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C4L4J5

- HEM1_EXISA

UniProt

C4L4J5 - HEM1_EXISA

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Protein
Glutamyl-tRNA reductase
Gene
hemA, EAT1b_2642
Organism
Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b)
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 sitei50 – 501Nucleophile By similarity
Sitei99 – 991Important for activity By similarity
Binding sitei109 – 1091Substrate By similarity
Binding sitei120 – 1201Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 1946NADP 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

BioCyciESP360911:GI4R-2739-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:EAT1b_2642
OrganismiExiguobacterium sp. (strain ATCC BAA-1283 / AT1b)
Taxonomic identifieri360911 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillales Family XII. Incertae SedisExiguobacterium
ProteomesiUP000000716: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 448448Glutamyl-tRNA reductaseUniRule annotation
PRO_1000202635Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi360911.EAT1b_2642.

Structurei

3D structure databases

ProteinModelPortaliC4L4J5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni114 – 1163Substrate 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.
HOGENOMiHOG000109651.
KOiK02492.
OMAiAITCGKK.
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.
SUPFAMiSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C4L4J5-1 [UniParc]FASTAAdd to Basket

« Hide

MHIVVVGLNN KTAPVAIREQ FSFGEQEIVD AMIALREEKS IFESVILSTC    50
NRTELYVVTD QLHTGRYYTK RFLANWFNLE MEQFTPYLSI REGEEAIRHL 100
FRVTSGLDSM IIGETQILGQ VKTSFFRAQE HGTTGTVFNK LFKEAVTLAK 150
RAHTDTQIGE MSVSVSSAAV TLAQEMYQQL EDKQVVVVGA GETGELTTLN 200
LFEAGAKQIA VFNRTESKAK AVADKFKGRA HSIREIACGL LDADILISST 250
GAKEAVIGYD DVAAAQLLRR ERPLLLIDIA VPRDIDPAVA TLPGVHLFDV 300
DDLNGIVNKN LEARLVEAEK IEMKIDEAIQ EFQTWLVTLG VVPIMNELRA 350
RALDIQEDTM TSLERKLDHL SARDKKVIGK HMKSIINQML RDPIDYIKDA 400
AAQPDANVRI AQFIETFGLD VELPEQPVDE VEETDATSAK APLRALMR 448
Length:448
Mass (Da):49,912
Last modified:July 7, 2009 - v1
Checksum:i1952C762AEDBF8E3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001615 Genomic DNA. Translation: ACQ71558.1.
RefSeqiWP_015881117.1. NC_012673.1.
YP_002887003.1. NC_012673.1.

Genome annotation databases

EnsemblBacteriaiACQ71558; ACQ71558; EAT1b_2642.
GeneIDi7869655.
KEGGieat:EAT1b_2642.
PATRICi21880546. VBIExiSp39724_2619.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001615 Genomic DNA. Translation: ACQ71558.1 .
RefSeqi WP_015881117.1. NC_012673.1.
YP_002887003.1. NC_012673.1.

3D structure databases

ProteinModelPortali C4L4J5.
ModBasei Search...

Protein-protein interaction databases

STRINGi 360911.EAT1b_2642.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACQ71558 ; ACQ71558 ; EAT1b_2642 .
GeneIDi 7869655.
KEGGi eat:EAT1b_2642.
PATRICi 21880546. VBIExiSp39724_2619.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
KOi K02492.
OMAi AITCGKK.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci ESP360911:GI4R-2739-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 BAA-1283 / AT1b.

Entry informationi

Entry nameiHEM1_EXISA
AccessioniPrimary (citable) accession number: C4L4J5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 7, 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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