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Q93ST4

- HEM1_CHLTE

UniProt

Q93ST4 - HEM1_CHLTE

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Protein
Glutamyl-tRNA reductase
Gene
hemA, CT1426
Organism
Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA) By similarity.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 – 501Nucleophile By similarity
Sitei99 – 991Important for activity By similarity
Binding sitei109 – 1091Substrate By similarity
Binding sitei120 – 1201Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 1946NADP By similarity

GO - Molecular functioni

  1. NADP binding Source: InterPro
  2. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. chlorophyll biosynthetic process Source: UniProtKB-HAMAP
  2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Chlorophyll biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciCTEP194439:GHN0-1465-MONOMER.
UniPathwayiUPA00251; UER00316.
UPA00668.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
Ordered Locus Names:CT1426
OrganismiChlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS)
Taxonomic identifieri194439 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum
ProteomesiUP000001007: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 426426Glutamyl-tRNA reductaseUniRule annotation
PRO_0000114007Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi194439.CT1426.

Structurei

3D structure databases

ProteinModelPortaliQ93ST4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni114 – 1163Substrate binding By similarity

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 By similarity.UniRule annotation

Sequence similaritiesi

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.

Q93ST4-1 [UniParc]FASTAAdd to Basket

« Hide

MNIISVGVNH KTAPIEIRER IALSEVQNKE LVTDLVSSGL ASEAMVVSTC    50
NRTELYVVPG MPEVNCDYLK DYIISYKNAR NAVRPEHFFS RFYCGTARHL 100
FEVSCAIDSL VLGEGQILGQ VKNAYRIAAE VGTAGILLTR LCHTAFSVAK 150
KVKTRTKLME GAVSVSYAAV ELAQKIFSNL SMKKVLLIGA GETGELAAKH 200
MYAKNARNIV ITNRTQSKAE ALAEELGTNR VLPYESYKEH LHEFDIIITA 250
VSTKEYILNA AEMQQSMAKR RLKPVIILDL GLPRNVDPEV GALQNMFLKD 300
IDALKHIIDK NLERRRAELP KVKAIIDEEL VAFGQWLNTL KVRPTIVDLQ 350
SKFLEIKEKE LERYRYKVSE EELRRMEHLT DRILKKILHH PIKMLKAPVD 400
TADNIPSKVN LVRNIFDLEE PNQSLQ 426
Length:426
Mass (Da):48,133
Last modified:August 30, 2002 - v2
Checksum:iA7122C2C947D2429
GO

Sequence cautioni

The sequence AAG12432.1 differs from that shown. Reason: Frameshift at position 319.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY005138 Genomic DNA. Translation: AAG12432.1. Frameshift.
AE006470 Genomic DNA. Translation: AAM72654.1.
RefSeqiNP_662312.1. NC_002932.3.
WP_010933093.1. NC_002932.3.

Genome annotation databases

EnsemblBacteriaiAAM72654; AAM72654; CT1426.
GeneIDi1006241.
KEGGicte:CT1426.
PATRICi21400779. VBIChlTep116050_1294.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY005138 Genomic DNA. Translation: AAG12432.1 . Frameshift.
AE006470 Genomic DNA. Translation: AAM72654.1 .
RefSeqi NP_662312.1. NC_002932.3.
WP_010933093.1. NC_002932.3.

3D structure databases

ProteinModelPortali Q93ST4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 194439.CT1426.

Protocols and materials databases

DNASUi 1006241.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAM72654 ; AAM72654 ; CT1426 .
GeneIDi 1006241.
KEGGi cte:CT1426.
PATRICi 21400779. VBIChlTep116050_1294.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
UPA00668 .
BioCyci CTEP194439:GHN0-1465-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

« Hide 'large scale' publications
  1. "Molecular evidence for the early evolution of photosynthesis."
    Xiong J., Fischer W.M., Inoue K., Nakahara M., Bauer C.E.
    Science 289:1724-1730(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 49652 / DSM 12025 / TLS.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49652 / DSM 12025 / TLS.

Entry informationi

Entry nameiHEM1_CHLTE
AccessioniPrimary (citable) accession number: Q93ST4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: August 30, 2002
Last modified: September 3, 2014
This is version 101 of the entry and version 2 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 By similarity.

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

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