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B2A1G4

- HEM1_NATTJ

UniProt

B2A1G4 - HEM1_NATTJ

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF)
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
Sitei101 – 1011Important for activityUniRule annotation
Binding sitei111 – 1111SubstrateUniRule annotation
Binding sitei122 – 1221SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi191 – 1966NADPUniRule 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

BioCyciNTHE457570:GHRL-1148-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:Nther_1121
OrganismiNatranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF)
Taxonomic identifieri457570 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaNatranaerobialesNatranaerobiaceaeNatranaerobius
ProteomesiUP000001683: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 458458Glutamyl-tRNA reductasePRO_1000093153Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi457570.Nther_1121.

Structurei

3D structure databases

ProteinModelPortaliB2A1G4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni116 – 1183Substrate 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.
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.

Sequencei

Sequence statusi: Complete.

B2A1G4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MILAVIGINH ETASVETREQ LAFSSKQVKE LVQKLIEGQP IKEASVLSTC
60 70 80 90 100
NRTEVHFTVN TGQIEAGKNH IMTYLSDFSD LDPREYVDHL YFITDQEAVS
110 120 130 140 150
HIFKVTAGLN SLVTGETEIL GQVKKAYQLS DEAGGVDSIF HGLYQQALRT
160 170 180 190 200
GKRVHRETGI NDNAASVSYA SVELATKIFG SLQNRRALII GAGKMSELAA
210 220 230 240 250
RHLYSNGVKD VIVINRTIER AKNLADKFGG LYASYDQLSE WLNEIDIVIT
260 270 280 290 300
STGAPHFVIK EEQIKRAMKS RKYSPMFLID IAVPRDVEPS VNNQDNAYLY
310 320 330 340 350
TIDDLEAVVE SNMQERQEEA RNAELIISEE VAEFMVWYKT RDVVPLISAL
360 370 380 390 400
REKAEDVRKM ELEKYHKKLK NLSPKEQEAV DKLTKSIVNK ILKEPVLRIK
410 420 430 440 450
EFAVEDKSEL YMATLAQLFD LEDEVIPKDG EEHSSSKEVE SVTQSSTERG

HHESDFHN
Length:458
Mass (Da):51,692
Last modified:May 20, 2008 - v1
Checksum:iAE53385E112E0088
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001034 Genomic DNA. Translation: ACB84704.1.
RefSeqiWP_012447579.1. NC_010718.1.
YP_001917292.1. NC_010718.1.

Genome annotation databases

EnsemblBacteriaiACB84704; ACB84704; Nther_1121.
GeneIDi6315350.
KEGGinth:Nther_1121.
PATRICi22670894. VBINatThe92436_1156.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001034 Genomic DNA. Translation: ACB84704.1 .
RefSeqi WP_012447579.1. NC_010718.1.
YP_001917292.1. NC_010718.1.

3D structure databases

ProteinModelPortali B2A1G4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 457570.Nther_1121.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACB84704 ; ACB84704 ; Nther_1121 .
GeneIDi 6315350.
KEGGi nth:Nther_1121.
PATRICi 22670894. VBINatThe92436_1156.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci NTHE457570:GHRL-1148-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.
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.
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN-LF."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.
    , Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.
    Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF.

Entry informationi

Entry nameiHEM1_NATTJ
AccessioniPrimary (citable) accession number: B2A1G4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: October 29, 2014
This is version 52 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