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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Mannheimia succiniciproducens (strain MBEL55E)
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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei50 – 501NucleophileUniRule annotation
Sitei107 – 1071Important for activityUniRule annotation
Binding sitei117 – 1171SubstrateUniRule annotation
Binding sitei128 – 1281SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi202 – 2076NADPUniRule annotation

GO - Molecular functioni

  1. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
  2. NADP binding Source: InterPro

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

BioCyciBMAN221988:GHGM-1365-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:MS1324
OrganismiMannheimia succiniciproducens (strain MBEL55E)
Taxonomic identifieri221988 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeBasfia
ProteomesiUP000000607 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Glutamyl-tRNA reductasePRO_0000114038Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi221988.MS1324.

Structurei

3D structure databases

ProteinModelPortaliQ65SX9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni122 – 1243Substrate 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.
HOGENOMiHOG000109650.
KOiK02492.
OMAiGAHSISM.
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.

Q65SX9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTILVLGINH KTASVALREK VAFSPEKRDL AFQQIAQSEL AQSEVILSTC
60 70 80 90 100
NRTEIYLHNK HISPEADQEN QRWLEQCIQW FADVHQLDVD ELRNCLYIKQ
110 120 130 140 150
NQSAVNHLMR VSCGLDSLVL GEPQILGQVK QAYQYSEDYC QAQHMPMSSE
160 170 180 190 200
FSRLFQKTFS VAKRVRTETN IGNSAVSVAY AACSLARQIF EGLKDLNILL
210 220 230 240 250
VGAGETIELV ARHLLRHGVK KLMISNRTLA RAELLVEKLE HNKYIQVLSL
260 270 280 290 300
QQLQDGLNQA DIVISSTGSP IVLITAEMVK QAQQKRRNAP MLIVDIAVPR
310 320 330 340 350
DVDERVEKLD GVYHYTVDDL HSIIQRNLSE REKASKEAET IIDAEASDFF
360 370 380 390 400
EWMKVHQFSN LIRTYRESAE QIRQDLLEKA VQAIGQNEDP ETVLQELSYK
410 420 430 440
LMNKLIHSPT QAMQAMMKQG SIQGLRSFSS ALGIADKKER NPQK
Length:444
Mass (Da):50,410
Last modified:October 24, 2004 - v1
Checksum:i758DB351D24DE442
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016827 Genomic DNA. Translation: AAU37931.1.
RefSeqiYP_088516.1. NC_006300.1.

Genome annotation databases

EnsemblBacteriaiAAU37931; AAU37931; MS1324.
KEGGimsu:MS1324.
PATRICi22445965. VBIManSuc86752_1208.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016827 Genomic DNA. Translation: AAU37931.1.
RefSeqiYP_088516.1. NC_006300.1.

3D structure databases

ProteinModelPortaliQ65SX9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi221988.MS1324.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAU37931; AAU37931; MS1324.
KEGGimsu:MS1324.
PATRICi22445965. VBIManSuc86752_1208.

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109650.
KOiK02492.
OMAiGAHSISM.
OrthoDBiEOG6MWNBM.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.
BioCyciBMAN221988:GHGM-1365-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. "The genome sequence of the capnophilic rumen bacterium Mannheimia succiniciproducens."
    Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H., Jeong H., Hur C.G., Kim J.J.
    Nat. Biotechnol. 22:1275-1281(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MBEL55E.

Entry informationi

Entry nameiHEM1_MANSM
AccessioniPrimary (citable) accession number: Q65SX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2005
Last sequence update: October 24, 2004
Last modified: March 31, 2015
This is version 77 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.