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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).UniRule annotation

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

Caution

Lacks the conserved histidine residue in position 89 which is potentially part of the active site; it is replaced by a tyrosine residue.Curated

Catalytic activityi

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotation

Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamyl-tRNA reductase (hemA)
  2. Glutamate-1-semialdehyde 2,1-aminomutase (hemL)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu), the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei52NucleophileUniRule annotation1
Binding sitei99SubstrateUniRule annotation1
Binding sitei110SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi179 – 184NADPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processPorphyrin biosynthesis
LigandNADP

Enzyme and pathway databases

BioCyciFNUC190304:G1FZS-1232-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:FN0646
OrganismiFusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131)
Taxonomic identifieri190304 [NCBI]
Taxonomic lineageiBacteriaFusobacteriaFusobacterialesFusobacteriaceaeFusobacterium
Proteomesi
  • UP000002521 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001140271 – 329Glutamyl-tRNA reductaseAdd BLAST329

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi190304.FN0646

Structurei

3D structure databases

ProteinModelPortaliQ8R687
SMRiQ8R687
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni51 – 54Substrate bindingUniRule annotation4
Regioni104 – 106Substrate bindingUniRule annotation3

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

eggNOGiENOG4105C7E Bacteria
COG0373 LUCA
HOGENOMiHOG000109108
InParanoidiQ8R687
KOiK02492
OMAiMANLVIK

Family and domain databases

Gene3Di3.30.460.30, 1 hit
HAMAPiMF_00087 Glu_tRNA_reductase, 1 hit
InterProiView protein in InterPro
IPR000343 4pyrrol_synth_GluRdtase
IPR015895 4pyrrol_synth_GluRdtase_N
IPR018214 GluRdtase_CS
IPR036343 GluRdtase_N_sf
IPR036291 NAD(P)-bd_dom_sf
IPR006151 Shikm_DH/Glu-tRNA_Rdtase
PfamiView protein in Pfam
PF05201 GlutR_N, 1 hit
PF01488 Shikimate_DH, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
SSF69742 SSF69742, 1 hit
TIGRFAMsiTIGR01035 hemA, 1 hit
PROSITEiView protein in PROSITE
PS00747 GLUTR, 1 hit

Sequencei

Sequence statusi: Complete.

Q8R687-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLDLENIIVI GVSHENLSLL ERENFMRTRP KYIIERLYTE KKINAYINLS
60 70 80 90 100
TCLRTEFYIE LNSNIKAKEI KNLFSVDMIV KSRVEAIEYL FKVGCGFYSV
110 120 130 140 150
IKGEDQILAQ VKGAYAEALE NEHSSKFLNI IFNKSIELGK KFRTKSMIAH
160 170 180 190 200
NALSLEAISL KFIKSKFPNI EDKNIFILGI GELAQDILTL LTKEQLKNIY
210 220 230 240 250
IANRTYHKAE QIKKEFDIVN IVDYREKYPK MIEADVIISA TSAPHIVVEY
260 270 280 290 300
DKFVAQMKEN KDYLFIDLAV PRDVDERLAN FKNIEIYNLD DIWEVYHLNS
310 320
MNRDKLLEDY SYLIDEQMEK LIKTLNYYK
Length:329
Mass (Da):38,592
Last modified:June 1, 2002 - v1
Checksum:i675E1B115629E9E2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009951 Genomic DNA Translation: AAL94842.1
RefSeqiNP_603543.1, NC_003454.1
WP_011016556.1, NC_003454.1

Genome annotation databases

EnsemblBacteriaiAAL94842; AAL94842; FN0646
GeneIDi993220
KEGGifnu:FN0646
PATRICifig|190304.8.peg.1210

Similar proteinsi

Entry informationi

Entry nameiHEM1_FUSNN
AccessioniPrimary (citable) accession number: Q8R687
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: June 1, 2002
Last modified: March 28, 2018
This is version 101 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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