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P46724

- HEM1_MYCLE

UniProt

P46724 - HEM1_MYCLE

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Mycobacterium leprae (strain TN)
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
Sitei99 – 991Important for activityUniRule annotation
Binding sitei109 – 1091SubstrateUniRule annotation
Binding sitei120 – 1201SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 1946NADPUniRule 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

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:ML2422
ORF Names:B2168_C3_261
OrganismiMycobacterium leprae (strain TN)
Taxonomic identifieri272631 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000000806: Chromosome

Organism-specific databases

LepromaiML2422.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 467467Glutamyl-tRNA reductasePRO_0000114040Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi272631.ML2422.

Structurei

3D structure databases

ProteinModelPortaliP46724.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni114 – 1163Substrate 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.
HOGENOMiHOG000109649.
KOiK02492.
OMAiLNKQFET.
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.

P46724-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSILLFGVSH RSAPVSVLEQ LSLDRSDQIK IVDRVLQSPL VTEAMVLSTC
60 70 80 90 100
NRVEVYAVVE AFHAGLSVIG QVLSEYSAMS IGDLTKYAYV RYSEAAVEHL
110 120 130 140 150
FTVASGLDSA VVGEQQVLGQ VRRAYAAAEA NRTVGQVLHE VAQRALSVGK
160 170 180 190 200
RVHSETAIDA AGVSVVSVAL GIAGRTLGGL AGRIAVVIGA GAMGALSSSY
210 220 230 240 250
LTQANVGRIH VLNRSLSRAR RLAGKIGESG VPADVWTLNH LDEALADADL
260 270 280 290 300
VVSCTGAVSP VVSLADVHHA LAAMRRDETT RPLVICDLGM PRDVDPAVAK
310 320 330 340 350
LPGVWVVDVE GVQREPSARA SAADVDAARR IVAAEVATYL TRQRMAEVAP
360 370 380 390 400
TVTALRQRAA DVVEAELLRL DHRLPGLESA QREEVARTVR RVVDKLLHAP
410 420 430 440 450
TVRIKQLASA PGGDSYTEAL RELFELDQTA VDAVATAGEL PVMVSGFSDT
460
TRYGTSPAQS SSKYHAE
Length:467
Mass (Da):49,483
Last modified:November 1, 1995 - v1
Checksum:iF93245F6861F96E9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00018 Genomic DNA. Translation: AAA17243.1.
AL583925 Genomic DNA. Translation: CAC31938.1.
PIRiS72907.
RefSeqiNP_302567.1. NC_002677.1.
WP_010908887.1. NC_002677.1.

Genome annotation databases

EnsemblBacteriaiCAC31938; CAC31938; CAC31938.
GeneIDi909785.
KEGGimle:ML2422.
PATRICi18059489. VBIMycLep78757_4659.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00018 Genomic DNA. Translation: AAA17243.1 .
AL583925 Genomic DNA. Translation: CAC31938.1 .
PIRi S72907.
RefSeqi NP_302567.1. NC_002677.1.
WP_010908887.1. NC_002677.1.

3D structure databases

ProteinModelPortali P46724.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272631.ML2422.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAC31938 ; CAC31938 ; CAC31938 .
GeneIDi 909785.
KEGGi mle:ML2422.
PATRICi 18059489. VBIMycLep78757_4659.

Organism-specific databases

Lepromai ML2422.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109649.
KOi K02492.
OMAi LNKQFET.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .

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

« Hide 'large scale' publications
  1. Smith D.R., Robison K.
    Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TN.

Entry informationi

Entry nameiHEM1_MYCLE
AccessioniPrimary (citable) accession number: P46724
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 1, 2014
This is version 109 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