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A9FDP5

- HEM1_SORC5

UniProt

A9FDP5 - HEM1_SORC5

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Protein

Glutamyl-tRNA reductase

Gene

hemA

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).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 – 481NucleophileUniRule annotation
Sitei115 – 1151Important for activityUniRule annotation
Binding sitei125 – 1251SubstrateUniRule annotation
Binding sitei136 – 1361SubstrateUniRule annotation

Regions

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

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

BioCyciSCEL448385:GJ75-1683-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTRUniRule annotation
Gene namesi
Name:hemAUniRule annotation
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 reductasePRO_0000335074Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi448385.sce1624.

Structurei

3D structure databases

ProteinModelPortaliA9FDP5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 504Substrate bindingUniRule annotation
Regioni130 – 1323Substrate bindingUniRule annotation

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.UniRule annotation

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.UniRule annotation

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

« Hide

        10         20         30         40         50
MIFVGLSHKT APIEVRERLA IGRDRLPEVL ARLTAHPAIG EALVLSTCNR
60 70 80 90 100
VEIYASPRQQ APAPPRPGSA PPPSDEELSR NNEALRAAVA TLVGLGGDAV
110 120 130 140 150
RGHLAGRVGS DAVLHLFRVA ASLDSMVVGE PQILGQMKEA IEVARGAKTL
160 170 180 190 200
GVRLGRAAHR AIKVGKRVRT ETAIGAGQVS VSSVAIDLAR QIFADLAGHT
210 220 230 240 250
ALLIGAGDMA EAASKLLVRA GARLIVVNRS PDRAAALARE VGGEPRPWAD
260 270 280 290 300
LERSVIDADI VISSTSSPNY VVTPDLVRRA RKARKGRSLF LIDIAVPRDI
310 320 330 340 350
DPAVNKLDSV YLYDVDDLSQ IVAESVEGRA AEAARAEAIV ADEAQAFEAW
360 370 380 390 400
TLERALTPTI VGLRARTRSI LVAEVERSLS GKLRHLGVAE RQALAMMIDA
410 420 430 440 450
ATNKLLHVPT TRLRAMASDP RVAEHVDSLR ELFDIDGAPP ENAAASALAE
460 470 480 490 500
GELRGAVDGP PTPRSARGAA PPASGARGGG SPRHADPRPQ AAEDNGVYAR
510 520
QPGGRPAEAG VMAVANPAAA VSAAGLKGA
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.
RefSeqiYP_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 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: October 29, 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.UniRule annotation

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