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Q1D8Z9

- HEM1_MYXXD

UniProt

Q1D8Z9 - HEM1_MYXXD

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Myxococcus xanthus (strain DK 1622)
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
Sitei94 – 941Important for activityUniRule annotation
Binding sitei104 – 1041SubstrateUniRule annotation
Binding sitei115 – 1151SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi184 – 1896NADPUniRule 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

BioCyciMXAN246197:GIWU-2632-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:MXAN_2655
OrganismiMyxococcus xanthus (strain DK 1622)
Taxonomic identifieri246197 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeMyxococcus
ProteomesiUP000002402: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 441441Glutamyl-tRNA reductasePRO_1000004653Add
BLAST

Proteomic databases

PRIDEiQ1D8Z9.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi246197.MXAN_2655.

Structurei

3D structure databases

ProteinModelPortaliQ1D8Z9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 504Substrate bindingUniRule annotation
Regioni109 – 1113Substrate 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.
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.

Q1D8Z9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MELICIGLSH RTAPLTVRER LALPESRQVD VLQRLAQAPV EALWVSTCNR
60 70 80 90 100
VEVYLFAPDA AMARQRALME LQVLGGVEAL EHLYEHQGEA ALVHLFRVAC
110 120 130 140 150
SLDSMVLGEA QILGQVKEAF ERGQGAGAVR GELMRACAAA FSCAKRVRTE
160 170 180 190 200
TAIGRAATSM AAAAVQLASK VFDGLAGKTV LVVGAGEMGE LAARHLKQAG
210 220 230 240 250
ASKLYVTNRT LSRAEALAAE VGGQARPFEE LLGLVAAADV VVCSTASQAP
260 270 280 290 300
LFTRDNVGAL GRGRRGRPLF MVDLAVPRDI DPAVGTLDWV HAYDVDDIQK
310 320 330 340 350
FVADNAAARA EEAQKAGVLV AQEVARFVKE RALREGTPVL ARLRQRAEAI
360 370 380 390 400
ARSEVERTLG ALGDGLNEKQ RKSIEAMGRA IVNKLLHEPT ARLRAVGPEG
410 420 430 440
EGNRLAGAAA ELFGLLEEEV GTAAAAPSVM AAPVQVATGG K
Length:441
Mass (Da):46,681
Last modified:July 11, 2006 - v1
Checksum:iDD574763161FD643
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000113 Genomic DNA. Translation: ABF92563.1.
RefSeqiYP_630874.1. NC_008095.1.

Genome annotation databases

EnsemblBacteriaiABF92563; ABF92563; MXAN_2655.
GeneIDi4107254.
KEGGimxa:MXAN_2655.
PATRICi22647839. VBIMyxXan43560_2606.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000113 Genomic DNA. Translation: ABF92563.1 .
RefSeqi YP_630874.1. NC_008095.1.

3D structure databases

ProteinModelPortali Q1D8Z9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 246197.MXAN_2655.

Proteomic databases

PRIDEi Q1D8Z9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABF92563 ; ABF92563 ; MXAN_2655 .
GeneIDi 4107254.
KEGGi mxa:MXAN_2655.
PATRICi 22647839. VBIMyxXan43560_2606.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci MXAN246197:GIWU-2632-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: DK 1622.

Entry informationi

Entry nameiHEM1_MYXXD
AccessioniPrimary (citable) accession number: Q1D8Z9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 11, 2006
Last modified: October 1, 2014
This is version 70 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