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A7HBF2

- HEM12_ANADF

UniProt

A7HBF2 - HEM12_ANADF

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Protein
Glutamyl-tRNA reductase 2
Gene
hemA2, Anae109_1845
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 sitei49 – 491Nucleophile By similarity
Sitei93 – 931Important for activity By similarity
Binding sitei103 – 1031Substrate By similarity
Binding sitei114 – 1141Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi183 – 1886NADP 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-1856-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase 2 (EC:1.2.1.70)
Short name:
GluTR 2
Gene namesi
Name:hemA2
Ordered Locus Names:Anae109_1845
OrganismiAnaeromyxobacter sp. (strain Fw109-5)
Taxonomic identifieri404589 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter
ProteomesiUP000006382: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 423423Glutamyl-tRNA reductase 2UniRule annotation
PRO_0000335008Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi404589.Anae109_1845.

Structurei

3D structure databases

ProteinModelPortaliA7HBF2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 514Substrate binding By similarity
Regioni108 – 1103Substrate 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.
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.

A7HBF2-1 [UniParc]FASTAAdd to Basket

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MLVAVGLNQK GATVADREVL ALPAEGFQST LAEYAALDAV DEIAVMSTCY    50
RVEIYAATRC PAAATLSLRQ ALNARAGREL PLFELHGEEA YRHLVRVASS 100
LESAILGEPQ ILGQVKEAFQ RSIDQGVAAK ELTSVLNRAL SAAKRVRTDT 150
AIGRAGISWG HAAATLAEKV LGKMQGRRVV VVGAGEMARL SAQHLRDQGA 200
RIVVLNRTLV NGEALAREVG GVARPLEALG EELAQADVVV SAAPVAPDAF 250
QPEAMAELSR SRKRPIVLVD LAVPRAIPAA TGAIRDVYLC DVDDLDRVMK 300
AAMSERAAAV ADADRIIAEE VGKFVRAEAE RRAAPLIQEM RTRASAIARE 350
EVERTLRRLG EDPEVERRLE AMAGSIVSKI LHAPSARLRQ AVCDGCSGEA 400
LVSAAVEIFE LSADIRVHRG NAA 423
Length:423
Mass (Da):45,130
Last modified:May 20, 2008 - v2
Checksum:i494272D1FBFC0093
GO

Sequence cautioni

The sequence ABS26048.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000769 Genomic DNA. Translation: ABS26048.1. Different initiation.
RefSeqiWP_012096626.1. NC_009675.1.
YP_001379032.1. NC_009675.1.

Genome annotation databases

EnsemblBacteriaiABS26048; ABS26048; Anae109_1845.
GeneIDi5377847.
KEGGiafw:Anae109_1845.
PATRICi20928931. VBIAnaSp113478_1943.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000769 Genomic DNA. Translation: ABS26048.1 . Different initiation.
RefSeqi WP_012096626.1. NC_009675.1.
YP_001379032.1. NC_009675.1.

3D structure databases

ProteinModelPortali A7HBF2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 404589.Anae109_1845.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABS26048 ; ABS26048 ; Anae109_1845 .
GeneIDi 5377847.
KEGGi afw:Anae109_1845.
PATRICi 20928931. VBIAnaSp113478_1943.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci ASP404589:GHMT-1856-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 nameiHEM12_ANADF
AccessioniPrimary (citable) accession number: A7HBF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: September 3, 2014
This is version 58 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 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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