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Q93ST4

- HEM1_CHLTE

UniProt

Q93ST4 - HEM1_CHLTE

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS)
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 bindingi189 – 1946NADPUniRule annotation

GO - Molecular functioni

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

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 reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTRUniRule annotation
Gene namesi
Name:hemAUniRule annotation
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 reductasePRO_0000114007Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi194439.CT1426.

Structurei

3D structure databases

ProteinModelPortaliQ93ST4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni114 – 1163Substrate 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.

Q93ST4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNIISVGVNH KTAPIEIRER IALSEVQNKE LVTDLVSSGL ASEAMVVSTC
60 70 80 90 100
NRTELYVVPG MPEVNCDYLK DYIISYKNAR NAVRPEHFFS RFYCGTARHL
110 120 130 140 150
FEVSCAIDSL VLGEGQILGQ VKNAYRIAAE VGTAGILLTR LCHTAFSVAK
160 170 180 190 200
KVKTRTKLME GAVSVSYAAV ELAQKIFSNL SMKKVLLIGA GETGELAAKH
210 220 230 240 250
MYAKNARNIV ITNRTQSKAE ALAEELGTNR VLPYESYKEH LHEFDIIITA
260 270 280 290 300
VSTKEYILNA AEMQQSMAKR RLKPVIILDL GLPRNVDPEV GALQNMFLKD
310 320 330 340 350
IDALKHIIDK NLERRRAELP KVKAIIDEEL VAFGQWLNTL KVRPTIVDLQ
360 370 380 390 400
SKFLEIKEKE LERYRYKVSE EELRRMEHLT DRILKKILHH PIKMLKAPVD
410 420
TADNIPSKVN LVRNIFDLEE PNQSLQ
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. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: October 1, 2014
This is version 102 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.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