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A8MAH6

- HEM1_CALMQ

UniProt

A8MAH6 - HEM1_CALMQ

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Protein

Glutamyl-tRNA reductase

Gene
hemA, Cmaq_1730
Organism
Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 / IC-167)
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 sitei52 – 521Nucleophile By similarity
Sitei91 – 911Important for activity By similarity
Binding sitei101 – 1011Substrate By similarity
Binding sitei112 – 1121Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi180 – 1856NADP By similarity

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

BioCyciCMAQ397948:GH9M-1770-MONOMER.
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:Cmaq_1730
OrganismiCaldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 / IC-167)
Taxonomic identifieri397948 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaeCaldivirga
ProteomesiUP000001137: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 406406Glutamyl-tRNA reductaseUniRule annotationPRO_0000335085Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi397948.Cmaq_1730.

Structurei

3D structure databases

ProteinModelPortaliA8MAH6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 544Substrate binding By similarity
Regioni106 – 1083Substrate 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.
HOGENOMiHOG000112880.
KOiK02492.
OMAiEHMIEDE.

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]
SUPFAMiSSF69742. SSF69742. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A8MAH6-1 [UniParc]FASTAAdd to Basket

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MGIDDYLSKI RALTLNHKRV STITLSETYF NRDEVYGKLM NYYDEVFLLQ    50
TCNRVEVYVY GDDDSVAEDM YKVKGTINHV DKLVGMNAVR HIFRVAAGLE 100
SAAVGESEIL GQVEDAFNDA RKRGALGGLL GFTIERAIRT GKEIRSRFPE 150
ISIGLASIGS LVAEYVHRVR GLNSRIAVIG AGSIGSDIVR RLAEKGFRNV 200
IIVNRTLDKA KAAALRYGFN YAPIDSLRSV IRDSDVVIFA TSATNPLLRR 250
RDAEELSGKP IIIDVGVPRN VDPEIPGVVS IDELKNIENE IREGKRKALD 300
EASRLIELRL IEYRRLFARR VIEGMIGELT KWGLSIGESE VKRAVKAGLI 350
KNEEDGAALA VKSTVKKIML PLLTYLKELA EEDKFDEALI IISGIKAKLN 400
GDGKQS 406
Length:406
Mass (Da):45,009
Last modified:December 4, 2007 - v1
Checksum:iB5047CF7B54810EA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000852 Genomic DNA. Translation: ABW02553.1.
RefSeqiYP_001541543.1. NC_009954.1.

Genome annotation databases

EnsemblBacteriaiABW02553; ABW02553; Cmaq_1730.
GeneIDi5710155.
KEGGicma:Cmaq_1730.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000852 Genomic DNA. Translation: ABW02553.1 .
RefSeqi YP_001541543.1. NC_009954.1.

3D structure databases

ProteinModelPortali A8MAH6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 397948.Cmaq_1730.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABW02553 ; ABW02553 ; Cmaq_1730 .
GeneIDi 5710155.
KEGGi cma:Cmaq_1730.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000112880.
KOi K02492.
OMAi EHMIEDE.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CMAQ397948:GH9M-1770-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 ]
SUPFAMi SSF69742. SSF69742. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700844 / DSM 13496 / JCM 10307 / IC-167.

Entry informationi

Entry nameiHEM1_CALMQ
AccessioniPrimary (citable) accession number: A8MAH6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: December 4, 2007
Last modified: September 3, 2014
This is version 54 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