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C3PKG1

- HEM1_CORA7

UniProt

C3PKG1 - HEM1_CORA7

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Protein

Glutamyl-tRNA reductase

Gene
hemA, cauri_0298
Organism
Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CN-1) (Corynebacterium nigricans)
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. 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

BioCyciCAUR548476:GH9E-309-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:cauri_0298
OrganismiCorynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CN-1) (Corynebacterium nigricans)
Taxonomic identifieri548476 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
ProteomesiUP000002077: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 458458Glutamyl-tRNA reductaseUniRule annotationPRO_1000190514Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi169292.cauri_0298.

Structurei

3D structure databases

ProteinModelPortaliC3PKG1.

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.

C3PKG1-1 [UniParc]FASTAAdd to Basket

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MSVLVVGMSH QSAPVALLEK LSMDETVQND TCRAMVSAGS LSEAMIISTC    50
NRLEVYTVTN SFHSGVQDVV HNLAEVSGVE EEKLRSYLYV RYADAAAEHL 100
MMVTSGLDSM VVGEQQIIGQ VRTAYQFASE QGTVGPRIHA LAQSALRTGK 150
RVHSETEIDE AGSSMVSFAF DQALSRMGRE DLAGKRVLIL GAGAMASLAA 200
THAGRLGAHL IIANRTIARA ERVAQHAHEA GVYADVIDFS ERAQALRDVD 250
VAISATGAQG FTITAADVER YHVADRELML VDLSLPRDID DAVAEAEGVD 300
LINIERLNNS LQAADTDLAA GTSPHAQARR IVSEELESYA SEQRVRDVVP 350
AVSALRKRAA NLVQCEVARM EQKHPELDER QMGDINRALK RVADKLLHEP 400
TVRAKQLAAN SGTVSHETAL QELFGLQLEG SGVAVDMAEL PDAAQMEAAE 450
NTKEEKDA 458
Length:458
Mass (Da):49,388
Last modified:June 16, 2009 - v1
Checksum:i925C261543213257
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001601 Genomic DNA. Translation: ACP31897.1.
RefSeqiWP_010189811.1. NZ_ACLH01000069.1.
YP_002833835.1. NC_012590.1.

Genome annotation databases

EnsemblBacteriaiACP31897; ACP31897; cauri_0298.
GeneIDi7801153.
KEGGicar:cauri_0298.
PATRICi21476536. VBICorAur68407_0319.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001601 Genomic DNA. Translation: ACP31897.1 .
RefSeqi WP_010189811.1. NZ_ACLH01000069.1.
YP_002833835.1. NC_012590.1.

3D structure databases

ProteinModelPortali C3PKG1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 169292.cauri_0298.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACP31897 ; ACP31897 ; cauri_0298 .
GeneIDi 7801153.
KEGGi car:cauri_0298.
PATRICi 21476536. VBICorAur68407_0319.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CAUR548476:GH9E-309-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. "Complete genome sequence and lifestyle of black-pigmented Corynebacterium aurimucosum ATCC 700975 (formerly C. nigricans CN-1) isolated from a vaginal swab of a woman with spontaneous abortion."
    Trost E., Gotker S., Schneider J., Schneiker-Bekel S., Szczepanowski R., Tilker A., Viehoever P., Arnold W., Bekel T., Blom J., Gartemann K.H., Linke B., Goesmann A., Puhler A., Shukla S.K., Tauch A.
    BMC Genomics 11:91-91(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700975 / DSM 44827 / CN-1.

Entry informationi

Entry nameiHEM1_CORA7
AccessioniPrimary (citable) accession number: C3PKG1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 16, 2009
Last modified: September 3, 2014
This is version 40 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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