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A4QB58

- HEM1_CORGB

UniProt

A4QB58 - HEM1_CORGB

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Corynebacterium glutamicum (strain R)
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 bindingi196 – 2016NADPUniRule 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

BioCyciCGLU340322:GJBE-511-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:cgR_0488
OrganismiCorynebacterium glutamicum (strain R)
Taxonomic identifieri340322 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
ProteomesiUP000006698: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 463463Glutamyl-tRNA reductasePRO_0000291541Add
BLAST

Proteomic databases

PRIDEiA4QB58.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi340322.cgR_0488.

Structurei

3D structure databases

ProteinModelPortaliA4QB58.
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.
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.

A4QB58-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSVLIVGMSH RSAPVSLLER LSMDDSVRGE TTQALLGRAS LSEALIVSTC
60 70 80 90 100
NRLEVYTVTS SFHTGVNDVV EVLHEASGVD IETLRGYLYV RYADAAAEHM
110 120 130 140 150
LVVTSGLDSM VLGEQQIIGQ VRTAYQAANE YGSVGPALHS LTQTALHTGK
160 170 180 190 200
RVHSETAIDD AGASMVSFAV DRALVQMGLD SEAEAPLSGK TALVLGAGAM
210 220 230 240 250
SSLAATHLGR AGISKLIMAN RTLERAERLA EHSLEAGVPA EVVEYDQRAS
260 270 280 290 300
AYNRVDLVVS ATGADDFTVK PEDIPEGASL MLVDLSMPRD IDDACADLPG
310 320 330 340 350
VDLVNIERLH KASREGGSGM APSEEEALAI VREELDSFTS EQRIRDIVPA
360 370 380 390 400
VSALRRQAAS VGSDELDRLR QRAPGISEVE WGEVEKTVRR VVDKLLHQPT
410 420 430 440 450
VRVKELAARS GSISYDSALQ ELFGLESLAS TAAPATTSVN ASELPDAGIV
460
AFVNAPSATQ TRE
Length:463
Mass (Da):49,229
Last modified:June 26, 2007 - v2
Checksum:i884940DB03E5DE9D
GO

Sequence cautioni

The sequence BAF53455.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF545862 Genomic DNA. Translation: AAN38289.1.
AP009044 Genomic DNA. Translation: BAF53455.1. Different initiation.
RefSeqiYP_001137357.1. NC_009342.1.

Genome annotation databases

EnsemblBacteriaiBAF53455; BAF53455; cgR_0488.
GeneIDi4994524.
KEGGicgt:cgR_0488.
PATRICi21505461. VBICorGlu58097_0510.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF545862 Genomic DNA. Translation: AAN38289.1 .
AP009044 Genomic DNA. Translation: BAF53455.1 . Different initiation.
RefSeqi YP_001137357.1. NC_009342.1.

3D structure databases

ProteinModelPortali A4QB58.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 340322.cgR_0488.

Proteomic databases

PRIDEi A4QB58.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAF53455 ; BAF53455 ; cgR_0488 .
GeneIDi 4994524.
KEGGi cgt:cgR_0488.
PATRICi 21505461. VBICorGlu58097_0510.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CGLU340322:GJBE-511-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

« Hide 'large scale' publications
  1. "Evolutionary considerations on the heme biosynthetic pathway of Corynebacteria and Mycobacteria."
    Vertes A.A., Kos P.B., Inui M., Yukawa H.
    Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Comparative analysis of the Corynebacterium glutamicum group and complete genome sequence of strain R."
    Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M., Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.
    Microbiology 153:1042-1058(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: R.

Entry informationi

Entry nameiHEM1_CORGB
AccessioniPrimary (citable) accession number: A4QB58
Secondary accession number(s): Q8GMZ2, Q8NT91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: October 1, 2014
This is version 57 of the entry and version 2 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