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Database: UniProt
Entry: A7GYU7
LinkDB: A7GYU7
Original site: A7GYU7 
ID   HEM1_CAMC5              Reviewed;         428 AA.
AC   A7GYU7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-SEP-2014, entry version 60.
DE   RecName: Full=Glutamyl-tRNA reductase;
DE            Short=GluTR;
DE            EC=1.2.1.70;
GN   Name=hemA; OrderedLocusNames=Ccur92_10850; ORFNames=CCV52592_0764;
OS   Campylobacter curvus (strain 525.92).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360105;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=525.92;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT   "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT   feces.";
RL   Submitted (JUL-2007) 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-containing compound metabolism; protoporphyrin-
CC       IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step
CC       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; CP000767; EAT99944.1; -; Genomic_DNA.
DR   RefSeq; YP_001408389.1; NC_009715.1.
DR   ProteinModelPortal; A7GYU7; -.
DR   STRING; 360105.CCV52592_0764; -.
DR   EnsemblBacteria; EAT99944; EAT99944; CCV52592_0764.
DR   GeneID; 5407303; -.
DR   KEGG; ccv:CCV52592_0764; -.
DR   PATRIC; 20032676; VBICamCur47627_1145.
DR   eggNOG; COG0373; -.
DR   HOGENOM; HOG000109651; -.
DR   KO; K02492; -.
DR   OMA; LAHKLTN; -.
DR   OrthoDB; EOG6MWNBM; -.
DR   BioCyc; CCUR360105:GJ9P-1184-MONOMER; -.
DR   UniPathway; UPA00251; UER00316.
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; IPR018073; Prot_inh_cystat_CS.
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; 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    428       Glutamyl-tRNA reductase.
FT                                /FTId=PRO_0000335020.
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   428 AA;  47977 MW;  6B0B44CB6ABDABD0 CRC64;
     MHYLNISFTY KNTDISVREK LAFDSDEKKD QILRLLKSSK NIIECMVLST CNRVEVLAYT
     NDIKSAMTHI IRCLTVYSGV FEDELFERAD IYEDSGAVHH LFAVASSLDS LVVGETQIVG
     QLKNAFKFAF DNASSGEHIS RLVHYACKCA ARVRNETQIS KNPISVSSVA VAKAKEIFGT
     LENKTAVVIG AGEMGELAAK HLITSGANVI IINRSSDHVE ELVENLGDKA SWDSILKLKE
     YINKYDLIFS STSAPHAIIT GELIEPQEFR RYFFDIAVPR DIDLVNTDKI SVYSVDSLEE
     MVRRNLALRE EQAQTAYSIV GQSTNEFLKF LKDNISIPLI KTIRKKAEIC AEAELEKALK
     KGYLKHSDKE EAAKLIHQVF KAFLHSPTIN LKSLASKNDA EQIAGGIKFL FDIKEENLEN
     LTKDIDEI
//
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