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A0PW28

- HEM1_MYCUA

UniProt

A0PW28 - HEM1_MYCUA

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Protein

Glutamyl-tRNA reductase

Gene
hemA, MUL_4598
Organism
Mycobacterium ulcerans (strain Agy99)
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 sitei50 – 501Nucleophile By similarity
Sitei99 – 991Important for activity By similarity
Binding sitei109 – 1091Substrate By similarity
Binding sitei120 – 1201Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 1946NADP By similarity

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 reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
Ordered Locus Names:MUL_4598
OrganismiMycobacterium ulcerans (strain Agy99)
Taxonomic identifieri362242 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000000765: Chromosome

Organism-specific databases

GenoListiMUL_4598.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Glutamyl-tRNA reductaseUniRule annotationPRO_0000335052Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi362242.MUL_4598.

Structurei

3D structure databases

ProteinModelPortaliA0PW28.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni114 – 1163Substrate 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.
HOGENOMiHOG000109649.
KOiK02492.
OMAiHEVTGEY.
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.

A0PW28-1 [UniParc]FASTAAdd to Basket

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MSILLFGVSH RSAPVSVLEQ LSIDESEQVK IVDRVLQSPL VTEAMVLSTC    50
NRVEVYAVVE AFHGGLSAIG QVLSDHSGMS MGELTKHAYV RYSEAAVEHL 100
FAVASGLDSA VVGEQQVLGQ VRRSYSAAEA NRTVGRVLHE LAQRTLSVGK 150
RVHSETSIDA AGASVVSVAL GIAERKLGGL GAKTAVVIGA GSMGALSSAH 200
LTRAGIGKVH VLNRSLARAQ RLAGKIRQSG VLAEARTLDR LAEVLTDADA 250
VVSCTGAVAP VVSLADVHHA LATARRDETT RPLVICDLGM PRDVDPAVAG 300
LPGVWLIDVE RVQREPSAHA ASADVAAARH IVAAEVAGYL AGQRMAEVTP 350
TVTALRQRAA DVVEAELLRL DNRLPGLDSA ERDEVARTVR RVVDKLLHAP 400
TVRIKQLASA PGGDSYAEAL RELFQLDQTA VDAVATAGEL PVFSSGLDAG 450
SGPQGADGPS AGPTPSAPNP SAE 473
Length:473
Mass (Da):49,215
Last modified:January 9, 2007 - v1
Checksum:i6F97EC513C9563A7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000325 Genomic DNA. Translation: ABL06547.1.
RefSeqiWP_011742144.1. NC_008611.1.
YP_908018.1. NC_008611.1.

Genome annotation databases

EnsemblBacteriaiABL06547; ABL06547; MUL_4598.
GeneIDi4554532.
KEGGimul:MUL_4598.
PATRICi18177043. VBIMycUlc37413_5322.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000325 Genomic DNA. Translation: ABL06547.1 .
RefSeqi WP_011742144.1. NC_008611.1.
YP_908018.1. NC_008611.1.

3D structure databases

ProteinModelPortali A0PW28.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 362242.MUL_4598.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABL06547 ; ABL06547 ; MUL_4598 .
GeneIDi 4554532.
KEGGi mul:MUL_4598.
PATRICi 18177043. VBIMycUlc37413_5322.

Organism-specific databases

GenoListi MUL_4598.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109649.
KOi K02492.
OMAi HEVTGEY.
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

  1. "Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer."
    Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.
    , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.
    Genome Res. 17:192-200(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Agy99.

Entry informationi

Entry nameiHEM1_MYCUA
AccessioniPrimary (citable) accession number: A0PW28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: January 9, 2007
Last modified: September 3, 2014
This is version 69 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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