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Protein

Glutamyl-tRNA reductase 2

Gene

hemA2

Organism
Anaeromyxobacter sp. (strain Fw109-5)
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 1 (hemA1), Glutamyl-tRNA reductase 2 (hemA2)
  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 sitei49 – 491NucleophileUniRule annotation
Sitei93 – 931Important for activityUniRule annotation
Binding sitei103 – 1031SubstrateUniRule annotation
Binding sitei114 – 1141SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi183 – 1886NADPUniRule 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

BioCyciASP404589:GHMT-1856-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase 2UniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTR 2UniRule annotation
Gene namesi
Name:hemA2UniRule annotation
Ordered Locus Names:Anae109_1845
OrganismiAnaeromyxobacter sp. (strain Fw109-5)
Taxonomic identifieri404589 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeAnaeromyxobacteraceaeAnaeromyxobacter
ProteomesiUP000006382 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 423423Glutamyl-tRNA reductase 2PRO_0000335008Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi404589.Anae109_1845.

Structurei

3D structure databases

ProteinModelPortaliA7HBF2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 514Substrate bindingUniRule annotation
Regioni108 – 1103Substrate 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.
HOGENOMiHOG000109651.
KOiK02492.
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.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A7HBF2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLVAVGLNQK GATVADREVL ALPAEGFQST LAEYAALDAV DEIAVMSTCY
60 70 80 90 100
RVEIYAATRC PAAATLSLRQ ALNARAGREL PLFELHGEEA YRHLVRVASS
110 120 130 140 150
LESAILGEPQ ILGQVKEAFQ RSIDQGVAAK ELTSVLNRAL SAAKRVRTDT
160 170 180 190 200
AIGRAGISWG HAAATLAEKV LGKMQGRRVV VVGAGEMARL SAQHLRDQGA
210 220 230 240 250
RIVVLNRTLV NGEALAREVG GVARPLEALG EELAQADVVV SAAPVAPDAF
260 270 280 290 300
QPEAMAELSR SRKRPIVLVD LAVPRAIPAA TGAIRDVYLC DVDDLDRVMK
310 320 330 340 350
AAMSERAAAV ADADRIIAEE VGKFVRAEAE RRAAPLIQEM RTRASAIARE
360 370 380 390 400
EVERTLRRLG EDPEVERRLE AMAGSIVSKI LHAPSARLRQ AVCDGCSGEA
410 420
LVSAAVEIFE LSADIRVHRG NAA
Length:423
Mass (Da):45,130
Last modified:May 20, 2008 - v2
Checksum:i494272D1FBFC0093
GO

Sequence cautioni

The sequence ABS26048.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000769 Genomic DNA. Translation: ABS26048.1. Different initiation.
RefSeqiWP_012096626.1. NC_009675.1.
YP_001379032.1. NC_009675.1.

Genome annotation databases

EnsemblBacteriaiABS26048; ABS26048; Anae109_1845.
KEGGiafw:Anae109_1845.
PATRICi20928931. VBIAnaSp113478_1943.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000769 Genomic DNA. Translation: ABS26048.1. Different initiation.
RefSeqiWP_012096626.1. NC_009675.1.
YP_001379032.1. NC_009675.1.

3D structure databases

ProteinModelPortaliA7HBF2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi404589.Anae109_1845.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABS26048; ABS26048; Anae109_1845.
KEGGiafw:Anae109_1845.
PATRICi20928931. VBIAnaSp113478_1943.

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109651.
KOiK02492.
OrthoDBiEOG6MWNBM.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.
BioCyciASP404589:GHMT-1856-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.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Fw109-5.

Entry informationi

Entry nameiHEM12_ANADF
AccessioniPrimary (citable) accession number: A7HBF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: April 1, 2015
This is version 61 of the entry and version 2 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.