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B9L0Q1

- HEM1_THERP

UniProt

B9L0Q1 - HEM1_THERP

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-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 sitei50 – 501NucleophileUniRule annotation
Sitei97 – 971Important for activityUniRule annotation
Binding sitei107 – 1071SubstrateUniRule annotation
Binding sitei118 – 1181SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi187 – 1926NADPUniRule 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

BioCyciTROS309801:GI0S-1110-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:trd_1122
OrganismiThermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2)
Taxonomic identifieri309801 [NCBI]
Taxonomic lineageiBacteriaChloroflexiThermomicrobialesThermomicrobiaceaeThermomicrobium
ProteomesiUP000000447: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 406406Glutamyl-tRNA reductasePRO_1000190542Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi309801.trd_1122.

Structurei

3D structure databases

ProteinModelPortaliB9L0Q1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni112 – 1143Substrate 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.
OMAiNISRGPR.
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]
SUPFAMiSSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B9L0Q1-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MTMTLSVVAV THRTAPVTIR ERLSLPVEQQ CQWLQRWGNQ VPEIVLLVTC
60 70 80 90 100
HRTEVYWLDG EETAHRGVEW LAELGGLTVE ELERWVLQRS GAEAVRHAFC
110 120 130 140 150
VAAGLDSRVV GEPQILGQVR RARDLARAAG TLGPILDRLF SCSLATGRMV
160 170 180 190 200
RVRAGWSTGK RSLARVAVRE AARLCSDLQS ARVLVLGAGE TGRDVIAALC
210 220 230 240 250
RCQPAVVWWT NRSPGRLAQI PSEEPVRIVD WSEWPRLVTE ADVVFVATNA
260 270 280 290 300
PEPIVRLEHV TRHARLPRLL VDLAVPRNVD PAISDVPGIR VVTIDDLPAD
310 320 330 340 350
PVPVAAWDGV AVEPYVERAV QRYLRWLEAR SIAAEIRAAH ETLQSMLERE
360 370 380 390 400
LEKVLRLALR DPARTGEVKR VAAASMARKT LFPLFRALES EPQRVALALR

LLAYDR
Length:406
Mass (Da):45,246
Last modified:March 24, 2009 - v1
Checksum:iF6684624F5083664
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001275 Genomic DNA. Translation: ACM05350.1.
RefSeqiYP_002522331.1. NC_011959.1.

Genome annotation databases

EnsemblBacteriaiACM05350; ACM05350; trd_1122.
GeneIDi7355377.
KEGGitro:trd_1122.
PATRICi23913416. VBITheRos91376_1058.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001275 Genomic DNA. Translation: ACM05350.1 .
RefSeqi YP_002522331.1. NC_011959.1.

3D structure databases

ProteinModelPortali B9L0Q1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 309801.trd_1122.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACM05350 ; ACM05350 ; trd_1122 .
GeneIDi 7355377.
KEGGi tro:trd_1122.
PATRICi 23913416. VBITheRos91376_1058.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci TROS309801:GI0S-1110-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 ]
SUPFAMi SSF69742. SSF69742. 1 hit.
TIGRFAMsi TIGR01035. hemA. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete genome sequence of the aerobic CO-oxidizing thermophile Thermomicrobium roseum."
    Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A., Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L., Eisen J.A.
    PLoS ONE 4:E4207-E4207(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27502 / DSM 5159 / P-2.

Entry informationi

Entry nameiHEM1_THERP
AccessioniPrimary (citable) accession number: B9L0Q1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: October 29, 2014
This is version 49 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