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Q92BF7

- HEM1_LISIN

UniProt

Q92BF7 - HEM1_LISIN

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Listeria innocua serovar 6a (strain CLIP 11262)
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

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:lin1592
OrganismiListeria innocua serovar 6a (strain CLIP 11262)
Taxonomic identifieri272626 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
ProteomesiUP000002513: Chromosome

Organism-specific databases

GenoListiLIN1592.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 435435Glutamyl-tRNA reductasePRO_0000114035Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi272626.lin1592.

Structurei

3D structure databases

ProteinModelPortaliQ92BF7.
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.

Q92BF7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFILTMGLNH HTAPIDIREK LVFKETEEEM ALVTLLQEKS ILENVIISTC
60 70 80 90 100
NRTEIVAVVD QIHTGRYYLK RFMANWFQMD MEKIEPYLFF HEEAEAVNHL
110 120 130 140 150
YKVTAGLDSL VLGETQILGQ VKHAFEIAKQ TGTTGTLLNK LFREVVTFAK
160 170 180 190 200
KVHHHTKINE NAVSVSYAAV EVAKKLYGSL DNKKIVLIGA GEMSELALQN
210 220 230 240 250
LAGSGIADIT IINRTKSNAE ILAHQFQAKV GAYENMSDHL LEADIVLVST
260 270 280 290 300
SAEEPIIKQV AMQELMEQKA SSMLVIDIGL PRNVEHDCSY IPNFHLYDID
310 320 330 340 350
DLAGVVSANS LERQRIVQEL ENTIETEVRS FFEWEKQLGV VPVIRALREK
360 370 380 390 400
ALDMQEVTMT SLENKLPGLT EREYIQIGKH MKSIINQMLK QPISELKEMS
410 420 430
VEENADTSIE HFKRIFGLTE TDVAIIEKEQ AETRS
Length:435
Mass (Da):49,228
Last modified:December 1, 2001 - v1
Checksum:iED4697E1E2C954E4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL596169 Genomic DNA. Translation: CAC96823.1.
PIRiAG1631.
RefSeqiNP_470928.1. NC_003212.1.

Genome annotation databases

EnsemblBacteriaiCAC96823; CAC96823; CAC96823.
GeneIDi1130212.
KEGGilin:lin1592.
PATRICi20299921. VBILisInn102668_1627.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL596169 Genomic DNA. Translation: CAC96823.1 .
PIRi AG1631.
RefSeqi NP_470928.1. NC_003212.1.

3D structure databases

ProteinModelPortali Q92BF7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272626.lin1592.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAC96823 ; CAC96823 ; CAC96823 .
GeneIDi 1130212.
KEGGi lin:lin1592.
PATRICi 20299921. VBILisInn102668_1627.

Organism-specific databases

GenoListi LIN1592.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
KOi K02492.
OMAi LAHKLTN.
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CLIP 11262.

Entry informationi

Entry nameiHEM1_LISIN
AccessioniPrimary (citable) accession number: Q92BF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: December 1, 2001
Last modified: October 1, 2014
This is version 96 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