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A8LDG7

- HEM1_FRASN

UniProt

A8LDG7 - HEM1_FRASN

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Frankia sp. (strain EAN1pec)
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 bindingi229 – 2346NADPUniRule 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

BioCyciFSP298653:GHPI-6162-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:Franean1_6131
OrganismiFrankia sp. (strain EAN1pec)
Taxonomic identifieri298653 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeFrankiaceaeFrankia
ProteomesiUP000001313: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 476476Glutamyl-tRNA reductasePRO_1000093137Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi298653.Franean1_6131.

Structurei

3D structure databases

ProteinModelPortaliA8LDG7.
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.
HOGENOMiHOG000109649.
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.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A8LDG7-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MSLLAVGLNH RTAPTSLLEL AAVSADDAPK VLHDLVGADH LSEAVLLSTC
60 70 80 90 100
NRTEIYAEVE TFHGGLADIS DQLSRVCGVP LTDLASHLYV HHEARAVSHL
110 120 130 140 150
FSVVCGLDSM LVGETQILGQ VRAAFRLAQA AEVTSGTLAN LFQTALRVGK
160 170 180 190 200
RAHTETSIDA AGASIVSVGV RMAAFDLQAR RPDMLVAPVA SPGCDPGDAV
210 220 230 240 250
EALLRPELTA PVEVAGPAPL AGARVLIIGA GAVGSLAAQT VRRAGAGDVV
260 270 280 290 300
VANRTAARAA RVADLHDARA VGLAEIAHEV GRADLVISST GASGLVVGHD
310 320 330 340 350
AVRASLAGRG ARPLVFLDLA LPRDIDPAVR ELPGVTLIDI EALRVALDGA
360 370 380 390 400
QVAHDVEAVR ALVTTEVAGF LDRRRAERVA PTVVALRAHA AAVVRDELER
410 420 430 440 450
LRTRLPDLDN REWDMVSGTV RRVVDKLLHA PTVRVQQLAE APGGDSYAEA
460 470
LRELFDLPRD VPAIVSAPDL DLVERT
Length:476
Mass (Da):49,893
Last modified:December 4, 2007 - v1
Checksum:iD40B3C26E5B8FC79
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000820 Genomic DNA. Translation: ABW15475.1.
RefSeqiWP_020463555.1. NC_009921.1.
YP_001510381.1. NC_009921.1.

Genome annotation databases

EnsemblBacteriaiABW15475; ABW15475; Franean1_6131.
GeneIDi5674452.
KEGGifre:Franean1_6131.
PATRICi21945803. VBIFraSp51419_6498.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000820 Genomic DNA. Translation: ABW15475.1 .
RefSeqi WP_020463555.1. NC_009921.1.
YP_001510381.1. NC_009921.1.

3D structure databases

ProteinModelPortali A8LDG7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 298653.Franean1_6131.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABW15475 ; ABW15475 ; Franean1_6131 .
GeneIDi 5674452.
KEGGi fre:Franean1_6131.
PATRICi 21945803. VBIFraSp51419_6498.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109649.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci FSP298653:GHPI-6162-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.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: EAN1pec.

Entry informationi

Entry nameiHEM1_FRASN
AccessioniPrimary (citable) accession number: A8LDG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 4, 2007
Last modified: October 1, 2014
This is version 56 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, 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