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A1VKB7

- HEM1_POLNA

UniProt

A1VKB7 - HEM1_POLNA

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Pnap_0776
Organism
Polaromonas naphthalenivorans (strain CJ2)
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 sitei51 – 511Nucleophile By similarity
Sitei98 – 981Important for activity By similarity
Binding sitei108 – 1081Substrate By similarity
Binding sitei119 – 1191Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi188 – 1936NADP 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

BioCyciPNAP365044:GJ8X-785-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:Pnap_0776
OrganismiPolaromonas naphthalenivorans (strain CJ2)
Taxonomic identifieri365044 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaePolaromonas
ProteomesiUP000000644: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 429429Glutamyl-tRNA reductaseUniRule annotation
PRO_0000335057Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi365044.Pnap_0776.

Structurei

3D structure databases

ProteinModelPortaliA1VKB7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 534Substrate binding By similarity
Regioni113 – 1153Substrate 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.
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]
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.

A1VKB7-1 [UniParc]FASTAAdd to Basket

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MSVWALGLNH HTAPLDLRGR FAFAIDQIEP TLRGLRASLA RQPEATLLST    50
CNRTEIYCAG DTNDLDSTME WLAHNGGVSP SLLRAHAYTL QDDQAARHAF 100
RVASGLDSMV LGEPQILGQM KDAVRAAEDA GAMGTTLHQL FQRSFAVAKE 150
VRTSTEIGAH SISMAAAAVR LAGQLFEDLG DIKVLFVGAG EMIDLAATHF 200
AAKNPKAMAI ANRSLDRGEK LASRFGAEVM RLGDLPGRLH EFDAVISCTA 250
STLPIIGLGA VERALKRRKH RPMFMVDLAV PRDIEPEVKE LSDIYLYTVD 300
DLAHVVQTGR DSRQAAVAEA EVIIDAGVQN FMHWLDQRGS VPLIQQLNAQ 350
ADAWRAAEIV RAKKLLARGE SIEEVLEAMS RGLTQKMLHG AMAELHAGDA 400
SSREATARTV SKLFLRGQMP RAATERKER 429
Length:429
Mass (Da):46,754
Last modified:February 6, 2007 - v1
Checksum:i8C2F21079F18F6A8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000529 Genomic DNA. Translation: ABM36095.1.
RefSeqiYP_981016.1. NC_008781.1.

Genome annotation databases

EnsemblBacteriaiABM36095; ABM36095; Pnap_0776.
GeneIDi4689755.
KEGGipna:Pnap_0776.
PATRICi22946077. VBIPolNap76733_1600.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000529 Genomic DNA. Translation: ABM36095.1 .
RefSeqi YP_981016.1. NC_008781.1.

3D structure databases

ProteinModelPortali A1VKB7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 365044.Pnap_0776.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABM36095 ; ABM36095 ; Pnap_0776 .
GeneIDi 4689755.
KEGGi pna:Pnap_0776.
PATRICi 22946077. VBIPolNap76733_1600.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci PNAP365044:GJ8X-785-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: CJ2.

Entry informationi

Entry nameiHEM1_POLNA
AccessioniPrimary (citable) accession number: A1VKB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 6, 2007
Last modified: September 3, 2014
This is version 64 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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