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Q9UXR8

- HEM1_METKA

UniProt

Q9UXR8 - HEM1_METKA

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). In the absence of NADPH, exhibits substrate esterase activity, leading to the release of glutamate from tRNA.1 Publication

Catalytic activityi

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.

Enzyme regulationi

Inhibited by heavy metal compounds, Zn2+, and heme. Also competitively inhibited by glutamycin.

pH dependencei

Optimum pH is 8.1.

Temperature dependencei

Optimum temperature is 90 degrees Celsius.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei48 – 481Nucleophile
Sitei84 – 841Important for activity
Binding sitei94 – 941Substrate
Binding sitei105 – 1051Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi174 – 1796NADPCurated

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

BRENDAi1.2.1.70. 3274.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
Ordered Locus Names:MK0200
OrganismiMethanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Taxonomic identifieri190192 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanopyriMethanopyralesMethanopyraceaeMethanopyrus
ProteomesiUP000001826: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi48 – 481C → S: Complete loss of activity. 1 Publication
Mutagenesisi84 – 841H → A: Complete loss of activity. 1 Publication
Mutagenesisi84 – 841H → N: 30% of wild-type reductase activity. 15% of wild-type esterase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 404404Glutamyl-tRNA reductasePRO_0000114102Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi190192.MK0200.

Structurei

Secondary structure

1
404
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107Combined sources
Turni11 – 133Combined sources
Helixi16 – 227Combined sources
Helixi29 – 368Combined sources
Beta strandi40 – 478Combined sources
Beta strandi50 – 578Combined sources
Helixi62 – 676Combined sources
Beta strandi74 – 774Combined sources
Helixi78 – 8912Combined sources
Turni90 – 934Combined sources
Beta strandi94 – 963Combined sources
Helixi100 – 11617Combined sources
Helixi121 – 14020Combined sources
Helixi150 – 16213Combined sources
Beta strandi169 – 1746Combined sources
Helixi177 – 18913Combined sources
Beta strandi192 – 1976Combined sources
Helixi201 – 21111Combined sources
Helixi218 – 2203Combined sources
Helixi221 – 2266Combined sources
Beta strandi229 – 2335Combined sources
Beta strandi236 – 2394Combined sources
Helixi244 – 25310Combined sources
Beta strandi260 – 2645Combined sources
Helixi275 – 2773Combined sources
Beta strandi281 – 2855Combined sources
Helixi286 – 30116Combined sources
Helixi304 – 35047Combined sources
Helixi365 – 38218Combined sources
Turni386 – 3905Combined sources
Helixi391 – 40212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GPJX-ray1.95A1-404[»]
ProteinModelPortaliQ9UXR8.
SMRiQ9UXR8. Positions 1-404.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UXR8.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 504Substrate binding
Regioni99 – 1013Substrate binding

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.Curated

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109651.
KOiK02492.
OMAiYREADAN.

Family and domain databases

Gene3Di1.10.1200.70. 1 hit.
3.40.50.720. 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.

Q9UXR8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEDLVCVGIT HKEAEVEELE KARFESDEAV RDIVESFGLS GCVLLQTCNR
60 70 80 90 100
VEVYASGARD RAEELGDLIH DDAWVKRGSE AVRHLFRVAC GLESMMVGEQ
110 120 130 140 150
EILRQVKKAY DRAARLGTLD EALKIVFRRA INLGKRAREE TRISEGAVSI
160 170 180 190 200
GSAAVELAER ELGSLHDKTV LVVGAGEMGK TVAKSLVDRG VRAVLVANRT
210 220 230 240 250
YERAVELARD LGGEAVRFDE LVDHLARSDV VVSATAAPHP VIHVDDVREA
260 270 280 290 300
LRKRDRRSPI LIIDIANPRD VEEGVENIED VEVRTIDDLR VIARENLERR
310 320 330 340 350
RKEIPKVEKL IEEELSTVEE ELEKLKERRL VADVAKSLHE IKDRELERAL
360 370 380 390 400
RRLKTGDPEN VLQDFAEAYT KRLINVLTSA IMELPDEYRR AACRALRRAS

ELNG
Length:404
Mass (Da):45,444
Last modified:May 1, 2000 - v1
Checksum:i8B6DBE436EA073B3
GO

Mass spectrometryi

Molecular mass is 45436±30 Da from positions 1 - 404. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ131561 Genomic DNA. Translation: CAB59204.1.
AE009439 Genomic DNA. Translation: AAM01417.1.
PIRiT45026.
RefSeqiNP_613487.1. NC_003551.1.
WP_011018572.1. NC_003551.1.

Genome annotation databases

EnsemblBacteriaiAAM01417; AAM01417; MK0200.
GeneIDi1477503.
KEGGimka:MK0200.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ131561 Genomic DNA. Translation: CAB59204.1 .
AE009439 Genomic DNA. Translation: AAM01417.1 .
PIRi T45026.
RefSeqi NP_613487.1. NC_003551.1.
WP_011018572.1. NC_003551.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GPJ X-ray 1.95 A 1-404 [» ]
ProteinModelPortali Q9UXR8.
SMRi Q9UXR8. Positions 1-404.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 190192.MK0200.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAM01417 ; AAM01417 ; MK0200 .
GeneIDi 1477503.
KEGGi mka:MK0200.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
KOi K02492.
OMAi YREADAN.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BRENDAi 1.2.1.70. 3274.

Miscellaneous databases

EvolutionaryTracei Q9UXR8.

Family and domain databases

Gene3Di 1.10.1200.70. 1 hit.
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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-30, FUNCTION, MASS SPECTROMETRY, CATALYTIC MECHANISM, MUTAGENESIS OF CYS-48 AND HIS-84.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.
  3. "V-shaped structure of glutamyl-tRNA reductase, the first enzyme of tRNA-dependent tetrapyrrole biosynthesis."
    Moser J., Schubert W.-D., Beier V., Bringemeier I., Jahn D., Heinz D.W.
    EMBO J. 20:6583-6590(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT, CATALYTIC MECHANISM, DOMAIN.

Entry informationi

Entry nameiHEM1_METKA
AccessioniPrimary (citable) accession number: Q9UXR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3