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A7HA35

- HEM11_ANADF

UniProt

A7HA35 - HEM11_ANADF

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Protein
Glutamyl-tRNA reductase 1
Gene
hemA1, Anae109_1374
Organism
Anaeromyxobacter sp. (strain Fw109-5)
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) 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 sitei53 – 531Nucleophile By similarity
Sitei94 – 941Important for activity By similarity
Binding sitei104 – 1041Substrate By similarity
Binding sitei115 – 1151Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi184 – 1896NADP By similarity

GO - Molecular functioni

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

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

BioCyciASP404589:GHMT-1383-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase 1 (EC:1.2.1.70)
Short name:
GluTR 1
Gene namesi
Name:hemA1
Ordered Locus Names:Anae109_1374
OrganismiAnaeromyxobacter sp. (strain Fw109-5)
Taxonomic identifieri404589 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter
ProteomesiUP000006382: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 440440Glutamyl-tRNA reductase 1UniRule annotation
PRO_0000335007Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi404589.Anae109_1374.

Structurei

3D structure databases

ProteinModelPortaliA7HA35.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni52 – 554Substrate binding By similarity
Regioni109 – 1113Substrate 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.
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.

A7HA35-1 [UniParc]FASTAAdd to Basket

« Hide

MNGKEIFLVG LSHKSAPIEV RERVALTGDL LKAALCELRA AESVAEAFVV    50
STCNRVEVYV QADGIEPARR FFTERAPDAD EHLYAKIGVE AIRHLFRVSA 100
SLDSMVVGEQ QILGQVKEAY GLASAAEAAG PFMSRLCNRA FATAKRVRTE 150
TDIGRGATSM SQVAVELVEK IFGDLKGRAI LLVGAGKMGA LSAKALAVLG 200
ADRILVTNRS PERGLALAEQ VGGAFRGWDE LPRLLVEADV VIVSTGAPTY 250
VVTRDLVQQA MKARRRRSLC LIDLAVPRNV DPACADLGEV FAYDVDDMEK 300
VVTATQEARR GEALRAEAIV EAEVMAFAKE RDARAALPVL AQLRRHAEQI 350
ARAEAERTLS HLGPKLDEKG KKSVEAMAQA IVNKLLHGPT ARLKAAAATG 400
DGDLPGAAAE LFGIDNDPAR PEGAPAQPAE GRAAASSERS 440
Length:440
Mass (Da):46,929
Last modified:September 11, 2007 - v1
Checksum:i941DD32337F8E19C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000769 Genomic DNA. Translation: ABS25581.1.
RefSeqiWP_011985687.1. NC_009675.1.
YP_001378565.1. NC_009675.1.

Genome annotation databases

EnsemblBacteriaiABS25581; ABS25581; Anae109_1374.
GeneIDi5375324.
KEGGiafw:Anae109_1374.
PATRICi20927931. VBIAnaSp113478_1445.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000769 Genomic DNA. Translation: ABS25581.1 .
RefSeqi WP_011985687.1. NC_009675.1.
YP_001378565.1. NC_009675.1.

3D structure databases

ProteinModelPortali A7HA35.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 404589.Anae109_1374.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABS25581 ; ABS25581 ; Anae109_1374 .
GeneIDi 5375324.
KEGGi afw:Anae109_1374.
PATRICi 20927931. VBIAnaSp113478_1445.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci ASP404589:GHMT-1383-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: Fw109-5.

Entry informationi

Entry nameiHEM11_ANADF
AccessioniPrimary (citable) accession number: A7HA35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: September 11, 2007
Last modified: September 3, 2014
This is version 59 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 By similarity.

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

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