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A1AUE9

- HEM1_PELPD

UniProt

A1AUE9 - HEM1_PELPD

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Pelobacter propionicus (strain DSM 2379)
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).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 – 501NucleophileUniRule annotation
Sitei99 – 991Important for activityUniRule annotation
Binding sitei109 – 1091SubstrateUniRule annotation
Binding sitei120 – 1201SubstrateUniRule annotation

Regions

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

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

BioCyciPPRO338966:GHL0-3435-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTRUniRule annotation
Gene namesi
Name:hemAUniRule annotation
Ordered Locus Names:Ppro_3377
OrganismiPelobacter propionicus (strain DSM 2379)
Taxonomic identifieri338966 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesPelobacteraceaePelobacter
ProteomesiUP000006732: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 436436Glutamyl-tRNA reductasePRO_1000004660Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi338966.Ppro_3377.

Structurei

3D structure databases

ProteinModelPortaliA1AUE9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni114 – 1163Substrate bindingUniRule annotation

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.UniRule annotation

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109651.
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.

A1AUE9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNIIVVGLSH KTAPVEVRER VAFSPNLIER PLRELVSLDD ISEGVIVSTC
60 70 80 90 100
NRVEIYATTH DIAGGTARIK RFLADHHRIP LESLEQYLYS YHSEAAIRHV
110 120 130 140 150
FRVASSLDSM VVGEPQILGQ IKTAYGYAAE YRTSGTILNR FLHKAFSVAK
160 170 180 190 200
RVRTETRIAS SAVSVAFAAV ELARKILGDL SGKTVMLIGA GEMCELAAKH
210 220 230 240 250
FLTSGARGLL VANRTFAKGE RLAAEFGGEA IPFEELFQEL HRADIVLSST
260 270 280 290 300
GAPHTIIAPR DVEAVVKRRK FKPMFFIDIA VPRDIDPRVN DLESAYLFTV
310 320 330 340 350
DDLQEIVEAN MAQRNQEASK GEEIVEQEIG QFHCWLSSLE STPTIVALRA
360 370 380 390 400
RFEEIRRAEL EKTLCGWKDL SPEAEKRLEI MTLSIMNKLL HTPTAVLKRA
410 420 430
GQGGRTDLYT DALRQLFDLQ TSRQDDDELE LELEEE
Length:436
Mass (Da):48,747
Last modified:January 23, 2007 - v1
Checksum:iB708C997F1666459
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000482 Genomic DNA. Translation: ABL00970.1.
RefSeqiWP_011737186.1. NC_008609.1.
YP_903027.1. NC_008609.1.

Genome annotation databases

EnsemblBacteriaiABL00970; ABL00970; Ppro_3377.
GeneIDi4572528.
KEGGippd:Ppro_3377.
PATRICi22899901. VBIPelPro64470_3536.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000482 Genomic DNA. Translation: ABL00970.1 .
RefSeqi WP_011737186.1. NC_008609.1.
YP_903027.1. NC_008609.1.

3D structure databases

ProteinModelPortali A1AUE9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 338966.Ppro_3377.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABL00970 ; ABL00970 ; Ppro_3377 .
GeneIDi 4572528.
KEGGi ppd:Ppro_3377.
PATRICi 22899901. VBIPelPro64470_3536.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci PPRO338966:GHL0-3435-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. "Complete sequence of chromosome of Pelobacter propionicus DSM 2379."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.
    , Land M., Hauser L., Kyrpides N., Kim E., Lovley D., Richardson P.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 2379.

Entry informationi

Entry nameiHEM1_PELPD
AccessioniPrimary (citable) accession number: A1AUE9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 61 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.UniRule annotation

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