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Q5L782

- HEM1_CHLAB

UniProt

Q5L782 - HEM1_CHLAB

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Protein
Glutamyl-tRNA reductase
Gene
hemA, CAB028
Organism
Chlamydophila abortus (strain DSM 27085 / S26/3)
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 sitei51 – 511Nucleophile By similarity
Sitei92 – 921Important for activity By similarity
Binding sitei102 – 1021Substrate By similarity
Binding sitei113 – 1131Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi181 – 1866NADP By similarity

GO - Molecular functioni

  1. NADP binding Source: InterPro
  2. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
Complete GO annotation...

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

BioCyciCABO218497:GJB0-30-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:CAB028
OrganismiChlamydophila abortus (strain DSM 27085 / S26/3)
Taxonomic identifieri218497 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila
ProteomesiUP000001012: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 338338Glutamyl-tRNA reductaseUniRule annotation
PRO_1000093121Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi218497.CAB028.

Structurei

3D structure databases

ProteinModelPortaliQ5L782.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 534Substrate binding By similarity
Regioni107 – 1093Substrate 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.
HOGENOMiHOG000110628.
KOiK02492.
OMAiCHRAELY.
OrthoDBiEOG6MWNBM.

Family and domain databases

HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
[Graphical view]
PfamiPF05201. GlutR_N. 1 hit.
[Graphical view]
SUPFAMiSSF69742. SSF69742. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5L782-1 [UniParc]FASTAAdd to Basket

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MVLGVVGISY REAALKEREA VINILKDFEA NSFFSQHFFG DDGSFVLLLT    50
CHRAEIYYFS KSNRHIQSKL LSRISSLGAR PYCYQGLACF THLFTVTSGM 100
DSLISGETEI QGQVKRAYIK AKTDRDLPFA LHFLFQKALK EGKDFRSQVS 150
LSHPVVTIES VVEETLDLHG KSTKDKLLFI GYSEINRKIA KGLSAKGYRN 200
LIFCSRKNIS IPYDTVARSQ LSFREPYDVI FFGSSESAKD FSGLSLESLA 250
SIPSRVIFDF NVPRTFTLAE SPKDIICLDM DFISERVQKK LQISKQCTNK 300
EKPFLALAAR KQWEVYEKKS SHIPSSQVRA SRPKLLIL 338
Length:338
Mass (Da):38,300
Last modified:June 21, 2005 - v1
Checksum:i12DEC577C95B9289
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR848038 Genomic DNA. Translation: CAH63486.1.
RefSeqiYP_219460.1. NC_004552.2.

Genome annotation databases

EnsemblBacteriaiCAH63486; CAH63486; CAB028.
GeneIDi3337916.
KEGGicab:CAB028.
PATRICi20201396. VBIChlAbo21869_0029.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR848038 Genomic DNA. Translation: CAH63486.1 .
RefSeqi YP_219460.1. NC_004552.2.

3D structure databases

ProteinModelPortali Q5L782.
ModBasei Search...

Protein-protein interaction databases

STRINGi 218497.CAB028.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAH63486 ; CAH63486 ; CAB028 .
GeneIDi 3337916.
KEGGi cab:CAB028.
PATRICi 20201396. VBIChlAbo21869_0029.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000110628.
KOi K02492.
OMAi CHRAELY.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CABO218497:GJB0-30-MONOMER.

Family and domain databases

HAMAPi MF_00087. Glu_tRNA_reductase.
InterProi IPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
[Graphical view ]
Pfami PF05201. GlutR_N. 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: DSM 27085 / S26/3.

Entry informationi

Entry nameiHEM1_CHLAB
AccessioniPrimary (citable) accession number: Q5L782
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 21, 2005
Last modified: September 3, 2014
This is version 61 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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