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C1AKI9

- HEM1_MYCBT

UniProt

C1AKI9 - HEM1_MYCBT

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019)
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

BioCyciMBOV561275:GHDN-526-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:JTY_0522
OrganismiMycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019)
Taxonomic identifieri561275 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000002205: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 468468Glutamyl-tRNA reductasePRO_1000190535Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi561275.JTY_0522.

Structurei

3D structure databases

ProteinModelPortaliC1AKI9.
SMRiC1AKI9. Positions 2-400.
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.
OMAiPYLYVHY.
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.

C1AKI9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSVLLFGVSH RSAPVVVLEQ LSIDESDQVK IIDRVLASPL VTEAMVLSTC
60 70 80 90 100
NRVEVYAVVD AFHGGLSVIG QVLAEHSGMS MGELTKYAYV RYSEAAVEHL
110 120 130 140 150
FAVASGLDSA VIGEQQVLGQ VRRAYAVAES NRTVGRVLHE LAQRALSVGK
160 170 180 190 200
RVHSETAIDA AGASVVSVAL GMAERKLGSL AGTTAVVIGA GAMGALSAVH
210 220 230 240 250
LTRAGVGHIQ VLNRSLSRAQ RLARRIRESG VPAEALALDR LANVLADADV
260 270 280 290 300
VVSCTGAVRP VVSLADVHHA LAAARRDEAT RPLVICDLGM PRDVDPAVAR
310 320 330 340 350
LPCVWVVDVD SVQHEPSAHA AAADVEAARH IVAAEVASYL VGQRMAEVTP
360 370 380 390 400
TVTALRQRAA EVVEAELLRL DNRLPGLQSV QREEVARTVR RVVDKLLHAP
410 420 430 440 450
TVRIKQLASA PGGDSYAEAL RELFELDQTA VDAVATAGEL PVVPSGFDAE
460
SRRGGGDMQS SPKRSPSN
Length:468
Mass (Da):49,361
Last modified:May 26, 2009 - v1
Checksum:iDDC257648FF6EAAB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP010918 Genomic DNA. Translation: BAH24818.1.
RefSeqiYP_002643586.1. NC_012207.1.

Genome annotation databases

EnsemblBacteriaiBAH24818; BAH24818; JTY_0522.
GeneIDi7561190.
KEGGimbt:JTY_0522.
PATRICi18020338. VBIMycBov85238_0567.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP010918 Genomic DNA. Translation: BAH24818.1 .
RefSeqi YP_002643586.1. NC_012207.1.

3D structure databases

ProteinModelPortali C1AKI9.
SMRi C1AKI9. Positions 2-400.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 561275.JTY_0522.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAH24818 ; BAH24818 ; JTY_0522 .
GeneIDi 7561190.
KEGGi mbt:JTY_0522.
PATRICi 18020338. VBIMycBov85238_0567.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci MBOV561275:GHDN-526-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. "Whole genome sequence analysis of Mycobacterium bovis bacillus Calmette-Guerin (BCG) Tokyo 172: a comparative study of BCG vaccine substrains."
    Seki M., Honda I., Fujita I., Yano I., Yamamoto S., Koyama A.
    Vaccine 27:1710-1716(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BCG / Tokyo 172 / ATCC 35737 / TMC 1019.

Entry informationi

Entry nameiHEM1_MYCBT
AccessioniPrimary (citable) accession number: C1AKI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 26, 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3