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Q3ING1

- HEM1_NATPD

UniProt

Q3ING1 - HEM1_NATPD

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Protein
Glutamyl-tRNA reductase
Gene
hemA, NP_4502A
Organism
Natronomonas pharaonis (strain ATCC 35678 / DSM 2160) (Halobacterium pharaonis)
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 sitei53 – 531Nucleophile By similarity
Sitei95 – 951Important for activity By similarity
Binding sitei105 – 1051Substrate By similarity
Binding sitei116 – 1161Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi184 – 1896NADP 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

BioCyciNPHA348780:GJX0-2285-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:NP_4502A
OrganismiNatronomonas pharaonis (strain ATCC 35678 / DSM 2160) (Halobacterium pharaonis)
Taxonomic identifieri348780 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeNatronomonas
ProteomesiUP000002698: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 453453Glutamyl-tRNA reductaseUniRule annotation
PRO_1000004654Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi348780.NP4502A.

Structurei

3D structure databases

ProteinModelPortaliQ3ING1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni52 – 554Substrate binding By similarity
Regioni110 – 1123Substrate 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.

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.

Q3ING1-1 [UniParc]FASTAAdd to Basket

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MTVETGIVVG ASVSHSHASI DQIETAADGS QQTAVEELLS KEGVSEAFVL    50
QTCNRAEAYV VANDSETGTA ALAGYLAGVD DDAIRMLSHN QSLKHLMAVA 100
CGLESLVIGE DQILGQVRDA YEDARGVGGV GPTLNDAVLK ALHVGERART 150
ETAINEGAVS LGSAAVRFAA ERHGVTGSTA LVVGAGEMAT LAAKALDDPA 200
SRVIVANRTR ERAERLAEEL STTASVVGVD SVDEAADAAD VVVSATGSED 250
YVIDTADLGG VGETCVLDIA QPRDVAPGAD GIDGVAVYDL DTIESVTDEA 300
RAKRREAAET VETMIDEEFE HLMTQYKRKR ADQVIAAMYE GAERIKAREL 350
RTAVSKFEAE REDGLSEREH EIVESMADAL VGQLLSAPTQ SLRDAAEEDD 400
WATINAALQL FGPGLEPEPT ELPTVPDGPE GVPEELRERM SSGMLEQFST 450
NDD 453
Length:453
Mass (Da):47,809
Last modified:November 8, 2005 - v1
Checksum:i839ADF48145910A7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR936257 Genomic DNA. Translation: CAI50342.1.
RefSeqiWP_011323957.1. NC_007426.1.
YP_330979.1. NC_007426.1.

Genome annotation databases

EnsemblBacteriaiCAI50342; CAI50342; NP_4502A.
GeneIDi3702804.
KEGGinph:NP4502A.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR936257 Genomic DNA. Translation: CAI50342.1 .
RefSeqi WP_011323957.1. NC_007426.1.
YP_330979.1. NC_007426.1.

3D structure databases

ProteinModelPortali Q3ING1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 348780.NP4502A.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAI50342 ; CAI50342 ; NP_4502A .
GeneIDi 3702804.
KEGGi nph:NP4502A.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci NPHA348780:GJX0-2285-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. "Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis."
    Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J., Oesterhelt D.
    Genome Res. 15:1336-1343(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35678 / DSM 2160.

Entry informationi

Entry nameiHEM1_NATPD
AccessioniPrimary (citable) accession number: Q3ING1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 8, 2005
Last modified: September 3, 2014
This is version 76 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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