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A6QHK6

- HEM1_STAAE

UniProt

A6QHK6 - HEM1_STAAE

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Staphylococcus aureus (strain Newman)
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 sitei50 – 501NucleophileUniRule annotation
Sitei99 – 991Important for activityUniRule annotation
Binding sitei109 – 1091SubstrateUniRule annotation
Binding sitei120 – 1201SubstrateUniRule annotation

Regions

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

BioCyciSAUR426430:GIXC-1589-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:NWMN_1566
OrganismiStaphylococcus aureus (strain Newman)
Taxonomic identifieri426430 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000006386: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 448448Glutamyl-tRNA reductasePRO_1000071249Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi426430.NWMN_1566.

Structurei

3D structure databases

ProteinModelPortaliA6QHK6.
SMRiA6QHK6. Positions 2-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni114 – 1163Substrate 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.
OMAiKMLHGTM.
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.

A6QHK6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHFIAISINH RTADVALREQ VAFRDDALRI AHEDLYETKS ILENVILSTC
60 70 80 90 100
NRTEVYAVVD QIHTGRYYIQ RFLARAFGFE VDDIKAMSEV KVGDEAVEHL
110 120 130 140 150
LRVTSGLDSI VLGETQILGQ IRDAFFLAQS TGTTGTIFNH LFKQAITFAK
160 170 180 190 200
RAHNETDIAD NAVSVSYAAV ELAKKVFGKL KSKQAIIIGA GEMSELSLLN
210 220 230 240 250
LLGSGITDIT VVNRTIENAM KLAAKHQVKY DELSSLPNLL ESADIVISST
260 270 280 290 300
SAQSYIITNE MIERIAENRK QDSLVLIDIA VPRDIEPGIS AITNIFNYDV
310 320 330 340 350
DDLKGLVDAN LRERQLAAAT ISEQIPAEIH AHNEWISMLG VVPVIRALRE
360 370 380 390 400
KAMAIQAETM DSIDRKLPGL SERERKIISK HTKSIINQML KDPIKQAKEL
410 420 430 440
SSDKKSNEKL ELFQNIFDIE AECPHEQAKQ QKESKVKEIS ARRIFSFE
Length:448
Mass (Da):50,099
Last modified:August 21, 2007 - v1
Checksum:iE3E5F81EC9E0F363
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP009351 Genomic DNA. Translation: BAF67838.1.
RefSeqiYP_001332600.1. NC_009641.1.

Genome annotation databases

EnsemblBacteriaiBAF67838; BAF67838; NWMN_1566.
GeneIDi5331994.
KEGGisae:NWMN_1566.
PATRICi19586739. VBIStaAur133992_1698.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP009351 Genomic DNA. Translation: BAF67838.1 .
RefSeqi YP_001332600.1. NC_009641.1.

3D structure databases

ProteinModelPortali A6QHK6.
SMRi A6QHK6. Positions 2-421.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 426430.NWMN_1566.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAF67838 ; BAF67838 ; NWMN_1566 .
GeneIDi 5331994.
KEGGi sae:NWMN_1566.
PATRICi 19586739. VBIStaAur133992_1698.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci SAUR426430:GIXC-1589-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 sequence of Staphylococcus aureus strain Newman and comparative analysis of staphylococcal genomes: polymorphism and evolution of two major pathogenicity islands."
    Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.
    J. Bacteriol. 190:300-310(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Newman.

Entry informationi

Entry nameiHEM1_STAAE
AccessioniPrimary (citable) accession number: A6QHK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: August 21, 2007
Last modified: October 1, 2014
This is version 59 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3