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Q6D552

- HEM1_PECAS

UniProt

Q6D552 - HEM1_PECAS

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Protein
Glutamyl-tRNA reductase
Gene
hemA, ECA2189
Organism
Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia carotovora subsp. atroseptica)
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
Sitei99 – 991Important for activity By similarity
Binding sitei109 – 1091Substrate By similarity
Binding sitei120 – 1201Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 1946NADP 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

BioCyciPATR218491:GJNB-2230-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:ECA2189
OrganismiPectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia carotovora subsp. atroseptica)
Taxonomic identifieri218491 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium
ProteomesiUP000007966: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 418418Glutamyl-tRNA reductaseUniRule annotation
PRO_0000114026Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi218491.ECA2189.

Structurei

3D structure databases

ProteinModelPortaliQ6D552.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni114 – 1163Substrate 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.

Q6D552-1 [UniParc]FASTAAdd to Basket

« Hide

MTLLALGINH KTAPVSLRER VVFSQDKLGV ALDSLLQQPL VQGGVVLSTC    50
NRTELYLSVD EQENQREQLI RWLCEYHQLR PEEVNSSLYW HQGNAAVSHL 100
MRVASGLDSL VLGEPQILGQ VKKAFAESQR GHSLSSELER LFQKSFTVAK 150
RVRTETDIGA SAVSVAFAAC TLARQIFESL ADVTVLLVGA GETIELVARY 200
LRDHNVQKMV IANRTRERAQ ALATEVGAEV ITLAELDEQL VHADIVISST 250
ASTLPIIGKG MMERTLKARR NQPMLMVDIA VPRDIEPEVG KLPNVYLYSV 300
DDLHAIIQHN LAQRKAAAVQ AESIVQQESS DFMAWLRAQS AVETIRDYRA 350
QADELRAEMT AKALAAIQQG NDVEAVIQEL THRLTNRLIH APTKSLQQAA 400
RDGDQNRLQI LRDSLGLD 418
Length:418
Mass (Da):46,329
Last modified:August 16, 2004 - v1
Checksum:iFA709EEE23990F45
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX950851 Genomic DNA. Translation: CAG75091.1.
RefSeqiWP_011093748.1. NC_004547.2.
YP_050283.1. NC_004547.2.

Genome annotation databases

EnsemblBacteriaiCAG75091; CAG75091; ECA2189.
GeneIDi2885594.
KEGGieca:ECA2189.
PATRICi20479674. VBIPecAtr54885_2223.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX950851 Genomic DNA. Translation: CAG75091.1 .
RefSeqi WP_011093748.1. NC_004547.2.
YP_050283.1. NC_004547.2.

3D structure databases

ProteinModelPortali Q6D552.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 218491.ECA2189.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAG75091 ; CAG75091 ; ECA2189 .
GeneIDi 2885594.
KEGGi eca:ECA2189.
PATRICi 20479674. VBIPecAtr54885_2223.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci PATR218491:GJNB-2230-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: SCRI 1043 / ATCC BAA-672.

Entry informationi

Entry nameiHEM1_PECAS
AccessioniPrimary (citable) accession number: Q6D552
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: August 16, 2004
Last modified: September 3, 2014
This is version 79 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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