HEM1_NATPD
ID HEM1_NATPD Reviewed; 453 AA.
AC Q3ING1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Glutamyl-tRNA reductase {ECO:0000255|HAMAP-Rule:MF_00087};
DE Short=GluTR {ECO:0000255|HAMAP-Rule:MF_00087};
DE EC=1.2.1.70 {ECO:0000255|HAMAP-Rule:MF_00087};
GN Name=hemA {ECO:0000255|HAMAP-Rule:MF_00087}; OrderedLocusNames=NP_4502A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu)
CC to glutamate 1-semialdehyde (GSA). {ECO:0000255|HAMAP-Rule:MF_00087}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-
CC glutamyl-tRNA(Glu) + NADPH; Xref=Rhea:RHEA:12344, Rhea:RHEA-
CC COMP:9663, Rhea:RHEA-COMP:9680, ChEBI:CHEBI:15378, ChEBI:CHEBI:57501,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78520; EC=1.2.1.70; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00087};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
CC {ECO:0000255|HAMAP-Rule:MF_00087}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00087}.
CC -!- DOMAIN: Possesses an unusual extended V-shaped dimeric structure with
CC each monomer consisting of three distinct domains arranged along a
CC curved 'spinal' alpha-helix. The N-terminal catalytic domain
CC specifically recognizes the glutamate moiety of the substrate. The
CC second domain is the NADPH-binding domain, and the third C-terminal
CC domain is responsible for dimerization. {ECO:0000255|HAMAP-
CC Rule:MF_00087}.
CC -!- MISCELLANEOUS: During catalysis, the active site Cys acts as a
CC nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate
CC with the formation of a thioester intermediate between enzyme and
CC glutamate, and the concomitant release of tRNA(Glu). The thioester
CC intermediate is finally reduced by direct hydride transfer from NADPH,
CC to form the product GSA. {ECO:0000255|HAMAP-Rule:MF_00087}.
CC -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
CC {ECO:0000255|HAMAP-Rule:MF_00087}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR936257; CAI50342.1; -; Genomic_DNA.
DR RefSeq; WP_011323957.1; NC_007426.1.
DR AlphaFoldDB; Q3ING1; -.
DR SMR; Q3ING1; -.
DR STRING; 348780.NP_4502A; -.
DR EnsemblBacteria; CAI50342; CAI50342; NP_4502A.
DR GeneID; 3702804; -.
DR KEGG; nph:NP_4502A; -.
DR eggNOG; arCOG01036; Archaea.
DR HOGENOM; CLU_035113_0_1_2; -.
DR OMA; FAFKCAA; -.
DR OrthoDB; 48038at2157; -.
DR UniPathway; UPA00251; UER00316.
DR Proteomes; UP000002698; Chromosome.
DR GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.460.30; -; 1.
DR HAMAP; MF_00087; Glu_tRNA_reductase; 1.
DR InterPro; IPR000343; 4pyrrol_synth_GluRdtase.
DR InterPro; IPR015896; 4pyrrol_synth_GluRdtase_dimer.
DR InterPro; IPR015895; 4pyrrol_synth_GluRdtase_N.
DR InterPro; IPR018214; GluRdtase_CS.
DR InterPro; IPR036453; GluRdtase_dimer_dom_sf.
DR InterPro; IPR036343; GluRdtase_N_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR Pfam; PF00745; GlutR_dimer; 1.
DR Pfam; PF05201; GlutR_N; 1.
DR Pfam; PF01488; Shikimate_DH; 1.
DR PIRSF; PIRSF000445; 4pyrrol_synth_GluRdtase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF69075; SSF69075; 1.
DR SUPFAM; SSF69742; SSF69742; 1.
DR TIGRFAMs; TIGR01035; hemA; 1.
DR PROSITE; PS00747; GLUTR; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase; Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..453
FT /note="Glutamyl-tRNA reductase"
FT /id="PRO_1000004654"
FT REGION 413..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 53
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 52..55
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 110..112
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 184..189
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT SITE 95
FT /note="Important for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
SQ SEQUENCE 453 AA; 47809 MW; 839ADF48145910A7 CRC64;
MTVETGIVVG ASVSHSHASI DQIETAADGS QQTAVEELLS KEGVSEAFVL QTCNRAEAYV
VANDSETGTA ALAGYLAGVD DDAIRMLSHN QSLKHLMAVA CGLESLVIGE DQILGQVRDA
YEDARGVGGV GPTLNDAVLK ALHVGERART ETAINEGAVS LGSAAVRFAA ERHGVTGSTA
LVVGAGEMAT LAAKALDDPA SRVIVANRTR ERAERLAEEL STTASVVGVD SVDEAADAAD
VVVSATGSED YVIDTADLGG VGETCVLDIA QPRDVAPGAD GIDGVAVYDL DTIESVTDEA
RAKRREAAET VETMIDEEFE HLMTQYKRKR ADQVIAAMYE GAERIKAREL RTAVSKFEAE
REDGLSEREH EIVESMADAL VGQLLSAPTQ SLRDAAEEDD WATINAALQL FGPGLEPEPT
ELPTVPDGPE GVPEELRERM SSGMLEQFST NDD
