Skip Header

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

A4G1N3

- HEM1_HERAR

UniProt

A4G1N3 - HEM1_HERAR

(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
Herminiimonas arsenicoxydans
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 sitei57 – 571NucleophileUniRule annotation
Sitei109 – 1091Important for activityUniRule annotation
Binding sitei119 – 1191SubstrateUniRule annotation
Binding sitei130 – 1301SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi199 – 2046NADPUniRule 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

BioCyciHARS204773:GJCA-181-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:HEAR0186
OrganismiHerminiimonas arsenicoxydans
Taxonomic identifieri204773 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesOxalobacteraceaeHerminiimonas
ProteomesiUP000006697: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 429429Glutamyl-tRNA reductasePRO_0000335046Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi204773.HEAR0186.

Structurei

3D structure databases

ProteinModelPortaliA4G1N3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni56 – 594Substrate bindingUniRule annotation
Regioni124 – 1263Substrate 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.
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.

A4G1N3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQLLAVGLNH TTAPVSLREK VAFPADQLGQ AVASARVWYG RSDSKTYSDE
60 70 80 90 100
AAILSTCNRT ELYAASHQPG GVNEAIDLTA HFLADYHKLP YSELRPYLYA
110 120 130 140 150
LPQDNAVRHA FRVASGLDSM VLGEPQILGQ MKDAVRQAEA AGGLGTYLHQ
160 170 180 190 200
MFQRTFAVAK EVRSNTEIGA HSVSMAAASV RLSQRIFDTI SEQNVLFIGA
210 220 230 240 250
GEMIELCATH FAAQNPKSLT IANRTLERGE TLAHRFNGRA IRLADLPDQL
260 270 280 290 300
ASYDIVISST ASSLPIIGLG MVERAIKARR HKPMFMVDLA VPRDIETEIG
310 320 330 340 350
RLDDVFLYTV DDLGTFVQTG LENRQAAVTQ AEAIIETRVQ SFMHWIDARA
360 370 380 390 400
VVPVIQDLHE SSEMMRMIEL ERARKLLAKG EDIDAVLEAL SKGLTAKFLH
410 420
GPQQALNNAQ GDERTRLAAL LPQLFRTKR
Length:429
Mass (Da):47,289
Last modified:April 17, 2007 - v1
Checksum:iB6C8D0E7E83455F1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU207211 Genomic DNA. Translation: CAL60420.1.
RefSeqiWP_011869769.1. NC_009138.1.
YP_001098549.1. NC_009138.1.

Genome annotation databases

EnsemblBacteriaiCAL60420; CAL60420; HEAR0186.
GeneIDi4932130.
KEGGihar:HEAR0186.
PATRICi22110578. VBIHerArs17568_0189.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU207211 Genomic DNA. Translation: CAL60420.1 .
RefSeqi WP_011869769.1. NC_009138.1.
YP_001098549.1. NC_009138.1.

3D structure databases

ProteinModelPortali A4G1N3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 204773.HEAR0186.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAL60420 ; CAL60420 ; HEAR0186 .
GeneIDi 4932130.
KEGGi har:HEAR0186.
PATRICi 22110578. VBIHerArs17568_0189.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci HARS204773:GJCA-181-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ULPAs1.

Entry informationi

Entry nameiHEM1_HERAR
AccessioniPrimary (citable) accession number: A4G1N3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 17, 2007
Last modified: October 1, 2014
This is version 65 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