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A5UU33

- HEM1_ROSS1

UniProt

A5UU33 - HEM1_ROSS1

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Protein
Glutamyl-tRNA reductase
Gene
hemA, RoseRS_1746
Organism
Roseiflexus sp. (strain RS-1)
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
Sitei97 – 971Important for activity By similarity
Binding sitei107 – 1071Substrate By similarity
Binding sitei118 – 1181Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi187 – 1926NADP By similarity

GO - Molecular functioni

  1. NADP binding Source: InterPro
  2. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. chlorophyll biosynthetic process Source: UniProtKB-HAMAP
  2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Chlorophyll biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciRSP357808:GH5Z-1770-MONOMER.
UniPathwayiUPA00251; UER00316.
UPA00668.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
Ordered Locus Names:RoseRS_1746
OrganismiRoseiflexus sp. (strain RS-1)
Taxonomic identifieri357808 [NCBI]
Taxonomic lineageiBacteriaChloroflexiChloroflexiaChloroflexalesRoseiflexineaeRoseiflexaceaeRoseiflexus
ProteomesiUP000006554: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 425425Glutamyl-tRNA reductaseUniRule annotation
PRO_1000004680Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi357808.RoseRS_1746.

Structurei

3D structure databases

ProteinModelPortaliA5UU33.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 504Substrate binding By similarity
Regioni112 – 1143Substrate 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.

A5UU33-1 [UniParc]FASTAAdd to Basket

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MQITLIGVHQ RNTPVTVRER LAFNLYELPD ALLALRRYVD EGIILSTCNR    50
VEVCAVTRNG VAGDEALKTF LVEQRGVDQA LFAPSLYVYH NEAVVRHLYR 100
LAAGLDSMVL GEDQIVGQVK EALAIAHAAG AIGPVLHRVL HGALAAGKRA 150
RTHTGIATGH VSVVSVAIDA MRQYPDLLKR GRALVIGAGH IAELSLKHLL 200
AGGCSAITIV NRTEARADAL AQRYGVAWRP WSDLEDALAA SDIVVSCTSA 250
PGIVLSQQMV ERAAAGRSTP LLLFDLAVPR DIDQGVAEIP GVYLHDVDAL 300
EPICRTNRAL RAAEAERAET IIEGEVAKFM EWWAVQQAVP TIRALRKRAE 350
DIRDAEIRRA LARCPELSPQ QRETVIALST AIINKLLHEP IVALRDPEAS 400
GELLTAVRRL FNIDDTAVYT SANMT 425
Length:425
Mass (Da):46,193
Last modified:July 10, 2007 - v1
Checksum:i54D8BE788641CEF4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000686 Genomic DNA. Translation: ABQ90136.1.
RefSeqiWP_011956483.1. NC_009523.1.
YP_001276086.1. NC_009523.1.

Genome annotation databases

EnsemblBacteriaiABQ90136; ABQ90136; RoseRS_1746.
GeneIDi5208703.
KEGGirrs:RoseRS_1746.
PATRICi23351698. VBIRosSp109359_1907.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000686 Genomic DNA. Translation: ABQ90136.1 .
RefSeqi WP_011956483.1. NC_009523.1.
YP_001276086.1. NC_009523.1.

3D structure databases

ProteinModelPortali A5UU33.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 357808.RoseRS_1746.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABQ90136 ; ABQ90136 ; RoseRS_1746 .
GeneIDi 5208703.
KEGGi rrs:RoseRS_1746.
PATRICi 23351698. VBIRosSp109359_1907.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
UPA00668 .
BioCyci RSP357808:GH5Z-1770-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RS-1.

Entry informationi

Entry nameiHEM1_ROSS1
AccessioniPrimary (citable) accession number: A5UU33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: September 3, 2014
This is version 58 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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