ID   HEM1_ARCFU              Reviewed;         437 AA.
AC   O28304;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   04-NOV-2008, entry version 61.
DE   RecName: Full=Glutamyl-tRNA reductase;
DE            Short=GluTR;
DE            EC=1.2.1.70;
GN   Name=hemA; OrderedLocusNames=AF_1975;
OS   Archaeoglobus fulgidus.
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
OC   Archaeoglobaceae; Archaeoglobus.
OX   NCBI_TaxID=2234;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
RX   MEDLINE=98049343; PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E.,
RA   Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D.,
RA   Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C.,
RA   Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R.,
RA   Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J.,
RA   Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A.,
RA   Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A.,
RA   Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P.,
RA   Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C.,
RA   Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O.,
RA   Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-
RT   reducing archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-
CC       tRNA(Glu) to glutamate 1-semialdehyde (GSA) (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-glutamate 1-semialdehyde + NADP(+) +
CC       tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.
CC   -!- PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-
CC       aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
CC   -!- SUBUNIT: Homodimer (By similarity).
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 (By
CC       similarity).
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 (By similarity).
CC   -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
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DR   EMBL; AE000782; AAB89281.1; -; Genomic_DNA.
DR   PIR; F69496; F69496.
DR   RefSeq; NP_070799.1; -.
DR   HSSP; Q9UXR8; 1GPJ.
DR   GeneID; 1485197; -.
DR   GenomeReviews; AE000782_GR; AF_1975.
DR   KEGG; afu:AF1975; -.
DR   NMPDR; fig|224325.1.peg.1960; -.
DR   TIGR; AF_1975; -.
DR   HOGENOM; O28304; -.
DR   BioCyc; AFUL224325:AF_1975-MON; -.
DR   GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006779; P:porphyrin biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00087; -; 1.
DR   InterPro; IPR000343; 4pyrrol_synth_GluRdtase.
DR   InterPro; IPR015896; 4pyrrol_synth_GluRdtase_C.
DR   InterPro; IPR015895; 4pyrrol_synth_GluRdtase_N.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   InterPro; IPR006151; Shikm_DHase/Glu-tRNA_Rdtase.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
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   TIGRFAMs; TIGR01035; hemA; 1.
DR   PROSITE; PS00747; GLUTR; 1.
PE   3: Inferred from homology;
KW   Complete proteome; NADP; Oxidoreductase; Porphyrin biosynthesis.
FT   CHAIN         1    437       Glutamyl-tRNA reductase.
FT                                /FTId=PRO_0000114098.
FT   NP_BIND     177    182       NADP (By similarity).
FT   REGION       46     49       Substrate binding (By similarity).
FT   REGION      102    104       Substrate binding (By similarity).
FT   ACT_SITE     47     47       Nucleophile (By similarity).
FT   BINDING      97     97       Substrate (By similarity).
FT   BINDING     108    108       Substrate (By similarity).
FT   SITE         87     87       Important for activity (By similarity).
SQ   SEQUENCE   437 AA;  48442 MW;  DD0A999D55790CD6 CRC64;
     MEIGCITISH KNAKVEEIEK IWLTVKPRLE DVISKCSFSE YAYIFTCNRF EIYLVGENLK
     SCLQDIAEEL GITGKAEIFV GESCLRHLLR VASGIESMIV GEEQILGQVR QCFNLCREGG
     QAGEVLERVF GKAVQVGRRV RRETAISKGS VSIGSAAVEV AERVLGTLKG KKALLVGAGE
     MGTLVAKAIA GKEVEAVLIA NRTYEKAEEL AKRIGGVAVK FDKLVDYLKV CDVVISATSA
     PHAVITRGDV ERAMRERSQK LLIIDIALPR DVDESVAQLD GVELLTIDDL RRISEENLAR
     RREEIAKVEG IIEEELEQLK LLLKDISARD AIAAMYSLAE RFVGEEVEEL YAKLNARYGV
     SEDVKEILND FANSLIKKFL REPTVRLREA ARKDEFHVIE SIKYVFGDGN GRVSEGKDAK
     VEEGKPEVDV QRSKAES
//