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B5EBG7

- HEM1_GEOBB

UniProt

B5EBG7 - HEM1_GEOBB

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Protein

Glutamyl-tRNA reductase

Gene

hemA

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).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

BioCyciGBEM404380:GHFR-409-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: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 reductasePRO_1000093139Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi404380.Gbem_0407.

Structurei

3D structure databases

ProteinModelPortaliB5EBG7.
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.
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

« Hide

        10         20         30         40         50
MNIIVVGLSH KTAAVEIREK VAFAPTQMEK PLQAVVALPD ITEAVIVSTC
60 70 80 90 100
NRVEIYATTR DVAGGMARIK RFLADYHNVP LELLEKHLYS YHGEDATRHV
110 120 130 140 150
FRVASSLDSM VVGEPQILGQ IKTSYGYAAE YKSSGIILNR FLHKAFSVAK
160 170 180 190 200
RVRTETKIAS SAVSVAFAAV ELAKKIFGEL SDKTVLLIGA GEMCELAAKH
210 220 230 240 250
FINTGVRGVM VTNRTYERAE KLAEEFDAKP VHFEALMETL PKADIILSST
260 270 280 290 300
GAPHFIIHEK DMEEVLRRRK HKPMFFIDIA VPRDIDPKVN NVENCYLYTV
310 320 330 340 350
DDLNGVVATN LEQRKVEAAK AEAIVEQEIG QFFKWLSSLE VTPTIVALRT
360 370 380 390 400
HFDEIRKAEL SKTISGWKDL PPGAEKKLDA LTNAIMNKLL HQPTSVLKRI
410 420 430
DQGNRNDLYV DALRNLFDLE VGGESQDNMM ELED
Length:434
Mass (Da):48,493
Last modified:October 14, 2008 - v1
Checksum:i28B570D80CAFEE73
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001124 Genomic DNA. Translation: ACH37436.1.
RefSeqiWP_012528844.1. NC_011146.1.
YP_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:
EMBLi
GenBanki
DDBJi
Links Updated
CP001124 Genomic DNA. Translation: ACH37436.1 .
RefSeqi WP_012528844.1. NC_011146.1.
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: November 26, 2014
This is version 50 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