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 29-MAY-2013, entry version 53.
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; GPILNRL; -.
DR ProtClustDB; PRK00045; -.
DR BioCyc; CCUR360105:GJ9P-1184-MONOMER; -.
DR UniPathway; UPA00251; UER00316.
DR GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:HAMAP.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:HAMAP.
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; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR018073; Prot_inh_cystat_CS.
DR InterPro; IPR018214; Pyrrol_synth_GluRdtase_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; 4pyrrol_synth_GluRdtase_C; 1.
DR SUPFAM; SSF69742; GlutR; 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
//
