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Q8D2K8

- HEM1_WIGBR

UniProt

Q8D2K8 - HEM1_WIGBR

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Wigglesworthia glossinidia brevipalpis
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 sitei50 – 501NucleophileUniRule 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

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:WIGBR3460
OrganismiWigglesworthia glossinidia brevipalpis
Taxonomic identifieri36870 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeWigglesworthia
ProteomesiUP000000562: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 420420Glutamyl-tRNA reductasePRO_0000114087Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi36870.WGLp346.

Structurei

3D structure databases

ProteinModelPortaliQ8D2K8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate 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.
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.

Q8D2K8 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLLVFGISY KTAPISLRER VIFSPENINI ALNNLLKKSD ILGGVILSTC
60 70 80 90 100
NRTEVYLSIK NFYKAKKIII LWLYKFFNDL KIKEIKNNFY SYIDNYAVSH
110 120 130 140 150
LMRVTSGLDS MILGEHQILS QVKSAFFRSL KNKNISIDLQ KLFESAFSVA
160 170 180 190 200
KKIRSETKIG SYSISIPYII CVLLKKIFIS FTEIKVMLIG SGTINELIAK
210 220 230 240 250
QLFKYKIKDL FISNRTIDHA KNLAIKVNGC VVEFNEIFKN LNKMQVIITS
260 270 280 290 300
TYSRKLIITY KIIKSIIEKN KNKKIIFIDI SIPRNIDKKI KKITGVHLYT
310 320 330 340 350
LEDLKDLITN NLEKRKNAAT LAENIIKKES IKFMSHIKGY YSSEIIKKYR
360 370 380 390 400
FQINKLKKIY EKKALLELKL GNNPENIIKK LTYKLTNRLV HKPTKLLYNT
410 420
SCSKNNKDLY DLYNKLKIDL
Length:420
Mass (Da):48,815
Last modified:March 1, 2003 - v1
Checksum:iA695FD99BB728DEF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000021 Genomic DNA. Translation: BAC24492.1.
RefSeqiNP_871349.1. NC_004344.2.

Genome annotation databases

EnsemblBacteriaiBAC24492; BAC24492; BAC24492.
GeneIDi1257153.
KEGGiwbr:WGLp346.
PATRICi24024896. VBIWigGlo15804_0378.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000021 Genomic DNA. Translation: BAC24492.1 .
RefSeqi NP_871349.1. NC_004344.2.

3D structure databases

ProteinModelPortali Q8D2K8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 36870.WGLp346.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC24492 ; BAC24492 ; BAC24492 .
GeneIDi 1257153.
KEGGi wbr:WGLp346.
PATRICi 24024896. VBIWigGlo15804_0378.

Phylogenomic databases

eggNOGi COG0373.
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. "Genome sequence of the endocellular obligate symbiont of tsetse flies, Wigglesworthia glossinidia."
    Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M., Aksoy S.
    Nat. Genet. 32:402-407(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiHEM1_WIGBR
AccessioniPrimary (citable) accession number: Q8D2K8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2003
Last modified: October 1, 2014
This is version 81 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