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A9KSC2

- HEM12_CLOPH

UniProt

A9KSC2 - HEM12_CLOPH

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Protein

Glutamyl-tRNA reductase 2

Gene
hemA2, Cphy_1784
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 sitei50 – 501Nucleophile By similarity
Binding sitei106 – 1061Substrate By similarity
Binding sitei117 – 1171Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi186 – 1916NADP By similarity

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

BioCyciCPHY357809:GHCL-1824-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase 2 (EC:1.2.1.70)
Short name:
GluTR 2
Gene namesi
Name:hemA2
Ordered Locus Names:Cphy_1784
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 – 413413Glutamyl-tRNA reductase 2UniRule annotationPRO_0000335024Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi357809.Cphy_1784.

Structurei

3D structure databases

ProteinModelPortaliA9KSC2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni111 – 1133Substrate 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.
OMAiKSNANHV.
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]
SUPFAMiSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A9KSC2-1 [UniParc]FASTAAdd to Basket

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MNISMVGIDY NTASIEDREH FTLTSDKQLE IAKIIKETYH ASGCIILSTC    50
NRTEIWFSEL GTSEAECFHQ LVLGENAKET MRSICVCRQG DEAVTYLMEL 100
GCGIHSQIFG EDQILTQLKQ ALQQARDYQY VDSVLECLFR TAITAAKKVK 150
TSIQIAKGNT SLPQTIVEQL EKEQGDLLGK SCLVIGNGEM GRLMTEKLLE 200
KKCKVWMTLR QYKKSKAIIP EGSGVVLYDE RYEHIAVMDY IFSATKSHHF 250
TINKSMFENI RLKGKTYCLI DLAIPRDIEP SVEELSDVTV YNMDYFCQEV 300
NDREKELEET RELLSEYVNE FKQWYQFRNL VSTVDDISNI VSDITDAKLT 350
KVYKSIDLSR EQQELLQSNV QMAAKKAVSK IIFGLRDVLQ IDQCEEVLQA 400
LEQSAMNCTD SVK 413
Length:413
Mass (Da):47,150
Last modified:February 5, 2008 - v1
Checksum:i98276B1B10DCAAFA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000885 Genomic DNA. Translation: ABX42154.1.
RefSeqiYP_001558893.1. NC_010001.1.

Genome annotation databases

EnsemblBacteriaiABX42154; ABX42154; Cphy_1784.
GeneIDi5741457.
KEGGicpy:Cphy_1784.
PATRICi19503212. VBICloPhy16213_1845.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000885 Genomic DNA. Translation: ABX42154.1 .
RefSeqi YP_001558893.1. NC_010001.1.

3D structure databases

ProteinModelPortali A9KSC2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 357809.Cphy_1784.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABX42154 ; ABX42154 ; Cphy_1784 .
GeneIDi 5741457.
KEGGi cpy:Cphy_1784.
PATRICi 19503212. VBICloPhy16213_1845.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CPHY357809:GHCL-1824-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 ]
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700394 / DSM 18823 / ISDg.

Entry informationi

Entry nameiHEM12_CLOPH
AccessioniPrimary (citable) accession number: A9KSC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: September 3, 2014
This is version 54 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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