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A9KP81

- HEM11_CLOPH

UniProt

A9KP81 - HEM11_CLOPH

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Protein
Glutamyl-tRNA reductase 1
Gene
hemA1, Cphy_1368
Organism
Clostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
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 sitei46 – 461Nucleophile By similarity
Sitei93 – 931Important for activity By similarity
Binding sitei103 – 1031Substrate By similarity
Binding sitei114 – 1141Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi183 – 1886NADP By similarity

GO - Molecular functioni

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

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

BioCyciCPHY357809:GHCL-1410-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase 1 (EC:1.2.1.70)
Short name:
GluTR 1
Gene namesi
Name:hemA1
Ordered Locus Names:Cphy_1368
OrganismiClostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
Taxonomic identifieri357809 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesLachnospiraceae
ProteomesiUP000000370: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 403403Glutamyl-tRNA reductase 1UniRule annotation
PRO_0000335023Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi357809.Cphy_1368.

Structurei

3D structure databases

ProteinModelPortaliA9KP81.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 484Substrate binding By similarity
Regioni108 – 1103Substrate 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.
HOGENOMiHOG000069583.
KOiK02492.
OMAiAETEIQG.
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.
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]
SUPFAMiSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.

Sequencei

Sequence statusi: Complete.

A9KP81-1 [UniParc]FASTAAdd to Basket

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MLGIDHNKAS IEEREIFSFT KKMAADVLLN IKEIEGINGC IILSTCNRME    50
VWVSCFEEFE TSIYEILCSI KKVDDNRYRH CFIERGGYDA IEHLFYMTCG 100
LKSKIIGEDQ ILTQVREALE LSRENYCTDS VLETLFRFAI TSAKQVKTQI 150
HLSVVNSSVI HHVVHELKLS NYLFKGKKCL VIGNGEMGKL AATKLEEEGS 200
DVTVTVRQYR SGIIEIPVGC NRINYGDRLE HIVEYDFVIS ATSSPNMTIH 250
LEQLSNLEFK KPVLFIDLAV PRDIDPRITE LKNITLYDID HFKVETVSDE 300
MKTQLRQIDE ILKTKMDEFI SWYECRGIIK VVQTLSENAA IDVGLRIDKT 350
MKKIEMDSND KELLAATVHS ATNKVVSKLM FGLRDHVSAA TFQECMVALK 400
NIY 403
Length:403
Mass (Da):46,029
Last modified:February 5, 2008 - v1
Checksum:i497F1715C4F6418F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000885 Genomic DNA. Translation: ABX41743.1.
RefSeqiWP_012199397.1. NC_010001.1.
YP_001558482.1. NC_010001.1.

Genome annotation databases

EnsemblBacteriaiABX41743; ABX41743; Cphy_1368.
GeneIDi5742318.
KEGGicpy:Cphy_1368.
PATRICi19502358. VBICloPhy16213_1418.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000885 Genomic DNA. Translation: ABX41743.1 .
RefSeqi WP_012199397.1. NC_010001.1.
YP_001558482.1. NC_010001.1.

3D structure databases

ProteinModelPortali A9KP81.
ModBasei Search...

Protein-protein interaction databases

STRINGi 357809.Cphy_1368.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABX41743 ; ABX41743 ; Cphy_1368 .
GeneIDi 5742318.
KEGGi cpy:Cphy_1368.
PATRICi 19502358. VBICloPhy16213_1418.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000069583.
KOi K02492.
OMAi AETEIQG.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CPHY357809:GHCL-1410-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.
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 ]
SUPFAMi SSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsi TIGR01035. hemA. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700394 / DSM 18823 / ISDg.

Entry informationi

Entry nameiHEM11_CLOPH
AccessioniPrimary (citable) accession number: A9KP81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: September 3, 2014
This is version 55 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

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