Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A9KGY4

- HEM1_COXBN

UniProt

A9KGY4 - HEM1_COXBN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Coxiella burnetii (strain Dugway 5J108-111)
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
Sitei95 – 951Important for activityUniRule annotation
Binding sitei105 – 1051SubstrateUniRule annotation
Binding sitei116 – 1161SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi185 – 1906NADPUniRule 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

BioCyciCBUR434922:GJTP-2173-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:CBUD_2065
OrganismiCoxiella burnetii (strain Dugway 5J108-111)
Taxonomic identifieri434922 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella
ProteomesiUP000008555: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 413413Glutamyl-tRNA reductasePRO_1000075405Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi434922.CBUD_2065.

Structurei

3D structure databases

ProteinModelPortaliA9KGY4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni110 – 1123Substrate 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.
HOGENOMiHOG000109650.
KOiK02492.
OMAiHEVTGEY.
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.

A9KGY4 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPLLVCGINH QSAPLTVREK LVFTPERTPL ALQSLLAEKA VNEALLLSTC
60 70 80 90 100
NRTEIYTTVD EAATILRWLS KQPQLSGIDL RSFCYARRDI EMVRHVMRVG
110 120 130 140 150
SGLDSMVLGE PQILGQMKQA YLLARRIGAV GSELGRLFPA VFAATKRIRS
160 170 180 190 200
ETAIGANPVS IAYAVVQLAK RIFSHLNQCQ ILLIGAGETI ELVFSHLYNQ
210 220 230 240 250
GARHFFIANR TLTRAKQIAE PYHAQAIRLS DIPTYLPKVD IVISATMSQL
260 270 280 290 300
PLVGKGAVES ALRQRKRRPL FMADLALPRD IEPETAQLED VYLYNIDDLQ
310 320 330 340 350
TLIAQNRQTR EAAAKQAEAM VEMQAIHYMR QLQVHKAGDT IRRFRERVEM
360 370 380 390 400
LRDQELEKAL AHFQRTNDPK AVIAHFAHNL TNKILHQPTT KLRQAAYEDQ
410
VQLLLSAKEL FDL
Length:413
Mass (Da):46,586
Last modified:February 5, 2008 - v1
Checksum:iA8FD01470941577D
GO

Sequence cautioni

The sequence ABS77974.2 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000733 Genomic DNA. Translation: ABS77974.2. Different initiation.
RefSeqiYP_001425371.2. NC_009727.1.

Genome annotation databases

EnsemblBacteriaiABS77974; ABS77974; CBUD_2065.
GeneIDi5459269.
KEGGicbd:CBUD_2065.
PATRICi17923927. VBICoxBur32972_2036.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000733 Genomic DNA. Translation: ABS77974.2 . Different initiation.
RefSeqi YP_001425371.2. NC_009727.1.

3D structure databases

ProteinModelPortali A9KGY4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 434922.CBUD_2065.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABS77974 ; ABS77974 ; CBUD_2065 .
GeneIDi 5459269.
KEGGi cbd:CBUD_2065.
PATRICi 17923927. VBICoxBur32972_2036.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109650.
KOi K02492.
OMAi HEVTGEY.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CBUR434922:GJTP-2173-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. "Comparative genomics reveal extensive transposon-mediated genomic plasticity and diversity among potential effector proteins within the genus Coxiella."
    Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E., Heinzen R.A.
    Infect. Immun. 77:642-656(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Dugway 5J108-111.

Entry informationi

Entry nameiHEM1_COXBN
AccessioniPrimary (citable) accession number: A9KGY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: October 1, 2014
This is version 58 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3