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Q65SX9

- HEM1_MANSM

UniProt

Q65SX9 - HEM1_MANSM

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Protein
Glutamyl-tRNA reductase
Gene
hemA, MS1324
Organism
Mannheimia succiniciproducens (strain MBEL55E)
Status
Reviewed - 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) By similarity.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 – 501Nucleophile By similarity
Sitei107 – 1071Important for activity By similarity
Binding sitei117 – 1171Substrate By similarity
Binding sitei128 – 1281Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi202 – 2076NADP By similarity

GO - Molecular functioni

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

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 reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
Ordered Locus Names:MS1324
OrganismiMannheimia succiniciproducens (strain MBEL55E)
Taxonomic identifieri221988 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeBasfia
ProteomesiUP000000607: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Glutamyl-tRNA reductaseUniRule annotation
PRO_0000114038Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi221988.MS1324.

Structurei

3D structure databases

ProteinModelPortaliQ65SX9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni122 – 1243Substrate binding By similarity

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 By similarity.UniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109650.
KOiK02492.
OMAiLAHKLTN.
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

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MTILVLGINH KTASVALREK VAFSPEKRDL AFQQIAQSEL AQSEVILSTC    50
NRTEIYLHNK HISPEADQEN QRWLEQCIQW FADVHQLDVD ELRNCLYIKQ 100
NQSAVNHLMR VSCGLDSLVL GEPQILGQVK QAYQYSEDYC QAQHMPMSSE 150
FSRLFQKTFS VAKRVRTETN IGNSAVSVAY AACSLARQIF EGLKDLNILL 200
VGAGETIELV ARHLLRHGVK KLMISNRTLA RAELLVEKLE HNKYIQVLSL 250
QQLQDGLNQA DIVISSTGSP IVLITAEMVK QAQQKRRNAP MLIVDIAVPR 300
DVDERVEKLD GVYHYTVDDL HSIIQRNLSE REKASKEAET IIDAEASDFF 350
EWMKVHQFSN LIRTYRESAE QIRQDLLEKA VQAIGQNEDP ETVLQELSYK 400
LMNKLIHSPT QAMQAMMKQG SIQGLRSFSS ALGIADKKER NPQK 444
Length:444
Mass (Da):50,410
Last modified:October 25, 2004 - v1
Checksum:i758DB351D24DE442
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016827 Genomic DNA. Translation: AAU37931.1.
RefSeqiWP_011200498.1. NC_006300.1.
YP_088516.1. NC_006300.1.

Genome annotation databases

EnsemblBacteriaiAAU37931; AAU37931; MS1324.
GeneIDi3074755.
KEGGimsu:MS1324.
PATRICi22445965. VBIManSuc86752_1208.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016827 Genomic DNA. Translation: AAU37931.1 .
RefSeqi WP_011200498.1. NC_006300.1.
YP_088516.1. NC_006300.1.

3D structure databases

ProteinModelPortali Q65SX9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 221988.MS1324.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAU37931 ; AAU37931 ; MS1324 .
GeneIDi 3074755.
KEGGi msu:MS1324.
PATRICi 22445965. VBIManSuc86752_1208.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109650.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci BMAN221988:GHGM-1365-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00087. Glu_tRNA_reductase.
InterProi IPR000343. 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 ]
Pfami PF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMi SSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsi TIGR01035. hemA. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(2004) [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: February 1, 2005
Last sequence update: October 25, 2004
Last modified: September 3, 2014
This is version 73 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 By similarity.

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3