UniProtKB - A1SV88 (HEM1_PSYIN)
(max 400 entries)x
Your basket is currently empty. i
Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)
Protein
Glutamyl-tRNA reductase
Gene
hemA
Organism
Psychromonas ingrahamii (strain 37)
Status
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
Catalytic activityi
L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotation
: protoporphyrin-IX biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).UniRule annotationProteins known to be involved in the 2 steps of the subpathway in this organism are:
- Glutamyl-tRNA reductase (hemA)
- Glutamate-1-semialdehyde 2,1-aminomutase (hemL)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 50 | NucleophileUniRule annotation | 1 | |
Sitei | 97 | Important for activityUniRule annotation | 1 | |
Binding sitei | 107 | SubstrateUniRule annotation | 1 | |
Binding sitei | 118 | SubstrateUniRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 187 – 192 | NADPUniRule annotation | 6 |
GO - Molecular functioni
- glutamyl-tRNA reductase activity Source: UniProtKB-EC
- NADP binding Source: InterPro
GO - Biological processi
- protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Porphyrin biosynthesis |
Ligand | NADP |
Enzyme and pathway databases
BioCyci | PING357804:G1G7R-1699-MONOMER. |
UniPathwayi | UPA00251; 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:Ping_1606 |
Organismi | Psychromonas ingrahamii (strain 37) |
Taxonomic identifieri | 357804 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Psychromonadaceae › Psychromonas › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_1000004678 | 1 – 419 | Glutamyl-tRNA reductaseAdd BLAST | 419 |
Interactioni
Subunit structurei
Homodimer.UniRule annotation
Protein-protein interaction databases
STRINGi | 357804.Ping_1606. |
Structurei
3D structure databases
ProteinModelPortali | A1SV88. |
SMRi | A1SV88. |
ModBasei | Search... |
MobiDBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 49 – 52 | Substrate bindingUniRule annotation | 4 | |
Regioni | 112 – 114 | Substrate bindingUniRule annotation | 3 |
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
eggNOGi | ENOG4105C7E. Bacteria. COG0373. LUCA. |
HOGENOMi | HOG000109650. |
KOi | K02492. |
OMAi | FAFKCAA. |
OrthoDBi | POG091H05DA. |
Family and domain databases
Gene3Di | 3.30.460.30. 1 hit. |
HAMAPi | MF_00087. Glu_tRNA_reductase. 1 hit. |
InterProi | View protein in InterPro IPR000343. 4pyrrol_synth_GluRdtase. IPR015896. 4pyrrol_synth_GluRdtase_dimer. IPR015895. 4pyrrol_synth_GluRdtase_N. IPR018214. GluRdtase_CS. IPR036453. GluRdtase_dimer_dom_sf. IPR036343. GluRdtase_N_sf. IPR036291. NAD(P)-bd_dom_sf. IPR006151. Shikm_DH/Glu-tRNA_Rdtase. |
Pfami | View protein in Pfam PF00745. GlutR_dimer. 1 hit. PF05201. GlutR_N. 1 hit. PF01488. Shikimate_DH. 1 hit. |
PIRSFi | PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit. |
SUPFAMi | SSF51735. SSF51735. 1 hit. SSF69075. SSF69075. 1 hit. SSF69742. SSF69742. 1 hit. |
TIGRFAMsi | TIGR01035. hemA. 1 hit. |
PROSITEi | View protein in PROSITE PS00747. GLUTR. 1 hit. |
i Sequence
Sequence statusi: Complete.
A1SV88-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MPLFALGINH QTASVALREK VAFSADLLLD AYQALLAQPT VLEAVIVSTC
60 70 80 90 100
NRTEIYCHLK QDNCDEVIKW LCSFHQIEDH KLRPSLYCYS EYQAIQHLFR
110 120 130 140 150
VSCGLDSLVL GEPQILGQIK QAFATAKQAK GVDKIVQKWF QHTFTVAKRV
160 170 180 190 200
RTETQIGANA ISVAFAAVCL AKQIFSDLSQ SRVLLIGAGE TIELVGKYLI
210 220 230 240 250
EHQVPNITIA NRTLSRAMAL VEQFDAQAIT LGEIPNHLAQ ADIIISSTAS
260 270 280 290 300
PLPIIGKGMV ERALKARRNR PMLFIDIAVP RDIEAEVSEL RDIYLYSVDD
310 320 330 340 350
LQGIIEENKQ ARQVAALEAE KIIDGCIVDF ISWIESLKAV ESIRTYRQNS
360 370 380 390 400
EQLRDDLLNR ASAALQNGEE AENVLKELAF KLTNKLIHHP SLALNETARS
410
GNDDELILLR NALGLSKKD
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP000510 Genomic DNA. Translation: ABM03403.1. |
RefSeqi | WP_011769963.1. NC_008709.1. |
Genome annotation databases
EnsemblBacteriai | ABM03403; ABM03403; Ping_1606. |
KEGGi | pin:Ping_1606. |
Similar proteinsi
Entry informationi
Entry namei | HEM1_PSYIN | |
Accessioni | A1SV88Primary (citable) accession number: A1SV88 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 15, 2008 |
Last sequence update: | February 6, 2007 | |
Last modified: | March 28, 2018 | |
This is version 82 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |