HEM1_PASMU
ID HEM1_PASMU Reviewed; 434 AA.
AC P95525;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 145.
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}; Synonyms=gltX1;
GN OrderedLocusNames=PM0684;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2.5;
RA Castrillon R.T.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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}.
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DR EMBL; Y10430; CAA71452.1; -; Genomic_DNA.
DR EMBL; AE004439; AAK02768.1; -; Genomic_DNA.
DR RefSeq; WP_010906790.1; NC_002663.1.
DR AlphaFoldDB; P95525; -.
DR SMR; P95525; -.
DR STRING; 747.DR93_1518; -.
DR EnsemblBacteria; AAK02768; AAK02768; PM0684.
DR KEGG; pmu:PM0684; -.
DR PATRIC; fig|272843.6.peg.692; -.
DR HOGENOM; CLU_035113_2_2_6; -.
DR OMA; FAFKCAA; -.
DR UniPathway; UPA00251; UER00316.
DR Proteomes; UP000000809; 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..434
FT /note="Glutamyl-tRNA reductase"
FT /id="PRO_0000114052"
FT ACT_SITE 50
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 49..52
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 119..121
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 199..204
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT SITE 104
FT /note="Important for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT CONFLICT 71..72
FT /note="TA -> AT (in Ref. 1; CAA71452)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="G -> D (in Ref. 1; CAA71452)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="M -> P (in Ref. 1; CAA71452)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="N -> S (in Ref. 1; CAA71452)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="A -> V (in Ref. 1; CAA71452)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="V -> A (in Ref. 1; CAA71452)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="A -> V (in Ref. 1; CAA71452)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="L -> F (in Ref. 1; CAA71452)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 434 AA; 48408 MW; 648A624862C5E164 CRC64;
MTILVIGINH KTASVAIREK VAFSAEKRVE ALAQIQQQAL AESAVILSTC NRTEVYFHHK
AIPPQEAESW TARCMQWFAE IHQLSLDALA GCLYSQQNQQ AVLHLMRVAC GLDSLVLGEP
QILGQVKDAY QLSKMYYQGQ NQPLSSEFSR LFQKTFSVAK RVRTETNIGG NAVSVAYGAC
SLARQIFDSL KTLNVLLVGA GETIELTCRH LLRHGVQRIM IANRTFERAQ HLVTKLDGAE
NVQVLALTQL QEGLNQADIV ISSTGSPTIL ITQDMVKIAQ KARCDLPMLL VDIAVPRDIE
ESVGELDSIY HYTVDDLQTI IQRNLVEREK ASAQAWVIIQ QECADFFEWL KVHQFSNLIR
SYRENAEDIR QILLEKALLA LRQGEDSEAV LQALSYKLTN KLLHSPTQVM NAMVKTGNST
GLALFSSTLK SDVE
