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Q6NJK1

- HEM1_CORDI

UniProt

Q6NJK1 - HEM1_CORDI

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Protein
Glutamyl-tRNA reductase
Gene
hemA, DIP0400
Organism
Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)
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 bindingi191 – 1966NADP By similarity

GO - Molecular functioni

  1. NADP binding Source: InterPro
  2. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP

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:DIP0400
OrganismiCorynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)
Taxonomic identifieri257309 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
ProteomesiUP000002198: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 438438Glutamyl-tRNA reductaseUniRule annotation
PRO_0000114015Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi257309.DIP0400.

Structurei

3D structure databases

ProteinModelPortaliQ6NJK1.

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.
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.

Q6NJK1-1 [UniParc]FASTAAdd to Basket

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MSVLVVGMSH RSAPVALLEK LSMDDGVRTN TVSDLVARPS LAEAMIVSTC    50
NRLEVYAMTS SFHTGVNDVV EVLHDMSGVD MEELRGYLYV RYADAAAEHM 100
MEVTSGLDSM VVGEQQIIGQ VRTAYHSATE AGTVGPALHG LVQASLHTGK 150
RVHTETDIDD AGASMVSFAC DEALAQMSAT NFAGCRALVL GAGAMASLAA 200
THLGRLGIEH ITVANRTFER AQRLADHAVE AGVAASAIEF ERRMDVLCDV 250
DVVVSATGAN TFTIEAANIP AAHGDLMMID LSLPRDISDD VAEVPGVHLV 300
NIEKLRDVAS SGEAKDHAAQ RIVAEELEAY TSAQRIRDVA PAVAALRRHA 350
SSLIDSELAR LSTRVPSMDE DDFSEVQRTV RRVVDKLLHQ PTVRVKELAA 400
QSGTVSYDTA IQELFGLAVE ATPVAVNVDE LPERINKR 438
Length:438
Mass (Da):46,918
Last modified:July 5, 2004 - v1
Checksum:i2BF1FD0E18AAF184
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX248355 Genomic DNA. Translation: CAE48904.1.
RefSeqiNP_938781.1. NC_002935.2.
WP_010934271.1. NC_002935.2.

Genome annotation databases

EnsemblBacteriaiCAE48904; CAE48904; DIP0400.
GeneIDi2650204.
KEGGicdi:DIP0400.
PATRICi21481957. VBICorDip47633_0383.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX248355 Genomic DNA. Translation: CAE48904.1 .
RefSeqi NP_938781.1. NC_002935.2.
WP_010934271.1. NC_002935.2.

3D structure databases

ProteinModelPortali Q6NJK1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 257309.DIP0400.

Protocols and materials databases

DNASUi 2650204.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAE48904 ; CAE48904 ; DIP0400 .
GeneIDi 2650204.
KEGGi cdi:DIP0400.
PATRICi 21481957. VBICorDip47633_0383.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109649.
KOi K02492.
OMAi PYLYVHY.
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700971 / NCTC 13129 / Biotype gravis.

Entry informationi

Entry nameiHEM1_CORDI
AccessioniPrimary (citable) accession number: Q6NJK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 5, 2004
Last modified: September 3, 2014
This is version 80 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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