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B1VEJ5

- HEM1_CORU7

UniProt

B1VEJ5 - HEM1_CORU7

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Protein
Glutamyl-tRNA reductase
Gene
hemA, cu0224
Organism
Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109)
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 sitei59 – 591Nucleophile By similarity
Sitei108 – 1081Important for activity By similarity
Binding sitei118 – 1181Substrate By similarity
Binding sitei129 – 1291Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi205 – 2106NADP 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

BioCyciCURE504474:GJ8Y-230-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:cu0224
OrganismiCorynebacterium urealyticum (strain ATCC 43042 / DSM 7109)
Taxonomic identifieri504474 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
ProteomesiUP000001727: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 494494Glutamyl-tRNA reductaseUniRule annotation
PRO_1000093129Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi504474.cur_0224.

Structurei

3D structure databases

ProteinModelPortaliB1VEJ5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 614Substrate binding By similarity
Regioni123 – 1253Substrate 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.
KOiK02492.
OMAiLNKQFET.
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.

B1VEJ5-1 [UniParc]FASTAAdd to Basket

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MAGHVHTGSA AVLLVGLSFR SAPVSLLEQV STVDTDLPKL ENALLDHDSL    50
SEALVLSTCN RMEFYTVANA FHPGLDHIVD TIATYSGLDD SELEPHLYVH 100
YSDAAVEHML NVASGLDSMV LGEQQIIGQL RGAYEESKGA GTVGRTLHDL 150
TQRALRTGKR VHSETEIDSA GSSMVSFALD RALTVLGIPE ASSDALSGRR 200
AVVIGAGAMA SLASTHLGRL GIEHVTVANR TVDRAEQLAS HAVEAGVPAR 250
GIGLDELPAA LTGADIVVSA TGAVGTVVSA ADIKAAQQVR DGRQQVLIDL 300
SMPRDIEQAT ADVPGVALLN IEELTGMTED TIEDEDAARG IVAEELESFL 350
EQQRAQAVVP TVKALRQQAM DALSNEMLAL QRQTPGMSDE DREAVNRSMR 400
RLVEKLLHTP TVQAKKLSAA GQSVSYPDAL AALFNLPTGM TQQVSAVKGA 450
NAGSGQRKKQ KPQENRVSTA RAVYRSTYQD LTQASTPGGK DDDQ 494
Length:494
Mass (Da):52,334
Last modified:May 20, 2008 - v1
Checksum:iBB6FE258AC21C0C9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM942444 Genomic DNA. Translation: CAQ04184.1.
RefSeqiWP_012359490.1. NC_010545.1.
YP_001799618.1. NC_010545.1.

Genome annotation databases

EnsemblBacteriaiCAQ04184; CAQ04184; cu0224.
GeneIDi6186320.
KEGGicur:cur_0224.
PATRICi21520146. VBICorUre58120_0220.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM942444 Genomic DNA. Translation: CAQ04184.1 .
RefSeqi WP_012359490.1. NC_010545.1.
YP_001799618.1. NC_010545.1.

3D structure databases

ProteinModelPortali B1VEJ5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 504474.cur_0224.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAQ04184 ; CAQ04184 ; cu0224 .
GeneIDi 6186320.
KEGGi cur:cur_0224.
PATRICi 21520146. VBICorUre58120_0220.

Phylogenomic databases

eggNOGi COG0373.
KOi K02492.
OMAi LNKQFET.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CURE504474:GJ8Y-230-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. "The lifestyle of Corynebacterium urealyticum derived from its complete genome sequence established by pyrosequencing."
    Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A., Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J., Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M., Puehler A.
    J. Biotechnol. 136:11-21(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43042 / DSM 7109.

Entry informationi

Entry nameiHEM1_CORU7
AccessioniPrimary (citable) accession number: B1VEJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: September 3, 2014
This is version 52 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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