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Q8CNY6

- HEM1_STAES

UniProt

Q8CNY6 - HEM1_STAES

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Protein

Glutamyl-tRNA reductase

Gene
hemA, SE_1347
Organism
Staphylococcus epidermidis (strain ATCC 12228)
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. 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

BioCyciSEPI176280:GCDG-1353-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:SE_1347
OrganismiStaphylococcus epidermidis (strain ATCC 12228)
Taxonomic identifieri176280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000001411: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 448448Glutamyl-tRNA reductaseUniRule annotationPRO_0000114073Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi176280.SE1347.

Structurei

3D structure databases

ProteinModelPortaliQ8CNY6.

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.
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.

Q8CNY6-1 [UniParc]FASTAAdd to Basket

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MHFVAISINH RTADVTLREQ VAFRDDALRL AHEDLYETKA ILENVILSTC    50
NRTEVYAIVD QVHTGRYYIQ RFLARSFGFE VDDIKDMSQV KVGDDAVEHL 100
LRVTSGLDSI VLGETQILGQ MRDAFFLAQN TGTTGTIFNH LFKQAITFAK 150
KAHSETDIAD NAVSVSYAAV ELAKKVFGKL KSKHAVVIGA GEMGELSLLN 200
LLGSGISNVT IVNRTLSKAK ILAEKHNVSY DSLSALPSLL ETTDIVISST 250
SAEDYIITNS MVKTISETRK LDSLVLIDIA VPRDIEPGID AITNIFNYDV 300
DDLKDLVDAN LRERQLAAET IAGQIPEEID SHNEWVNMLG VVPVIRALRE 350
KAMNIQAETM ESIDRKLPDL SERERKVISK HTKSIINQML KDPIKQAKEL 400
STDKKSNEKL ELFQNIFDIE AEDPREKAKL EKESRAKEIL AHRIFSFE 448
Length:448
Mass (Da):50,151
Last modified:March 1, 2003 - v1
Checksum:iF89F44784F3256A2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE015929 Genomic DNA. Translation: AAO04946.1.
RefSeqiNP_764902.1. NC_004461.1.

Genome annotation databases

EnsemblBacteriaiAAO04946; AAO04946; SE_1347.
GeneIDi1056307.
KEGGisep:SE1347.
PATRICi19608486. VBIStaEpi113981_1316.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE015929 Genomic DNA. Translation: AAO04946.1 .
RefSeqi NP_764902.1. NC_004461.1.

3D structure databases

ProteinModelPortali Q8CNY6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 176280.SE1347.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAO04946 ; AAO04946 ; SE_1347 .
GeneIDi 1056307.
KEGGi sep:SE1347.
PATRICi 19608486. VBIStaEpi113981_1316.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci SEPI176280:GCDG-1353-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. "Genome-based analysis of virulence genes in a non-biofilm-forming Staphylococcus epidermidis strain (ATCC 12228)."
    Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.
    Mol. Microbiol. 49:1577-1593(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 12228.

Entry informationi

Entry nameiHEM1_STAES
AccessioniPrimary (citable) accession number: Q8CNY6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: March 1, 2003
Last modified: September 3, 2014
This is version 93 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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