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A8LDG7

- HEM1_FRASN

UniProt

A8LDG7 - HEM1_FRASN

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Franean1_6131
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) 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
Sitei99 – 991Important for activity By similarity
Binding sitei109 – 1091Substrate By similarity
Binding sitei120 – 1201Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi229 – 2346NADP 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

BioCyciFSP298653:GHPI-6162-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: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 reductaseUniRule annotation
PRO_1000093137Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi298653.Franean1_6131.

Structurei

3D structure databases

ProteinModelPortaliA8LDG7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni114 – 1163Substrate 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.
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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MSLLAVGLNH RTAPTSLLEL AAVSADDAPK VLHDLVGADH LSEAVLLSTC    50
NRTEIYAEVE TFHGGLADIS DQLSRVCGVP LTDLASHLYV HHEARAVSHL 100
FSVVCGLDSM LVGETQILGQ VRAAFRLAQA AEVTSGTLAN LFQTALRVGK 150
RAHTETSIDA AGASIVSVGV RMAAFDLQAR RPDMLVAPVA SPGCDPGDAV 200
EALLRPELTA PVEVAGPAPL AGARVLIIGA GAVGSLAAQT VRRAGAGDVV 250
VANRTAARAA RVADLHDARA VGLAEIAHEV GRADLVISST GASGLVVGHD 300
AVRASLAGRG ARPLVFLDLA LPRDIDPAVR ELPGVTLIDI EALRVALDGA 350
QVAHDVEAVR ALVTTEVAGF LDRRRAERVA PTVVALRAHA AAVVRDELER 400
LRTRLPDLDN REWDMVSGTV RRVVDKLLHA PTVRVQQLAE APGGDSYAEA 450
LRELFDLPRD VPAIVSAPDL DLVERT 476
Length:476
Mass (Da):49,893
Last modified:December 4, 2007 - v1
Checksum:iD40B3C26E5B8FC79
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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: September 3, 2014
This is version 55 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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