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A4FPY4

- HEM1_SACEN

UniProt

A4FPY4 - HEM1_SACEN

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Protein

Glutamyl-tRNA reductase

Gene
hemA, SACE_6946
Organism
Saccharopolyspora erythraea (strain NRRL 23338)
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 bindingi189 – 1946NADP 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

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:SACE_6946
OrganismiSaccharopolyspora erythraea (strain NRRL 23338)
Taxonomic identifieri405948 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeSaccharopolyspora
ProteomesiUP000006728: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 468468Glutamyl-tRNA reductaseUniRule annotationPRO_1000004682Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi405948.SACE_6946.

Structurei

3D structure databases

ProteinModelPortaliA4FPY4.

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.
OMAiLAHKLTN.
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.

A4FPY4-1 [UniParc]FASTAAdd to Basket

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MNLLTVGLSH HSAPVRVLER VAIGADELGK VLHELLQRDH ICEAFVVSTC    50
NRVEVYAVAE TFHGGLEDVT SVLARHSGSD VAELTDHMYV FYAGAAVEHL 100
FSVAAGLDSM VVGEAQILGQ IRQSYGVADE AGTVGRTLHE LAQQALRVGK 150
RVHAETGIDS EGASVVSEAL ADAETELGGL AGRRALLVGA GSMGGLAAAQ 200
LRRAGIGEVV IANRTAVNGE RLAESLRTDG VPASAVALDG LRSAISWADL 250
VVTCTGAVGA VVTTEHVETG DRGPLVFCDL GLPRDTAPEV AELPGVTVVD 300
LATLQRRLSE QQGGNESERA AAIVAEEVRG YLAAQRSAEV TPTVTALRKR 350
AAEVVDAELL RLDSKLPALE GDVRDELART VRRVVDKLLH APTVRVKQLA 400
STPGGSGYAD ALRELFELDP QTAAVLGTAQ ADDGRARGSA SVAEARRAGA 450
PGARDELRDL PAQDGDDR 468
Length:468
Mass (Da):48,954
Last modified:April 17, 2007 - v1
Checksum:i60560B145F6A7FFA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM420293 Genomic DNA. Translation: CAM06109.1.
RefSeqiWP_009943986.1. NZ_ABFV01000011.1.
YP_001109034.1. NC_009142.1.

Genome annotation databases

EnsemblBacteriaiCAM06109; CAM06109; SACE_6946.
GeneIDi4946678.
KEGGisen:SACE_6946.
PATRICi23421356. VBISacEry28377_6956.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM420293 Genomic DNA. Translation: CAM06109.1 .
RefSeqi WP_009943986.1. NZ_ABFV01000011.1.
YP_001109034.1. NC_009142.1.

3D structure databases

ProteinModelPortali A4FPY4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 405948.SACE_6946.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAM06109 ; CAM06109 ; SACE_6946 .
GeneIDi 4946678.
KEGGi sen:SACE_6946.
PATRICi 23421356. VBISacEry28377_6956.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .

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 of the erythromycin-producing bacterium Saccharopolyspora erythraea NRRL23338."
    Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S., Haydock S.F., Leadlay P.F.
    Nat. Biotechnol. 25:447-453(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NRRL 23338.

Entry informationi

Entry nameiHEM1_SACEN
AccessioniPrimary (citable) accession number: A4FPY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 17, 2007
Last modified: September 3, 2014
This is version 61 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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