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B9DZF9

- HEM1_CLOK1

UniProt

B9DZF9 - HEM1_CLOK1

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Protein
Glutamyl-tRNA reductase
Gene
hemA, CKR_0583
Organism
Clostridium kluyveri (strain NBRC 12016)
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 sitei46 – 461Nucleophile 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 bindingi177 – 1826NADP 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

BioCyciCKLU583346:GJNQ-616-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:CKR_0583
OrganismiClostridium kluyveri (strain NBRC 12016)
Taxonomic identifieri583346 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000007969: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 399399Glutamyl-tRNA reductaseUniRule annotation
PRO_1000190513Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi583346.CKR_0583.

Structurei

3D structure databases

ProteinModelPortaliB9DZF9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 484Substrate 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.
HOGENOMiHOG000090159.
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.
SUPFAMiSSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B9DZF9-1 [UniParc]FASTAAdd to Basket

« Hide

MIQLIGIKSQ CDIGIRQKFS ITSEVLEGKL KYINELVGSV LILSTCNRTE    50
IYVDSNLEEK KLIDTVFYGL DWDYDLVSYI FYIKDKYAIK HLMEVSCGFH 100
SKILGEDQIL GQIKTAYDAA LEAKTIKGKL QRLFQKAITC GKEFKHICES 150
YRIPVSIPSI VAKEILNMDI RKYMIIGFGK IGQLLFKYLN NSQAQIIYIA 200
VRDLNKVHDS YKKCGKIRFI SFKDRKSYYN DIDCIVSCTS APDKIISKGD 250
LPCRKLTIFD LAVPEDIDRN VLDLDNVTLY DIDNISVIDE KNKAIRKKTM 300
GKYRYILENH IDKFIKWEKL HQLSPEIQKV KKYGDEICEK RITTFKNKKH 350
TKDNDILVKT MIESTARFYI NRAIEVMKEE KLNGREEECL RLINKIFCK 399
Length:399
Mass (Da):46,435
Last modified:March 24, 2009 - v1
Checksum:i5D94C09FD7EBFC71
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP009049 Genomic DNA. Translation: BAH05634.1.
RefSeqiYP_002471048.1. NC_011837.1.

Genome annotation databases

EnsemblBacteriaiBAH05634; BAH05634; CKR_0583.
GeneIDi7274060.
KEGGickr:CKR_0583.
PATRICi19470916. VBICloKlu118830_0717.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP009049 Genomic DNA. Translation: BAH05634.1 .
RefSeqi YP_002471048.1. NC_011837.1.

3D structure databases

ProteinModelPortali B9DZF9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 583346.CKR_0583.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAH05634 ; BAH05634 ; CKR_0583 .
GeneIDi 7274060.
KEGGi ckr:CKR_0583.
PATRICi 19470916. VBICloKlu118830_0717.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000090159.
KOi K02492.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CKLU583346:GJNQ-616-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 SSF69742. SSF69742. 1 hit.
TIGRFAMsi TIGR01035. hemA. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete genome sequence of Clostridium kluyveri and comparative genomics of Clostridia species."
    Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., Vertes A.A., Yukawa H.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NBRC 12016.

Entry informationi

Entry nameiHEM1_CLOK1
AccessioniPrimary (citable) accession number: B9DZF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: September 3, 2014
This is version 44 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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