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A5N5Y0

- HEM1_CLOK5

UniProt

A5N5Y0 - HEM1_CLOK5

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)
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 sitei46 – 461NucleophileUniRule annotation
Sitei91 – 911Important for activityUniRule annotation
Binding sitei101 – 1011SubstrateUniRule annotation
Binding sitei112 – 1121SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi177 – 1826NADPUniRule 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

BioCyciCKLU431943:GJF1-657-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:CKL_0657
OrganismiClostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)
Taxonomic identifieri431943 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000002411: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 399399Glutamyl-tRNA reductasePRO_0000335022Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi431943.CKL_0657.

Structurei

3D structure databases

ProteinModelPortaliA5N5Y0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 484Substrate bindingUniRule annotation
Regioni106 – 1083Substrate 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.
HOGENOMiHOG000090159.
KOiK02492.
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.
SUPFAMiSSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A5N5Y0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIQLIGIKSQ CDIGIRQKFS ITSEVLEGKL KYINELVGSV LILSTCNRTE
60 70 80 90 100
IYVDSNLEEK KLIDTVFYGL DWDYDLVSYI FYIKDKYAIK HLMEVSCGFH
110 120 130 140 150
SKILGEDQIL GQIKTAYDAA LEAKTIKGKL QRLFQKAITC GKEFKHICES
160 170 180 190 200
YRIPVSIPSI VAKEILNMDI RKYMIIGFGK IGQLLFKYLN NSQAQIIYIA
210 220 230 240 250
VRDLNKVHDS YKKCGKIRFI SFKDRKSYYN DIDCIVSCTS APDKIISKGD
260 270 280 290 300
LPCRKLTIFD LAVPEDIDRN VLDLDNVTLY DIDNISVIDE KNKAIRKKTM
310 320 330 340 350
GKYRYILENH IDKFIKWEKL HQLSPEIQKV KKYGDEICEK RITTFKNKKH
360 370 380 390
TKDNDILVKT MIESTARFYI NRAIEVMKEE KLNGREEECL RLINKIFCK
Length:399
Mass (Da):46,435
Last modified:May 20, 2008 - v2
Checksum:i5D94C09FD7EBFC71
GO

Sequence cautioni

The sequence EDK32711.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000673 Genomic DNA. Translation: EDK32711.1. Different initiation.
RefSeqiYP_001394059.1. NC_009706.1.

Genome annotation databases

EnsemblBacteriaiEDK32711; EDK32711; CKL_0657.
GeneIDi5390734.
KEGGickl:CKL_0657.
PATRICi19462741. VBICloKlu111549_0717.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000673 Genomic DNA. Translation: EDK32711.1 . Different initiation.
RefSeqi YP_001394059.1. NC_009706.1.

3D structure databases

ProteinModelPortali A5N5Y0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 431943.CKL_0657.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai EDK32711 ; EDK32711 ; CKL_0657 .
GeneIDi 5390734.
KEGGi ckl:CKL_0657.
PATRICi 19462741. VBICloKlu111549_0717.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000090159.
KOi K02492.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CKLU431943:GJF1-657-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 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 8527 / DSM 555 / NCIMB 10680.

Entry informationi

Entry nameiHEM1_CLOK5
AccessioniPrimary (citable) accession number: A5N5Y0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: October 1, 2014
This is version 61 of the entry and version 2 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