HEM1_METTM
ID HEM1_METTM Reviewed; 398 AA.
AC P42809; D9PXN3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Glutamyl-tRNA reductase;
DE Short=GluTR;
DE EC=1.2.1.70;
GN Name=hemA; OrderedLocusNames=MTBMA_c13940;
OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79929;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=8831980; DOI=10.1016/0968-0896(96)00098-3;
RA Hungerer C., Weiss D.S., Thauer R.K., Jahn D.;
RT "The hemA gene encoding glutamyl-tRNA reductase from the archaeon
RT Methanobacterium thermoautotrophicum strain Marburg.";
RL Bioorg. Med. Chem. 4:1089-1095(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=20802048; DOI=10.1128/jb.00844-10;
RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA Gottschalk G., Thauer R.K.;
RT "Complete genome sequence of Methanothermobacter marburgensis, a
RT methanoarchaeon model organism.";
RL J. Bacteriol. 192:5850-5851(2010).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu)
CC to glutamate 1-semialdehyde (GSA). {ECO:0000269|PubMed:8831980}.
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 Evidence={ECO:0000269|PubMed:8831980};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:8831980};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius.
CC {ECO:0000269|PubMed:8831980};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
CC {ECO:0000305}.
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DR EMBL; X83691; CAA58664.1; -; Genomic_DNA.
DR EMBL; CP001710; ADL58981.1; -; Genomic_DNA.
DR PIR; S51136; S51136.
DR RefSeq; WP_013296193.1; NC_014408.1.
DR AlphaFoldDB; P42809; -.
DR SMR; P42809; -.
DR STRING; 79929.MTBMA_c13940; -.
DR EnsemblBacteria; ADL58981; ADL58981; MTBMA_c13940.
DR GeneID; 9705103; -.
DR KEGG; mmg:MTBMA_c13940; -.
DR PATRIC; fig|79929.8.peg.1358; -.
DR HOGENOM; CLU_035113_0_0_2; -.
DR OMA; FAFKCAA; -.
DR OrthoDB; 48038at2157; -.
DR UniPathway; UPA00251; UER00316.
DR Proteomes; UP000000345; 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 NADP; Oxidoreductase; Porphyrin biosynthesis.
FT CHAIN 1..398
FT /note="Glutamyl-tRNA reductase"
FT /id="PRO_0000114106"
FT ACT_SITE 46
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 45..48
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 93..95
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 168..173
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 78
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 398 AA; 44536 MW; 7A2C457D9E48CB67 CRC64;
MILNIRLDHK TSDVKTMETA SGRIEEIVGE LEALGAVTEK VPLMTCNRVE YYLHVTGVPP
EFDFNGFTVE KDEDALLHLL RLASGLESMI IGEDQILGQI KAARLQALRE GTCGPLLDMV
FTKAVHVGQT VRRKTKINRG SVSIGSAAVD LAESIHGDLK CKKVLVIGAG KMGTLVARAL
AEKHLKAIMV ANRTYERAYQ LACELGGDAI HFDRLNRALR DADVVISATG SPHYILTRER
VMDAVPPERR SSIVMVDIAN PRDIEESVRE LGVRLFTIDD LRGVAEENRK RREAEAREAE
GIVRAELELL LRAMKHREVE PLLAEIRGRM ESLRQREAGK AIKKIENSKD PERVVEGLTR
SIVDKIFHDI ALKIRDAAER DDREFLRMCS ELFDCDES