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B5EBG7

- HEM1_GEOBB

UniProt

B5EBG7 - HEM1_GEOBB

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Gbem_0407
Organism
Geobacter bemidjiensis (strain Bem / ATCC BAA-1014 / DSM 16622)
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

BioCyciGBEM404380:GHFR-409-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:Gbem_0407
OrganismiGeobacter bemidjiensis (strain Bem / ATCC BAA-1014 / DSM 16622)
Taxonomic identifieri404380 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter
ProteomesiUP000008825: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434Glutamyl-tRNA reductaseUniRule annotation
PRO_1000093139Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi404380.Gbem_0407.

Structurei

3D structure databases

ProteinModelPortaliB5EBG7.

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.
HOGENOMiHOG000109651.
KOiK02492.
OMAiHEVTGEY.
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.

B5EBG7-1 [UniParc]FASTAAdd to Basket

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MNIIVVGLSH KTAAVEIREK VAFAPTQMEK PLQAVVALPD ITEAVIVSTC    50
NRVEIYATTR DVAGGMARIK RFLADYHNVP LELLEKHLYS YHGEDATRHV 100
FRVASSLDSM VVGEPQILGQ IKTSYGYAAE YKSSGIILNR FLHKAFSVAK 150
RVRTETKIAS SAVSVAFAAV ELAKKIFGEL SDKTVLLIGA GEMCELAAKH 200
FINTGVRGVM VTNRTYERAE KLAEEFDAKP VHFEALMETL PKADIILSST 250
GAPHFIIHEK DMEEVLRRRK HKPMFFIDIA VPRDIDPKVN NVENCYLYTV 300
DDLNGVVATN LEQRKVEAAK AEAIVEQEIG QFFKWLSSLE VTPTIVALRT 350
HFDEIRKAEL SKTISGWKDL PPGAEKKLDA LTNAIMNKLL HQPTSVLKRI 400
DQGNRNDLYV DALRNLFDLE VGGESQDNMM ELED 434
Length:434
Mass (Da):48,493
Last modified:October 14, 2008 - v1
Checksum:i28B570D80CAFEE73
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001124 Genomic DNA. Translation: ACH37436.1.
RefSeqiYP_002137232.1. NC_011146.1.

Genome annotation databases

EnsemblBacteriaiACH37436; ACH37436; Gbem_0407.
GeneIDi6783233.
KEGGigbm:Gbem_0407.
PATRICi21984477. VBIGeoBem56306_0403.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001124 Genomic DNA. Translation: ACH37436.1 .
RefSeqi YP_002137232.1. NC_011146.1.

3D structure databases

ProteinModelPortali B5EBG7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 404380.Gbem_0407.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACH37436 ; ACH37436 ; Gbem_0407 .
GeneIDi 6783233.
KEGGi gbm:Gbem_0407.
PATRICi 21984477. VBIGeoBem56306_0403.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci GBEM404380:GHFR-409-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: Bem / ATCC BAA-1014 / DSM 16622.

Entry informationi

Entry nameiHEM1_GEOBB
AccessioniPrimary (citable) accession number: B5EBG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 14, 2008
Last modified: September 3, 2014
This is version 48 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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