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A9FDP5

- HEM1_SORC5

UniProt

A9FDP5 - HEM1_SORC5

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Protein
Glutamyl-tRNA reductase
Gene
hemA, sce1624
Organism
Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So ce56))
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
Sitei115 – 1151Important for activity By similarity
Binding sitei125 – 1251Substrate By similarity
Binding sitei136 – 1361Substrate By similarity

Regions

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

BioCyciSCEL448385:GJ75-1683-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:sce1624
OrganismiSorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So ce56))
Taxonomic identifieri448385 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesSorangiineaePolyangiaceaeSorangium
ProteomesiUP000002139: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 529529Glutamyl-tRNA reductaseUniRule annotation
PRO_0000335074Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi448385.sce1624.

Structurei

3D structure databases

ProteinModelPortaliA9FDP5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 504Substrate binding By similarity
Regioni130 – 1323Substrate 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. 2 hits.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A9FDP5-1 [UniParc]FASTAAdd to Basket

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MIFVGLSHKT APIEVRERLA IGRDRLPEVL ARLTAHPAIG EALVLSTCNR    50
VEIYASPRQQ APAPPRPGSA PPPSDEELSR NNEALRAAVA TLVGLGGDAV 100
RGHLAGRVGS DAVLHLFRVA ASLDSMVVGE PQILGQMKEA IEVARGAKTL 150
GVRLGRAAHR AIKVGKRVRT ETAIGAGQVS VSSVAIDLAR QIFADLAGHT 200
ALLIGAGDMA EAASKLLVRA GARLIVVNRS PDRAAALARE VGGEPRPWAD 250
LERSVIDADI VISSTSSPNY VVTPDLVRRA RKARKGRSLF LIDIAVPRDI 300
DPAVNKLDSV YLYDVDDLSQ IVAESVEGRA AEAARAEAIV ADEAQAFEAW 350
TLERALTPTI VGLRARTRSI LVAEVERSLS GKLRHLGVAE RQALAMMIDA 400
ATNKLLHVPT TRLRAMASDP RVAEHVDSLR ELFDIDGAPP ENAAASALAE 450
GELRGAVDGP PTPRSARGAA PPASGARGGG SPRHADPRPQ AAEDNGVYAR 500
QPGGRPAEAG VMAVANPAAA VSAAGLKGA 529
Length:529
Mass (Da):55,293
Last modified:February 5, 2008 - v1
Checksum:iC115B5E9345DF6EF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM746676 Genomic DNA. Translation: CAN91782.1.
RefSeqiWP_012234259.1. NC_010162.1.
YP_001612262.1. NC_010162.1.

Genome annotation databases

EnsemblBacteriaiCAN91782; CAN91782; sce1624.
GeneIDi5807028.
KEGGiscl:sce1624.
PATRICi23661093. VBISorCel80414_1772.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM746676 Genomic DNA. Translation: CAN91782.1 .
RefSeqi WP_012234259.1. NC_010162.1.
YP_001612262.1. NC_010162.1.

3D structure databases

ProteinModelPortali A9FDP5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 448385.sce1624.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAN91782 ; CAN91782 ; sce1624 .
GeneIDi 5807028.
KEGGi scl:sce1624.
PATRICi 23661093. VBISorCel80414_1772.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci SCEL448385:GJ75-1683-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. 2 hits.
TIGRFAMsi TIGR01035. hemA. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete genome sequence of the myxobacterium Sorangium cellulosum."
    Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O., Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J., Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.
    , Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C., Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T., Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S., Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F., Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G., Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D., Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H., Puehler A., Mueller R.
    Nat. Biotechnol. 25:1281-1289(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: So ce56.

Entry informationi

Entry nameiHEM1_SORC5
AccessioniPrimary (citable) accession number: A9FDP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: September 3, 2014
This is version 56 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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