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B1VEJ5

- HEM1_CORU7

UniProt

B1VEJ5 - HEM1_CORU7

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Protein

Glutamyl-tRNA reductase

Gene

hemA

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).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 – 591NucleophileUniRule annotation
Sitei108 – 1081Important for activityUniRule annotation
Binding sitei118 – 1181SubstrateUniRule annotation
Binding sitei129 – 1291SubstrateUniRule annotation

Regions

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

BioCyciCURE504474:GJ8Y-230-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: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 reductasePRO_1000093129Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi504474.cur_0224.

Structurei

3D structure databases

ProteinModelPortaliB1VEJ5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 614Substrate bindingUniRule annotation
Regioni123 – 1253Substrate 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.
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

« Hide

        10         20         30         40         50
MAGHVHTGSA AVLLVGLSFR SAPVSLLEQV STVDTDLPKL ENALLDHDSL
60 70 80 90 100
SEALVLSTCN RMEFYTVANA FHPGLDHIVD TIATYSGLDD SELEPHLYVH
110 120 130 140 150
YSDAAVEHML NVASGLDSMV LGEQQIIGQL RGAYEESKGA GTVGRTLHDL
160 170 180 190 200
TQRALRTGKR VHSETEIDSA GSSMVSFALD RALTVLGIPE ASSDALSGRR
210 220 230 240 250
AVVIGAGAMA SLASTHLGRL GIEHVTVANR TVDRAEQLAS HAVEAGVPAR
260 270 280 290 300
GIGLDELPAA LTGADIVVSA TGAVGTVVSA ADIKAAQQVR DGRQQVLIDL
310 320 330 340 350
SMPRDIEQAT ADVPGVALLN IEELTGMTED TIEDEDAARG IVAEELESFL
360 370 380 390 400
EQQRAQAVVP TVKALRQQAM DALSNEMLAL QRQTPGMSDE DREAVNRSMR
410 420 430 440 450
RLVEKLLHTP TVQAKKLSAA GQSVSYPDAL AALFNLPTGM TQQVSAVKGA
460 470 480 490
NAGSGQRKKQ KPQENRVSTA RAVYRSTYQD LTQASTPGGK DDDQ
Length:494
Mass (Da):52,334
Last modified:May 20, 2008 - v1
Checksum:iBB6FE258AC21C0C9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 55 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.UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3