ID   HEM1_CAMFF              Reviewed;         422 AA.
AC   A0RNT0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Glutamyl-tRNA reductase;
DE            Short=GluTR;
DE            EC=1.2.1.70;
GN   Name=hemA; OrderedLocusNames=CFF8240_0688;
OS   Campylobacter fetus subsp. fetus (strain 82-40).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fouts D.E., Nelson K.E.;
RT   "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000487; ABK82043.1; -; Genomic_DNA.
DR   RefSeq; YP_891863.1; -.
DR   GeneID; 4539153; -.
DR   GenomeReviews; CP000487_GR; CFF8240_0688.
DR   KEGG; cff:CFF8240_0688; -.
DR   NMPDR; fig|360106.5.peg.651; -.
DR   TIGR; CFF8240_0688; -.
DR   OMA; A0RNT0; GPILNRL.
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 or NADPH 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_dom.
DR   InterPro; IPR018214; pyrrol_synth_GluRdtase_CS.
DR   InterPro; IPR006151; Shikm_DH/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    422       Glutamyl-tRNA reductase.
FT                                /FTId=PRO_1000057571.
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   422 AA;  47142 MW;  9A2B9A3FE3EC3FAB CRC64;
     MHYVSISFTH KNTDIGVREK LSFSDNNRRR EILRLIGAND SIAESMALST CNRVEIFAYV
     LDTQSSIRHI LNSISILTLV PFEALELRAD IYEDQGAIHH LFAVASSLDS LVVGETQIAG
     QLKEAFKFAY DNEDCGVNIS SAMHFAFKCA AEVRALTTIS KNPVSVSSVA VAKAKEIYGN
     IGGMSAVVIG AGEMSRLAAQ HLINAEVNVI IINRDEIKAQ TLAKELGELA SYASFDKLSE
     YINRYRLIFS ATGAPNAIIT NEIIEQKDFH RYFFDIAVPR DIDIEEDEYI HVYAVDDLEE
     IVRTNLALRE EQASIAYSIV GKSTTSFFKW RLSEGSTPAI KALRLKAKDI ACKEIEKAVK
     KGYLKCSDQD EASKLVHQVF KAFLHTPSVR LKEKNSDDIL KALEYLFDIK IQKDENLEGN
     LK
//