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B5YJZ3

- HEM1_THEYD

UniProt

B5YJZ3 - HEM1_THEYD

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Protein
Glutamyl-tRNA reductase
Gene
hemA, THEYE_A0716
Organism
Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87)
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 sitei51 – 511Nucleophile By similarity
Sitei106 – 1061Important for activity By similarity
Binding sitei116 – 1161Substrate By similarity
Binding sitei127 – 1271Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi196 – 2016NADP 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

BioCyciTYEL289376:GH9L-714-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:THEYE_A0716
OrganismiThermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87)
Taxonomic identifieri289376 [NCBI]
Taxonomic lineageiBacteriaNitrospiraeNitrospiralesNitrospiraceaeThermodesulfovibrio
ProteomesiUP000000718: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 429429Glutamyl-tRNA reductaseUniRule annotation
PRO_1000093176Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi289376.THEYE_A0716.

Structurei

3D structure databases

ProteinModelPortaliB5YJZ3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 534Substrate binding By similarity
Regioni121 – 1233Substrate 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.
HOGENOMiHOG000109651.
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.

B5YJZ3-1 [UniParc]FASTAAdd to Basket

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MSLIVIGLNH KTAPVEIREK IAFNSKEAIK EALKELIQRE GIGEVVIIST    50
CNRVEIYVYT ANVSDLKREN QVEETIKAFL SNFHNIEIGE FENYLYVYKD 100
TEAVEHLFKV ASSLDSMIVG EPQITGQVKE SYEIALSERT TSLILNYLMN 150
RALFTAKRVR NETRIGENPV SVSYAAVGLI KKVFDELSKK SILLVGAGEM 200
AELALRHLIG SGIKNVYLTN RTFQRAEEIA KEFNGVAVPF GNLKEQLVKT 250
DIVICSTGAP HYVITEQMLK EVMPLRKHKP IFFIDISVPR NVDPACNELD 300
NVYLYNIDDL QDVVDSNILE RKKEAEKALS IVQEETEKFF QWLNSLESVP 350
VIVSIRNKAE QVRQEEIEKF KAKYKDLPPE LINSIDYLTQ SIINKIMHSP 400
TVALKNNCEN KEILIFSARR LFGLDSEEE 429
Length:429
Mass (Da):48,820
Last modified:November 25, 2008 - v1
Checksum:iBEF10E3F580CE867
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001147 Genomic DNA. Translation: ACI21817.1.
RefSeqiWP_012546522.1. NC_011296.1.
YP_002248558.1. NC_011296.1.

Genome annotation databases

EnsemblBacteriaiACI21817; ACI21817; THEYE_A0716.
GeneIDi6941976.
KEGGitye:THEYE_A0716.
PATRICi23908453. VBITheYel104483_0708.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001147 Genomic DNA. Translation: ACI21817.1 .
RefSeqi WP_012546522.1. NC_011296.1.
YP_002248558.1. NC_011296.1.

3D structure databases

ProteinModelPortali B5YJZ3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 289376.THEYE_A0716.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACI21817 ; ACI21817 ; THEYE_A0716 .
GeneIDi 6941976.
KEGGi tye:THEYE_A0716.
PATRICi 23908453. VBITheYel104483_0708.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
KOi K02492.
OMAi LNKQFET.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci TYEL289376:GH9L-714-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 complete genome sequence of Thermodesulfovibrio yellowstonii strain ATCC 51303 / DSM 11347 / YP87."
    Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.
    Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51303 / DSM 11347 / YP87.

Entry informationi

Entry nameiHEM1_THEYD
AccessioniPrimary (citable) accession number: B5YJZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 25, 2008
Last modified: September 3, 2014
This is version 47 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, 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

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