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A8MAH6

- HEM1_CALMQ

UniProt

A8MAH6 - HEM1_CALMQ

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Protein

Glutamyl-tRNA reductase

Gene

hemA

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).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 – 521NucleophileUniRule annotation
Sitei91 – 911Important for activityUniRule annotation
Binding sitei101 – 1011SubstrateUniRule annotation
Binding sitei112 – 1121SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi180 – 1856NADPUniRule 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

BioCyciCMAQ397948:GH9M-1770-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: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 reductasePRO_0000335085Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi397948.Cmaq_1730.

Structurei

3D structure databases

ProteinModelPortaliA8MAH6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 544Substrate bindingUniRule annotation
Regioni106 – 1083Substrate 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.
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

« Hide

        10         20         30         40         50
MGIDDYLSKI RALTLNHKRV STITLSETYF NRDEVYGKLM NYYDEVFLLQ
60 70 80 90 100
TCNRVEVYVY GDDDSVAEDM YKVKGTINHV DKLVGMNAVR HIFRVAAGLE
110 120 130 140 150
SAAVGESEIL GQVEDAFNDA RKRGALGGLL GFTIERAIRT GKEIRSRFPE
160 170 180 190 200
ISIGLASIGS LVAEYVHRVR GLNSRIAVIG AGSIGSDIVR RLAEKGFRNV
210 220 230 240 250
IIVNRTLDKA KAAALRYGFN YAPIDSLRSV IRDSDVVIFA TSATNPLLRR
260 270 280 290 300
RDAEELSGKP IIIDVGVPRN VDPEIPGVVS IDELKNIENE IREGKRKALD
310 320 330 340 350
EASRLIELRL IEYRRLFARR VIEGMIGELT KWGLSIGESE VKRAVKAGLI
360 370 380 390 400
KNEEDGAALA VKSTVKKIML PLLTYLKELA EEDKFDEALI IISGIKAKLN

GDGKQS
Length:406
Mass (Da):45,009
Last modified:December 4, 2007 - v1
Checksum:iB5047CF7B54810EA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: October 1, 2014
This is version 55 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