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A6LKW9

- HEM1_THEM4

UniProt

A6LKW9 - HEM1_THEM4

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Tmel_0706
Organism
Thermosipho melanesiensis (strain BI429 / DSM 12029)
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 sitei44 – 441Nucleophile By similarity
Sitei79 – 791Important for activity By similarity
Binding sitei89 – 891Substrate By similarity
Binding sitei100 – 1001Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi164 – 1696NADP By similarity

GO - Molecular functioni

  1. NADP binding Source: InterPro
  2. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
Complete GO annotation...

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

BioCyciTMEL391009:GHM1-752-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:Tmel_0706
OrganismiThermosipho melanesiensis (strain BI429 / DSM 12029)
Taxonomic identifieri391009 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermosipho
ProteomesiUP000001110: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 368368Glutamyl-tRNA reductaseUniRule annotation
PRO_1000004716Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi391009.Tmel_0706.

Structurei

3D structure databases

ProteinModelPortaliA6LKW9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni43 – 464Substrate binding By similarity
Regioni94 – 963Substrate 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.
OMAiKMLHGTM.
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.

A6LKW9-1 [UniParc]FASTAAdd to Basket

« Hide

MKLNLVGLGR NTPIYILEKF DFDEQEFFSS LKVKTTEVAV LKTCHRREIY    50
YIGDKEPLTI NEIIEPYIIR KSGIDVVRHL FKVSCGLDSM VLGEHQILSQ 100
VKNTHKNFCH GKILNKLFNE AVSLGKEART KTGINKYPLS ISYIAVKLIE 150
EQINIEGKKI FVIGTGMMGQ KVIKYLVSRG ADIYISNRTI KKAYEIKKMF 200
SEVNIVDFEE KYKHISSSDV VISATNAPHY VVEEKKVNSQ KNIIFIDLSM 250
PRNIEPSIKE YHTLYTLEDL NEISKKYNKL RQEKISTIQN LIETRIKKFL 300
TWYKLQTVKD DILYIQNLAE KLVYEEIEKL SKKILLDDNS LKQIQKSLKS 350
CTKKIVSYHI NYIKEKVI 368
Length:368
Mass (Da):42,784
Last modified:July 24, 2007 - v1
Checksum:i6074AC5A541663BC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000716 Genomic DNA. Translation: ABR30570.1.
RefSeqiYP_001305955.1. NC_009616.1.

Genome annotation databases

EnsemblBacteriaiABR30570; ABR30570; Tmel_0706.
GeneIDi5297066.
KEGGitme:Tmel_0706.
PATRICi23922617. VBITheMel19269_0736.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000716 Genomic DNA. Translation: ABR30570.1 .
RefSeqi YP_001305955.1. NC_009616.1.

3D structure databases

ProteinModelPortali A6LKW9.
ModBasei Search...

Protein-protein interaction databases

STRINGi 391009.Tmel_0706.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABR30570 ; ABR30570 ; Tmel_0706 .
GeneIDi 5297066.
KEGGi tme:Tmel_0706.
PATRICi 23922617. VBITheMel19269_0736.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci TMEL391009:GHM1-752-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: BI429 / DSM 12029.

Entry informationi

Entry nameiHEM1_THEM4
AccessioniPrimary (citable) accession number: A6LKW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 24, 2007
Last modified: September 3, 2014
This is version 60 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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