Entry sw:HEM1_SHIFL

ID   HEM1_SHIFL              Reviewed;         418 AA.
AC   Q83RP1; Q7UCS4;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 2.
DT   02-NOV-2016, entry version 103.
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};
GN   OrderedLocusNames=SF1213, S1297;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H.,
RA   Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J.,
RA   Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S.,
RA   Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y.,
RA   Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/IAI.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W.,
RA   Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A.,
RA   Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S.,
RA   Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella
RT   flexneri serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-
CC       tRNA(Glu) to glutamate 1-semialdehyde (GSA). {ECO:0000255|HAMAP-
CC       Rule:MF_00087}.
CC   -!- CATALYTIC ACTIVITY: L-glutamate 1-semialdehyde + NADP(+) +
CC       tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. {ECO:0000255|HAMAP-
CC       Rule:MF_00087}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-
CC       IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step
CC       1/2. {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
CC       with each monomer consisting of three distinct domains arranged
CC       along a curved 'spinal' alpha-helix. The N-terminal catalytic
CC       domain specifically recognizes the glutamate moiety of the
CC       substrate. The second domain is the NADPH-binding domain, and the
CC       third C-terminal domain is responsible for dimerization.
CC       {ECO:0000255|HAMAP-Rule:MF_00087}.
CC   -!- MISCELLANEOUS: During catalysis, the active site Cys acts as a
CC       nucleophile attacking the alpha-carbonyl group of tRNA-bound
CC       glutamate with the formation of a thioester intermediate between
CC       enzyme and glutamate, and the concomitant release of tRNA(Glu).
CC       The thioester intermediate is finally reduced by direct hydride
CC       transfer from NADPH, to form the product GSA. {ECO:0000255|HAMAP-
CC       Rule:MF_00087}.
CC   -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00087}.
DR   EMBL; AE005674; AAN42826.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16712.1; -; Genomic_DNA.
DR   RefSeq; NP_707119.2; NC_004337.2.
DR   RefSeq; WP_005049668.1; NZ_LVJC01000023.1.
DR   ProteinModelPortal; Q83RP1; -.
DR   STRING; 198214.SF1213; -.
DR   PaxDb; Q83RP1; -.
DR   EnsemblBacteria; AAN42826; AAN42826; SF1213.
DR   EnsemblBacteria; AAP16712; AAP16712; S1297.
DR   GeneID; 1024143; -.
DR   KEGG; sfl:SF1213; -.
DR   KEGG; sfx:S1297; -.
DR   PATRIC; 18703832; VBIShiFle31049_1421.
DR   eggNOG; ENOG4105C7E; Bacteria.
DR   eggNOG; COG0373; LUCA.
DR   HOGENOM; HOG000109650; -.
DR   KO; K02492; -.
DR   OMA; NHCPNIK; -.
DR   UniPathway; UPA00251; UER00316.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.720; -; 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; IPR016040; NAD(P)-bd_dom.
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   Complete proteome; NADP; Oxidoreductase; Porphyrin biosynthesis.
FT   CHAIN         1    418       Glutamyl-tRNA reductase.
FT                                /FTId=PRO_0000114066.
FT   NP_BIND     189    194       NADP. {ECO:0000255|HAMAP-Rule:MF_00087}.
FT   REGION       49     52       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00087}.
FT   REGION      114    116       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00087}.
FT   ACT_SITE     50     50       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00087}.
FT   BINDING     109    109       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00087}.
FT   BINDING     120    120       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00087}.
FT   SITE         99     99       Important for activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00087}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         6    156       ipfam:GlutR_N [T]
FT   MYHIT        99    122       ipat:GLUTR [T]
FT   MYHIT         2    418       ihamap:Glu_tRNA_reductase [T]
FT   MYHIT       172    306       ipfam:Shikimate_DH [T]
FT   MYHIT       320    416       ipfam:GlutR_dimer [T]
SQ   SEQUENCE   418 AA;  46358 MW;  E756E4F2928C535A CRC64;
     MTLLALGINH KTAPVSLRER VSFSPDKLDQ ALDSLLAQPM VQGGVVLSTC NRTELYLSVE
     EQDNLQEALI RWLCDYHNLN EEDLRKSLYW HQDNDAVSHL MRVASGLDSL VLGEPQILGQ
     VKKAFVDSQK GHMKASELER MFQKSFSVAK RVRTETDIGA SAVSVAFAAC TLARQIFESL
     STVTVLLVGA GETIELVARH LREHKVQKMI IANRTRERAQ ILADEVGAEV IALSEIDERL
     READIIISST ASPLPIIGKG MVERALKSRR NQPMLLVDIA VPRDVEPEVG KLANAYLYSV
     DDLQSIISHN LAQRKAAAVE AETIVAQETS EFMAWLRAQS ASETIREYRS QAEHVRDELT
     AKALAALEQG GDAQAIMQDL AWKLTNRLIH APTKSLQQAA RDGDNERLNI LRDSLGLE
//