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C4XPF2

- HEM1_DESMR

UniProt

C4XPF2 - HEM1_DESMR

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Desulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / 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).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 – 511NucleophileUniRule annotation
Sitei100 – 1001Important for activityUniRule annotation
Binding sitei110 – 1101SubstrateUniRule annotation
Binding sitei121 – 1211SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi190 – 1956NADPUniRule 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

BioCyciDMAG573370:GHJL-1656-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:DMR_16420
OrganismiDesulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1)
Taxonomic identifieri573370 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
ProteomesiUP000009071: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 453453Glutamyl-tRNA reductasePRO_1000202632Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi573370.DMR_16420.

Structurei

3D structure databases

ProteinModelPortaliC4XPF2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 534Substrate bindingUniRule annotation
Regioni115 – 1173Substrate 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.
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.

C4XPF2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEQQIYLFGL NHKTAGVEVR EAFALGERPK LGELLVDGEA RVREALVLST
60 70 80 90 100
CNRVEVLVVD PVGRDPKAAV LAAWAGQCGQ DPALLAPHLY AHQGMAAVDH
110 120 130 140 150
LFCVASGLDS LVLGEPQILG QLKAAYRHAV ASRTAGVIIN RLCHKAFSVA
160 170 180 190 200
KKVRTATGIG ASAVSISYAA VELAKRIFGE MAGKKAMLVG AGEMAELAAM
210 220 230 240 250
HLLTSGVSEI LVANRTYARA EELAGRFKGR AVAFEEFVSR LHEVDIVISS
260 270 280 290 300
TGAPHVVIRA KDVRAVLKAR RHKPMFFIDI AVPRDIDPDI NSLDNVYLYD
310 320 330 340 350
IDDLQEVVEE NLAQRREEAA RARDIIGLQV ERFGEWVKSL DVKPTIVDLL
360 370 380 390 400
DVGASLARQE LQKTLRRLGP EVPEETRAAL ETMALSISRK MLHEPIAFLK
410 420 430 440 450
RRAKEEHGER FVDLTRRMYN LDREKVPTDA HADRKPPNFA ETSDDFDVTD

ASE
Length:453
Mass (Da):49,859
Last modified:July 28, 2009 - v1
Checksum:i9C9312275C756136
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP010904 Genomic DNA. Translation: BAH75133.1.
RefSeqiYP_002953019.1. NC_012796.1.

Genome annotation databases

EnsemblBacteriaiBAH75133; BAH75133; DMR_16420.
GeneIDi7981754.
KEGGidma:DMR_16420.
PATRICi21749513. VBIDesMag26496_1537.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP010904 Genomic DNA. Translation: BAH75133.1 .
RefSeqi YP_002953019.1. NC_012796.1.

3D structure databases

ProteinModelPortali C4XPF2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 573370.DMR_16420.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAH75133 ; BAH75133 ; DMR_16420 .
GeneIDi 7981754.
KEGGi dma:DMR_16420.
PATRICi 21749513. VBIDesMag26496_1537.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci DMAG573370:GHJL-1656-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. "Whole genome sequence of Desulfovibrio magneticus strain RS-1 revealed common gene clusters in magnetotactic bacteria."
    Nakazawa H., Arakaki A., Narita-Yamada S., Yashiro I., Jinno K., Aoki N., Tsuruyama A., Okamura Y., Tanikawa S., Fujita N., Takeyama H., Matsunaga T.
    Genome Res. 19:1801-1808(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700980 / DSM 13731 / RS-1.

Entry informationi

Entry nameiHEM1_DESMR
AccessioniPrimary (citable) accession number: C4XPF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: October 29, 2014
This is version 44 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