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A6Q3S5

- HEM1_NITSB

UniProt

A6Q3S5 - HEM1_NITSB

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Nitratiruptor sp. (strain SB155-2)
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 sitei51 – 511NucleophileUniRule annotation
Sitei100 – 1001Important for activityUniRule annotation
Binding sitei110 – 1101SubstrateUniRule annotation
Binding sitei121 – 1211SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi190 – 1956NADPUniRule 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

BioCyciNSP387092:GHA5-1063-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:NIS_1024
OrganismiNitratiruptor sp. (strain SB155-2)
Taxonomic identifieri387092 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaNitratiruptor
ProteomesiUP000001118: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Glutamyl-tRNA reductasePRO_1000057577Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi387092.NIS_1024.

Structurei

3D structure databases

ProteinModelPortaliA6Q3S5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 534Substrate bindingUniRule annotation
Regioni115 – 1173Substrate 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.
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.

A6Q3S5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQYLVVSFSH KNTDIVTREK LALSDDNKRE DVATTLLQNP VINEAIILST
60 70 80 90 100
CNRIEIILSV KDPFSATEAV LKKLSEVSGI NYEELEGRAD IYEDNGAIHH
110 120 130 140 150
VFSVASGLDS LVVGETQITG QIKDAYKEAY EKGWCGQKLG RVMHYAFKCS
160 170 180 190 200
KEVRSSTDIT RSPVSVASAA VSMAKEKLGN LGGMSALVVG AGEMGRLAAK
210 220 230 240 250
HLISHGCNVI LVGRDLEKTK TVAQEIDPDI RVEHVSNLQK LINSYRLLFS
260 270 280 290 300
ATSSKNPVIT KDMVKEQSFD RYWFDMAVPR DIEEIYVARI HYFAVDDLKE
310 320 330 340 350
IVNKNMAFRE EQARNAYKIV GHHVNEFFKW LQTLEIDPII KEIRKRAKDS
360 370 380 390 400
ALAELQKAIK KGYIPKEYEK SIEKLLHNAF NRFLHDPTKQ LKAIADEPRA
410 420 430
DTIVEAIKFF FEIEEEVGLN RYKCEYYMNL RS
Length:432
Mass (Da):49,015
Last modified:August 21, 2007 - v1
Checksum:iE0F4DCE8BFEA4EE5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009178 Genomic DNA. Translation: BAF70134.1.
RefSeqiWP_012082397.1. NC_009662.1.
YP_001356491.1. NC_009662.1.

Genome annotation databases

EnsemblBacteriaiBAF70134; BAF70134; NIS_1024.
GeneIDi5361241.
KEGGinis:NIS_1024.
PATRICi22684128. VBINitSp82229_1068.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009178 Genomic DNA. Translation: BAF70134.1 .
RefSeqi WP_012082397.1. NC_009662.1.
YP_001356491.1. NC_009662.1.

3D structure databases

ProteinModelPortali A6Q3S5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 387092.NIS_1024.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAF70134 ; BAF70134 ; NIS_1024 .
GeneIDi 5361241.
KEGGi nis:NIS_1024.
PATRICi 22684128. VBINitSp82229_1068.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci NSP387092:GHA5-1063-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. "Deep-sea vent epsilon-proteobacterial genomes provide insights into emergence of pathogens."
    Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K., Horikoshi K.
    Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SB155-2.

Entry informationi

Entry nameiHEM1_NITSB
AccessioniPrimary (citable) accession number: A6Q3S5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: August 21, 2007
Last modified: October 1, 2014
This is version 55 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