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Q1INI5

- HEM12_KORVE

UniProt

Q1INI5 - HEM12_KORVE

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Protein
Glutamyl-tRNA reductase 2
Gene
hemA2, Acid345_2564
Organism
Koribacter versatilis (strain Ellin345)
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
Sitei96 – 961Important for activity 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. 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

BioCyciKVER204669:GHL8-2586-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:Acid345_2564
OrganismiKoribacter versatilis (strain Ellin345)
Taxonomic identifieri204669 [NCBI]
Taxonomic lineageiBacteriaAcidobacteriaCandidatus Koribacter
ProteomesiUP000002432: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 436436Glutamyl-tRNA reductase 2UniRule annotation
PRO_0000334999Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi204669.Acid345_2564.

Structurei

3D structure databases

ProteinModelPortaliQ1INI5.

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.
HOGENOMiHOG000109651.
OMAiAITCGKK.
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.

Q1INI5-1 [UniParc]FASTAAdd to Basket

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MNFFVIGVNH KTAPVEVRER FAIPESRLPE ATKLLASYPG IEEGMIVSTC    50
NRVEMVARSV NGNADMRGFL KQLYNIDPAQ YEQYLYEYRS TEAVRHMFRV 100
ASSLDSMVVG EPQILGQVKE AYATARAVGA VSSQLDALLT RAFAVAKRVR 150
TDTSIASSSV SIASVAVELA KKIFGSLQGR SVYIVGAGKM CELAARHFVA 200
HGVEKIYVAN RTYERGVAFA KKFNGEAVPI EHLYETVDKA DIVLSSTGAP 250
IAIFRKEHGE KFLSRRKNRP MFFLDIAVPR DVDAKMNELD GIFVYDIDDL 300
QQVVHSHISD RKDEAAHAEA IVNAEVEKFE ERLRTLDVVP TIVSLQEHLE 350
TVRQAEIDRL RGRLGELSPE QEMAVDALTK GIINKIMHTP ITTLKTAAKE 400
PESTTVIELV KRIFNLHEKA KDETVKTGPP QSGPGK 436
Length:436
Mass (Da):48,410
Last modified:June 13, 2006 - v1
Checksum:i407B8A871D22A84C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000360 Genomic DNA. Translation: ABF41565.1.
RefSeqiYP_591639.1. NC_008009.1.

Genome annotation databases

EnsemblBacteriaiABF41565; ABF41565; Acid345_2564.
GeneIDi4072208.
KEGGiaba:Acid345_2564.
PATRICi31982188. VBICanKor57425_2730.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000360 Genomic DNA. Translation: ABF41565.1 .
RefSeqi YP_591639.1. NC_008009.1.

3D structure databases

ProteinModelPortali Q1INI5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 204669.Acid345_2564.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABF41565 ; ABF41565 ; Acid345_2564 .
GeneIDi 4072208.
KEGGi aba:Acid345_2564.
PATRICi 31982188. VBICanKor57425_2730.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
OMAi AITCGKK.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci KVER204669:GHL8-2586-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ellin345.

Entry informationi

Entry nameiHEM12_KORVE
AccessioniPrimary (citable) accession number: Q1INI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 13, 2006
Last modified: September 3, 2014
This is version 69 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, 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

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