HEM1_PSEAE
ID HEM1_PSEAE Reviewed; 422 AA.
AC P42807;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 149.
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=PA4666;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=7883699; DOI=10.1128/jb.177.6.1435-1443.1995;
RA Hungerer C., Troup B., Roemling U., Jahn D.;
RT "Regulation of the hemA gene during 5-aminolevulinic acid formation in
RT Pseudomonas aeruginosa.";
RL J. Bacteriol. 177:1435-1443(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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 -!- SEQUENCE CAUTION:
CC Sequence=CAA57574.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X82071; CAA57574.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE004091; AAG08053.1; -; Genomic_DNA.
DR PIR; C83063; C83063.
DR RefSeq; NP_253355.1; NC_002516.2.
DR RefSeq; WP_003095001.1; NZ_QZGE01000029.1.
DR AlphaFoldDB; P42807; -.
DR SMR; P42807; -.
DR STRING; 287.DR97_1975; -.
DR PaxDb; P42807; -.
DR PRIDE; P42807; -.
DR EnsemblBacteria; AAG08053; AAG08053; PA4666.
DR GeneID; 881361; -.
DR KEGG; pae:PA4666; -.
DR PATRIC; fig|208964.12.peg.4888; -.
DR PseudoCAP; PA4666; -.
DR HOGENOM; CLU_035113_2_2_6; -.
DR InParanoid; P42807; -.
DR OMA; FAFKCAA; -.
DR PhylomeDB; P42807; -.
DR BioCyc; PAER208964:G1FZ6-4762-MON; -.
DR UniPathway; UPA00251; UER00316.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0008883; F:glutamyl-tRNA reductase activity; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0019353; P:protoporphyrinogen IX biosynthetic process from glutamate; IBA:GO_Central.
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..422
FT /note="Glutamyl-tRNA reductase"
FT /id="PRO_0000114058"
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 107
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 112..114
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 187..192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT SITE 97
FT /note="Important for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT CONFLICT 59
FT /note="I -> V (in Ref. 1; CAA57574)"
FT /evidence="ECO:0000305"
FT CONFLICT 153..155
FT /note="DTA -> ETD (in Ref. 1; CAA57574)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="G -> A (in Ref. 1; CAA57574)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="L -> V (in Ref. 1; CAA57574)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="G -> C (in Ref. 1; CAA57574)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 46124 MW; 33EA54A65BA94787 CRC64;
MAFIALGINH KTASVAVRER VAFTPEQMVE ALQQLCRLTT SREAAILSTC NRSELYLEID
HPTADDVLAW LADYHRLTLD ELRACAYVHQ DEDAVRHMMR VASGLDSMVL GEPQILGQMK
SAYAVAREAG TVGPLLGRLF QATFSTAKTV RTDTAIGENP VSVAFAAVSL AKQIFSDLHR
SQALLIGAGE TITLVARHLF EQGVKRIVVA NRTLERASLL AEQFGAHAVL LSEIPEELAN
SDIVISSTAS QLPILGKGAV ERALKQRKHK PMFMVDIAVP RDIEPEVGEL DDVYLYSVDD
LHEVVAENLK SRQGAAQAAE ELVGSGVAEF MQRLRELAAV DVLRAYRQQA ERLRDEELGK
AQRQLANGAD PAEVMAQLAR GLTNKLLHAP SVQMKKMSAE GRIDALALAQ ELFALDEGAP
RH
