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A3CU63

- HEM1_METMJ

UniProt

A3CU63 - HEM1_METMJ

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)
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
Sitei89 – 891Important for activityUniRule annotation
Binding sitei99 – 991SubstrateUniRule annotation
Binding sitei110 – 1101SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi179 – 1846NADPUniRule 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

BioCyciMMAR368407:GH7L-998-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:Memar_0980
OrganismiMethanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)
Taxonomic identifieri368407 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanomicrobiaceaeMethanoculleus
ProteomesiUP000002146: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 423423Glutamyl-tRNA reductasePRO_0000335092Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi368407.Memar_0980.

Structurei

3D structure databases

ProteinModelPortaliA3CU63.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 544Substrate bindingUniRule annotation
Regioni104 – 1063Substrate 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.
HOGENOMiHOG000109651.
KOiK02492.
OMAiHEVTGEY.

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.

A3CU63-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPELFTIPLA LAGISHHAAD IATLEAFRFP DEAAFLHEAR ERFRGVLLLQ
60 70 80 90 100
TCNRIEVLVQ GDARSLEGFL QEKGRHGFTV IEGEAVPRHL LELAAGIDSL
110 120 130 140 150
IVGEDQILGQ LKQALAAAEE AGTCCSAIGL CIKKAVHAGV RVRRQTQINR
160 170 180 190 200
GAVSVGSAAV TLAENLLGTL RDRHILVVGS GEMGVLVAQA LAARGLTAIY
210 220 230 240 250
VANRTYERAV MLADKIGGRA VNFKDLYRYI ALSDVVISCT AAPHPVIRTE
260 270 280 290 300
DIRAVMEERL WPLDTHPRHL ILIDIAQPRD VEEGVRSIEG VHLFTIDDLR
310 320 330 340 350
NVNDATMESR RSEADRARGI IDEEAEHFVR LLRRAAADET LALLYTWAES
360 370 380 390 400
IRARERDRAL ARLRERDDRT AEVIDDLTHA LTNKILSDVT TAIRACAECG
410 420
DITTAEALMR AITRGEPCFQ NEE
Length:423
Mass (Da):46,577
Last modified:March 20, 2007 - v1
Checksum:iE6C88D544AB01966
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000562 Genomic DNA. Translation: ABN56913.1.
RefSeqiWP_011843824.1. NC_009051.1.
YP_001046895.1. NC_009051.1.

Genome annotation databases

EnsemblBacteriaiABN56913; ABN56913; Memar_0980.
GeneIDi4847471.
KEGGimem:Memar_0980.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000562 Genomic DNA. Translation: ABN56913.1 .
RefSeqi WP_011843824.1. NC_009051.1.
YP_001046895.1. NC_009051.1.

3D structure databases

ProteinModelPortali A3CU63.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 368407.Memar_0980.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABN56913 ; ABN56913 ; Memar_0980 .
GeneIDi 4847471.
KEGGi mem:Memar_0980.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci MMAR368407:GH7L-998-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: ATCC 35101 / DSM 1498 / JR1.

Entry informationi

Entry nameiHEM1_METMJ
AccessioniPrimary (citable) accession number: A3CU63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 20, 2007
Last modified: October 1, 2014
This is version 63 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