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A4QB58

- HEM1_CORGB

UniProt

A4QB58 - HEM1_CORGB

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Protein
Glutamyl-tRNA reductase
Gene
hemA, cgR_0488
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) 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 bindingi196 – 2016NADP 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

BioCyciCGLU340322:GJBE-511-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: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 reductaseUniRule annotation
PRO_0000291541Add
BLAST

Proteomic databases

PRIDEiA4QB58.

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi340322.cgR_0488.

Structurei

3D structure databases

ProteinModelPortaliA4QB58.

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.
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

MSVLIVGMSH RSAPVSLLER LSMDDSVRGE TTQALLGRAS LSEALIVSTC    50
NRLEVYTVTS SFHTGVNDVV EVLHEASGVD IETLRGYLYV RYADAAAEHM 100
LVVTSGLDSM VLGEQQIIGQ VRTAYQAANE YGSVGPALHS LTQTALHTGK 150
RVHSETAIDD AGASMVSFAV DRALVQMGLD SEAEAPLSGK TALVLGAGAM 200
SSLAATHLGR AGISKLIMAN RTLERAERLA EHSLEAGVPA EVVEYDQRAS 250
AYNRVDLVVS ATGADDFTVK PEDIPEGASL MLVDLSMPRD IDDACADLPG 300
VDLVNIERLH KASREGGSGM APSEEEALAI VREELDSFTS EQRIRDIVPA 350
VSALRRQAAS VGSDELDRLR QRAPGISEVE WGEVEKTVRR VVDKLLHQPT 400
VRVKELAARS GSISYDSALQ ELFGLESLAS TAAPATTSVN ASELPDAGIV 450
AFVNAPSATQ TRE 463
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.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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...

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: September 3, 2014
This is version 56 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 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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