HEM1_METKA
ID HEM1_METKA Reviewed; 404 AA.
AC Q9UXR8;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Glutamyl-tRNA reductase;
DE Short=GluTR;
DE EC=1.2.1.70;
GN Name=hemA; OrderedLocusNames=MK0200;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-30, FUNCTION, MASS
RP SPECTROMETRY, CATALYTIC MECHANISM, AND MUTAGENESIS OF CYS-48 AND HIS-84.
RX PubMed=10521455; DOI=10.1074/jbc.274.43.30679;
RA Moser J., Lorenz S., Hubschwerlen C., Rompf A., Jahn D.;
RT "Methanopyrus kandleri glutamyl-tRNA reductase.";
RL J. Biol. Chem. 274:30679-30685(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP SUBUNIT, CATALYTIC MECHANISM, AND DOMAIN.
RX PubMed=11726494; DOI=10.1093/emboj/20.23.6583;
RA Moser J., Schubert W.-D., Beier V., Bringemeier I., Jahn D., Heinz D.W.;
RT "V-shaped structure of glutamyl-tRNA reductase, the first enzyme of tRNA-
RT dependent tetrapyrrole biosynthesis.";
RL EMBO J. 20:6583-6590(2001).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu)
CC to glutamate 1-semialdehyde (GSA). In the absence of NADPH, exhibits
CC substrate esterase activity, leading to the release of glutamate from
CC tRNA. {ECO:0000269|PubMed:10521455}.
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;
CC -!- ACTIVITY REGULATION: Inhibited by heavy metal compounds, Zn(2+), and
CC heme. Also competitively inhibited by glutamycin.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.1.;
CC Temperature dependence:
CC Optimum temperature is 90 degrees Celsius.;
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11726494}.
CC -!- MASS SPECTROMETRY: Mass=45436; Mass_error=30; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10521455};
CC -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
CC {ECO:0000305}.
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DR EMBL; AJ131561; CAB59204.1; -; Genomic_DNA.
DR EMBL; AE009439; AAM01417.1; -; Genomic_DNA.
DR PIR; T45026; T45026.
DR PDB; 1GPJ; X-ray; 1.95 A; A=1-404.
DR PDBsum; 1GPJ; -.
DR AlphaFoldDB; Q9UXR8; -.
DR SMR; Q9UXR8; -.
DR STRING; 190192.MK0200; -.
DR EnsemblBacteria; AAM01417; AAM01417; MK0200.
DR KEGG; mka:MK0200; -.
DR PATRIC; fig|190192.8.peg.201; -.
DR HOGENOM; CLU_035113_0_0_2; -.
DR OMA; FAFKCAA; -.
DR BRENDA; 1.2.1.70; 3274.
DR UniPathway; UPA00251; UER00316.
DR EvolutionaryTrace; Q9UXR8; -.
DR Proteomes; UP000001826; 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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NADP; Oxidoreductase;
KW Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..404
FT /note="Glutamyl-tRNA reductase"
FT /id="PRO_0000114102"
FT ACT_SITE 48
FT /note="Nucleophile"
FT BINDING 47..50
FT /ligand="substrate"
FT BINDING 94
FT /ligand="substrate"
FT BINDING 99..101
FT /ligand="substrate"
FT BINDING 105
FT /ligand="substrate"
FT BINDING 174..179
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000305"
FT SITE 84
FT /note="Important for activity"
FT MUTAGEN 48
FT /note="C->S: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:10521455"
FT MUTAGEN 84
FT /note="H->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:10521455"
FT MUTAGEN 84
FT /note="H->N: 30% of wild-type reductase activity. 15% of
FT wild-type esterase activity."
FT /evidence="ECO:0000269|PubMed:10521455"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:1GPJ"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:1GPJ"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:1GPJ"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:1GPJ"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:1GPJ"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:1GPJ"
FT HELIX 62..67
FT /evidence="ECO:0007829|PDB:1GPJ"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1GPJ"
FT HELIX 78..89
FT /evidence="ECO:0007829|PDB:1GPJ"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:1GPJ"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1GPJ"
FT HELIX 100..116
FT /evidence="ECO:0007829|PDB:1GPJ"
FT HELIX 121..140
FT /evidence="ECO:0007829|PDB:1GPJ"
FT HELIX 150..162
FT /evidence="ECO:0007829|PDB:1GPJ"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:1GPJ"
FT HELIX 177..189
FT /evidence="ECO:0007829|PDB:1GPJ"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:1GPJ"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:1GPJ"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:1GPJ"
FT HELIX 221..226
FT /evidence="ECO:0007829|PDB:1GPJ"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:1GPJ"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:1GPJ"
FT HELIX 244..253
FT /evidence="ECO:0007829|PDB:1GPJ"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:1GPJ"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:1GPJ"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:1GPJ"
FT HELIX 286..301
FT /evidence="ECO:0007829|PDB:1GPJ"
FT HELIX 304..350
FT /evidence="ECO:0007829|PDB:1GPJ"
FT HELIX 365..382
FT /evidence="ECO:0007829|PDB:1GPJ"
FT TURN 386..390
FT /evidence="ECO:0007829|PDB:1GPJ"
FT HELIX 391..402
FT /evidence="ECO:0007829|PDB:1GPJ"
SQ SEQUENCE 404 AA; 45444 MW; 8B6DBE436EA073B3 CRC64;
MEDLVCVGIT HKEAEVEELE KARFESDEAV RDIVESFGLS GCVLLQTCNR VEVYASGARD
RAEELGDLIH DDAWVKRGSE AVRHLFRVAC GLESMMVGEQ EILRQVKKAY DRAARLGTLD
EALKIVFRRA INLGKRAREE TRISEGAVSI GSAAVELAER ELGSLHDKTV LVVGAGEMGK
TVAKSLVDRG VRAVLVANRT YERAVELARD LGGEAVRFDE LVDHLARSDV VVSATAAPHP
VIHVDDVREA LRKRDRRSPI LIIDIANPRD VEEGVENIED VEVRTIDDLR VIARENLERR
RKEIPKVEKL IEEELSTVEE ELEKLKERRL VADVAKSLHE IKDRELERAL RRLKTGDPEN
VLQDFAEAYT KRLINVLTSA IMELPDEYRR AACRALRRAS ELNG
