ID   HEM1_ARCB4              Reviewed;         432 AA.
AC   A8ERT8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-NOV-2008, entry version 11.
DE   RecName: Full=Glutamyl-tRNA reductase;
DE            Short=GluTR;
DE            EC=1.2.1.70;
GN   Name=hemA; OrderedLocusNames=Abu_0387;
OS   Arcobacter butzleri (strain RM4018).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Arcobacter.
OX   NCBI_TaxID=367737;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18159241; DOI=10.1371/journal.pone.0001358;
RA   Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M.,
RA   Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G.,
RA   Malek J.A., Rogosin A., Stanker L.H., Mandrell R.E.;
RT   "The complete genome sequence and analysis of the
RT   Epsilonproteobacterium Arcobacter butzleri.";
RL   PLoS ONE 2:E1358-E1358(2007).
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; CP000361; ABV66662.1; -; Genomic_DNA.
DR   RefSeq; YP_001489331.1; -.
DR   GeneID; 5624856; -.
DR   GenomeReviews; CP000361_GR; Abu_0387.
DR   KEGG; abu:Abu_0387; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:HAMAP.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004764; F:shikimate 5-dehydrogenase activity; IEA:InterPro.
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    432       Glutamyl-tRNA reductase.
FT                                /FTId=PRO_1000057569.
FT   NP_BIND     190    195       NADP (By similarity).
FT   REGION       50     53       Substrate binding (By similarity).
FT   REGION      115    117       Substrate binding (By similarity).
FT   ACT_SITE     51     51       Nucleophile (By similarity).
FT   BINDING     110    110       Substrate (By similarity).
FT   BINDING     121    121       Substrate (By similarity).
FT   SITE        100    100       Important for activity (By similarity).
SQ   SEQUENCE   432 AA;  48438 MW;  E7753AA710ECAB7B CRC64;
     MSYLVISFSH KNTDIKLREK LAFNSDEDKD RFLKLILEND ITKEAILLST CNRVEIITRS
     LNIKQSSKDI IEKLATYSKV DFDVLYDRAD IYDADGAVHH LFSVASALDS LVIGETQIVG
     QLKDAFRFSQ AKGYCSLNIT RVMHYAFKCA AQVRTATSLG TGSVSVASTA VSKAKDIIGN
     TKDVKALVVG AGEMSELTVK HLIASGFDVT IISRDTKKAQ NLASTFEVHV NVEPYDKLTQ
     LLITTPIMIT ATSAPYPIIT KENAPSSNIN RYWFDIAVPR DIDENISMSN LEIFSVDDLQ
     DIVNENMSLR AEQAKTAYGI VSRMSLEFFE WLKSLEIEPI VKNLYLKGNE IIDKKVKNAI
     KKGFIDSKDE ENIRKLCLTV ITEYLHNPAK QLKDISKNME CDLVVGTVQN MFSLNENSTS
     KNRYKCDHLS KN
//