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Q1QED0

- HEM1_PSYCK

UniProt

Q1QED0 - HEM1_PSYCK

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Pcryo_0189
Organism
Psychrobacter cryohalolentis (strain K5)
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 sitei48 – 481Nucleophile By similarity
Sitei135 – 1351Important for activity By similarity
Binding sitei145 – 1451Substrate By similarity
Binding sitei156 – 1561Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi225 – 2306NADP 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

BioCyciPCRY335284:GHE9-196-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:Pcryo_0189
OrganismiPsychrobacter cryohalolentis (strain K5)
Taxonomic identifieri335284 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter
ProteomesiUP000002425: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 464464Glutamyl-tRNA reductaseUniRule annotation
PRO_1000004677Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi335284.Pcryo_0189.

Structurei

3D structure databases

ProteinModelPortaliQ1QED0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 504Substrate binding By similarity
Regioni150 – 1523Substrate 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.
HOGENOMiHOG000109650.
KOiK02492.
OMAiAITCGKK.
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.
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. 2 hits.
TIGRFAMsiTIGR01035. hemA. 1 hit.

Sequencei

Sequence statusi: Complete.

Q1QED0-1 [UniParc]FASTAAdd to Basket

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MRLVVIGVNH KTAPVALRER LALVGDEVSI ALAQLQGFSD GSVIVSTCNR    50
TEIYALVPES ILSPHTLLPN SASAVVETSV IESSMTANNS ANLSSTIISA 100
HILKIKTWLA GFKQLSLDEI DPYLYVHRNT HALTHWLRVA AGLDSMILGE 150
PQILGQIKRA VHMAQDQKAL SNQLGWIVDQ VFAAAKRVRN ETQVGAQAVS 200
LSYAAAKLVT QIFDDLPSRT LLVVAAGEMN RLVATHIAGL GVGRVIICNR 250
NPERAEALAA ELRNPNRRIE VRTLQELPQV LAEADIVSSC SGSMDILIDK 300
TMTLRALKSR RYQPMLMIDL AVPRDIDSTV SRIDDVYLYS VDDLQHVIAG 350
NIEQRRQAAV DAELLVSQLV VEMDRRFQVR QVGKDIQQYR TRTHEQVNKL 400
LQASIAELHG DSANPEDIMI ELTRRLTQNL THAPSKLMRK AAREGDNELL 450
DFVVSGLQDA HRNH 464
Length:464
Mass (Da):51,284
Last modified:May 16, 2006 - v1
Checksum:i6A7D35BF1B8B38A3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000323 Genomic DNA. Translation: ABE73973.1.
RefSeqiWP_011512562.1. NC_007969.1.
YP_579457.1. NC_007969.1.

Genome annotation databases

EnsemblBacteriaiABE73973; ABE73973; Pcryo_0189.
GeneIDi4035669.
KEGGipcr:Pcryo_0189.
PATRICi23059787. VBIPsyCry128170_0241.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000323 Genomic DNA. Translation: ABE73973.1 .
RefSeqi WP_011512562.1. NC_007969.1.
YP_579457.1. NC_007969.1.

3D structure databases

ProteinModelPortali Q1QED0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 335284.Pcryo_0189.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABE73973 ; ABE73973 ; Pcryo_0189 .
GeneIDi 4035669.
KEGGi pcr:Pcryo_0189.
PATRICi 23059787. VBIPsyCry128170_0241.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109650.
KOi K02492.
OMAi AITCGKK.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci PCRY335284:GHE9-196-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.
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. 2 hits.
TIGRFAMsi TIGR01035. hemA. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of chromosome of Psychrobacter cryohalolentis K5."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J.
    , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.
    Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K5.

Entry informationi

Entry nameiHEM1_PSYCK
AccessioniPrimary (citable) accession number: Q1QED0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 16, 2006
Last modified: September 3, 2014
This is version 71 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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