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B8IZD9

- HEM1_DESDA

UniProt

B8IZD9 - HEM1_DESDA

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Protein

Glutamyl-tRNA reductase

Gene
hemA, Ddes_0959
Organism
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
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. 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

BioCyciDDES525146:GIWF-988-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:Ddes_0959
OrganismiDesulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Taxonomic identifieri525146 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
ProteomesiUP000002598: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 430430Glutamyl-tRNA reductaseUniRule annotationPRO_1000190520Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi525146.Ddes_0959.

Structurei

3D structure databases

ProteinModelPortaliB8IZD9.

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.
HOGENOMiHOG000109651.
KOiK02492.
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.

B8IZD9-1 [UniParc]FASTAAdd to Basket

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MDCDIFLVGL NHRTAGVDVR ERFALANHCD EEHWALPCTG AVSESIILST    50
CNRVEILAAG TGEVAEQVLR NWAGARKSDV EDLRPYVYVH KNLEAVRHLF 100
SVASSLDSMV LGEPQILGQL KTAYRKAVKS RATGVILNRL LHKAFSVAKR 150
VRTETAVASS AVSISYAAVE LAKRIFGDMR AHKAMLVGAG EMAELAAMHL 200
LQAGIADILV ANRTLVRGQE LAKQFNGHAI PFEDMPRHLL DVDIIITSTG 250
SQEPIIRARD IRAALKIRKN RPMFFIDIAV PRDIDPDVNG LDNVYLYDID 300
DLKEVVEENL ATRRDEAAKA AEIVNEEVVQ FSRWLASLDM QPTIVDLIKK 350
GQRAAEEELA KTLKRLGPVD DNTREALEAM AGALVRKLNH DPIMFLKHGG 400
MSQEGNGPRI SIMRRIFNLD KTGCIYSEEN 430
Length:430
Mass (Da):47,662
Last modified:March 3, 2009 - v1
Checksum:iF6C0AFD678B6B81C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001358 Genomic DNA. Translation: ACL48866.1.
RefSeqiWP_012624591.1. NC_011883.1.
YP_002479544.1. NC_011883.1.

Genome annotation databases

EnsemblBacteriaiACL48866; ACL48866; Ddes_0959.
GeneIDi7284639.
KEGGidds:Ddes_0959.
PATRICi21735548. VBIDesDes50650_1137.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001358 Genomic DNA. Translation: ACL48866.1 .
RefSeqi WP_012624591.1. NC_011883.1.
YP_002479544.1. NC_011883.1.

3D structure databases

ProteinModelPortali B8IZD9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 525146.Ddes_0959.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACL48866 ; ACL48866 ; Ddes_0959 .
GeneIDi 7284639.
KEGGi dds:Ddes_0959.
PATRICi 21735548. VBIDesDes50650_1137.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci DDES525146:GIWF-988-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 Desulfovibrio desulfuricans subsp. desulfuricans str. ATCC 27774."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L.
    , Kyrpides N., Ovchinnikova G., Hazen T.C.
    Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27774 / DSM 6949.

Entry informationi

Entry nameiHEM1_DESDA
AccessioniPrimary (citable) accession number: B8IZD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: September 3, 2014
This is version 42 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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