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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201)
Status
Reviewed-Annotation score: 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

Pathway: 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei47 – 471NucleophileUniRule annotation
Sitei101 – 1011Important for activityUniRule annotation
Binding sitei111 – 1111SubstrateUniRule annotation
Binding sitei122 – 1221SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi192 – 1976NADPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciKRHI378753:GJ8F-864-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:KRH_08480
OrganismiKocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201)
Taxonomic identifieri378753 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrococcaceaeKocuria
ProteomesiUP000008838 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 437437Glutamyl-tRNA reductasePRO_1000190532Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi378753.KRH_08480.

Structurei

3D structure databases

ProteinModelPortaliB2GL19.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni46 – 494Substrate bindingUniRule annotation
Regioni116 – 1183Substrate 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.
OMAiEHAPAEH.
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.

B2GL19-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLFCLVASH RTVDLNTVAR LSTGALGVAE DAVSRGALAG AITLSTCNRL
60 70 80 90 100
ELYGELPEHA SVDVPGAQQQ LAERIARRAG LDERFVLETM DAYEGPEVPR
110 120 130 140 150
HLFTVVSGLE SAVVGEREIT GQVRRALAGA QQSGTASPHL VQLFEAAART
160 170 180 190 200
AREVGASTGL GERGRSIVSV ALDLADDITS GDWPERHALV FGTGAYAGAT
210 220 230 240 250
MAALRDRGCA DIEVYSGSGR AQQFTDQRGG SPVTDESLPG ALRRADVIIG
260 270 280 290 300
CSGGSAPMPA SRFPAGPRTV VDLALARDFD PAVADLPNVE LITLESVRVA
310 320 330 340 350
APEETRESVA AAREIVERAA RDFENARTAR SMDQAIVALR KHTMAVLDAE
360 370 380 390 400
LDKVRTHHGC TGAEEQIEMA MRRMVRSLLH TPTVRARQLA AEGRADEYIT
410 420 430
GLEALYGLEV AVPDVPEETA PSTRQDPSDT PRPRAVG
Length:437
Mass (Da):46,442
Last modified:June 10, 2008 - v1
Checksum:i5C9A0BA85B99378A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009152 Genomic DNA. Translation: BAG29195.1.
RefSeqiWP_012397916.1. NC_010617.1.
YP_001854701.1. NC_010617.1.

Genome annotation databases

EnsemblBacteriaiBAG29195; BAG29195; KRH_08480.
KEGGikrh:KRH_08480.
PATRICi22181910. VBIKocRhi5258_0824.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009152 Genomic DNA. Translation: BAG29195.1.
RefSeqiWP_012397916.1. NC_010617.1.
YP_001854701.1. NC_010617.1.

3D structure databases

ProteinModelPortaliB2GL19.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi378753.KRH_08480.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAG29195; BAG29195; KRH_08480.
KEGGikrh:KRH_08480.
PATRICi22181910. VBIKocRhi5258_0824.

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109649.
KOiK02492.
OMAiEHAPAEH.
OrthoDBiEOG6MWNBM.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.
BioCyciKRHI378753:GJ8F-864-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 9341 / DSM 348 / NBRC 103217 / DC2201.

Entry informationi

Entry nameiHEM1_KOCRD
AccessioniPrimary (citable) accession number: B2GL19
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 10, 2008
Last modified: June 24, 2015
This is version 60 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.