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Q9WX15

- HEM1_STRCO

UniProt

Q9WX15 - HEM1_STRCO

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
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
Sitei99 – 991Important for activityUniRule annotation
Binding sitei109 – 1091SubstrateUniRule annotation
Binding sitei120 – 1201SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi192 – 1976NADPUniRule 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:SCO3319
ORF Names:SCE68.17c
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
ProteomesiUP000001973: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 581581Glutamyl-tRNA reductasePRO_0000114076Add
BLAST

Proteomic databases

PRIDEiQ9WX15.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi100226.SCO3319.

Structurei

3D structure databases

ProteinModelPortaliQ9WX15.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni114 – 1163Substrate bindingUniRule annotation
Regioni292 – 416125InsertAdd
BLAST

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.
InParanoidiQ9WX15.
KOiK02492.
OMAiPYLYVHY.
OrthoDBiEOG6MWNBM.
PhylomeDBiQ9WX15.

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]
SUPFAMiSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9WX15-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSLLVVGLSH RSAPVSVLER ASLNADAQLK LLQDTVAAEP AAEAAVLATC
60 70 80 90 100
NRIELYADVD KFHAGVAELS TLLAQHSGVG LEELTPYLYV HYEDRAVHHL
110 120 130 140 150
FSVACGLDSM VVGEGQILGQ IKDSLARAQD LHTAGRLLND LFQQALRVGK
160 170 180 190 200
RAHSETGIDR AGQSLVTFGL EQLSAGADVE QWARGKKALV IGAGSMSSLA
210 220 230 240 250
AATLARAGVA EIVVANRTFE RAERLALLLE EQYGQRLSEG DDTDVLARAV
260 270 280 290 300
PMDAVPGELT RADVAVSCTG ATGLVLTADS VAATVEGRTG APAVEDTAVQ
310 320 330 340 350
ETAVREAGET PLPGAGSAAD ENCPLDLSSV SSVPSGFSVM GEAAVAGMDA
360 370 380 390 400
ATLEQHGAWA AGGTAVDRTR EAGRSGPEAD AELIGALAAT ATRVGRIPER
410 420 430 440 450
RRPEPVAEAP RPQPVLFLLD LAMPRDVDAA VHRLAGVRLV DIESLADASA
460 470 480 490 500
DAPMAADVDM VRRIVADEVA AFGAAQRAAH ITPTVVALRS MAADVVAGEI
510 520 530 540 550
ARLEGRLPGL DDKHRAEITQ TVKRVVDKLL HAPTVRVKQL AAEPGGAGYA
560 570 580
DALRTLFDLD QETVASVSRA ENSTEKNRGP A
Length:581
Mass (Da):60,562
Last modified:November 1, 1999 - v1
Checksum:iD4E256B105AFA037
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939116 Genomic DNA. Translation: CAB45353.1.
PIRiT36267.
RefSeqiNP_627529.1. NC_003888.3.
WP_011028907.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAB45353; CAB45353; CAB45353.
GeneIDi1098753.
KEGGisco:SCO3319.
PATRICi23736382. VBIStrCoe124346_3379.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939116 Genomic DNA. Translation: CAB45353.1 .
PIRi T36267.
RefSeqi NP_627529.1. NC_003888.3.
WP_011028907.1. NC_003888.3.

3D structure databases

ProteinModelPortali Q9WX15.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 100226.SCO3319.

Proteomic databases

PRIDEi Q9WX15.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB45353 ; CAB45353 ; CAB45353 .
GeneIDi 1098753.
KEGGi sco:SCO3319.
PATRICi 23736382. VBIStrCoe124346_3379.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109649.
InParanoidi Q9WX15.
KOi K02492.
OMAi PYLYVHY.
OrthoDBi EOG6MWNBM.
PhylomeDBi Q9WX15.

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 ]
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: ATCC BAA-471 / A3(2) / M145.

Entry informationi

Entry nameiHEM1_STRCO
AccessioniPrimary (citable) accession number: Q9WX15
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: November 26, 2014
This is version 114 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