIDHNI EQRKIEAIQA EAIVSEESAG FMTWIRSRQA VNSIRQYREN
360 370 380 390 400
SESIRIELLQ KSIQALASGQ NAEKVLAELS NKLTNKLIHA PTLAMQQAAK
410
NGEPDKLAVI RTSIGLDN
Length:418
Mass (Da):45,894
Last modified:November 25, 2008 - v1
Checksum:iAC7906DFFAAE841D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FM178379 Genomic DNA. Translation: CAQ78474.1.
RefSeqiWP_012549582.1. NC_011312.1.
YP_002262299.1. NC_011312.1.

Genome annotation databases

EnsemblBacteriaiCAQ78474; CAQ78474; VSAL_I0789.
GeneIDi6986666.
KEGGivsa:VSAL_I0789.
PATRICi20851760. VBIAliSal95923_0908.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FM178379 Genomic DNA. Translation: CAQ78474.1 .
RefSeqi WP_012549582.1. NC_011312.1.
YP_002262299.1. NC_011312.1.

3D structure databases

ProteinModelPortali B6EHH4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 316275.VSAL_I0789.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAQ78474 ; CAQ78474 ; VSAL_I0789 .
GeneIDi 6986666.
KEGGi vsa:VSAL_I0789.
PATRICi 20851760. VBIAliSal95923_0908.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .

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. "The genome sequence of the fish pathogen Aliivibrio salmonicida strain LFI1238 shows extensive evidence of gene decay."
    Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N., Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S., Thurston S., Parkhill J., Willassen N.P., Thomson N.R.
    BMC Genomics 9:616-616(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LFI1238.

Entry informationi

Entry nameiHEM1_ALISL
AccessioniPrimary (citable) accession number: B6EHH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 25, 2008
Last modified: October 29, 2014
This is version 50 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