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Database: UniProt/TrEMBL
Entry: D2TMG4_CITRI
LinkDB: D2TMG4_CITRI
Original site: D2TMG4_CITRI 
;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP006580; AHE70556.1; -; Genomic_DNA.
DR   EnsemblBacteria; AHE70556; AHE70556; M942_14165.
DR   Proteomes; UP000018832; Chromosome.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   InterPro; IPR003719; Phenazine_PhzF.
DR   Pfam; PF02567; PhzC-PhzF; 1.
DR   PIRSF; PIRSF016184; PhzC_PhzF; 1.
DR   TIGRFAMs; TIGR00654; PhzF_family; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000018832};
KW   Isomerase {ECO:0000313|EMBL:AHE70556.1}.
FT   ACT_SITE     47     47       {ECO:0000256|PIRSR:PIRSR016184-1}.
SQ   SEQUENCE   262 AA;  28842 MW;  A9E7971835AEB9B0 CRC64;
     MQEIDFYLVD AFSNASFGGN PAAVCPLDAW LPDETLLRMA QQHNQSETAF FVCSKAGIEL
     RWFTTLTEVN LCGHATLAAA YVLFNELNYP DPRIHFDTAS GQLTVSREGD WMTLDFPACP
     TQEETPPPAM LAALGIGHYV EARKGRAWVV VLENRQQVEA LAPNISAMTP GEHKVSVTAR
     GEGDYDFVSR FFSPGVAVWE DPVTGSAHTM LIPYWSEKLG KTAMFARQVS ARGGDLRCEL
     KGSRVLMSGQ ASLYLKGTVF LR
//
ID   W0BPL0_ENTCL            Unreviewed;       418 AA.
AC   W0BPL0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   29-APR-2015, entry version 13.
DE   RecName: Full=Glutamyl-tRNA reductase {ECO:0000256|HAMAP-Rule:MF_00087, ECO:0000256|RuleBase:RU000584};
DE            Short=GluTR {ECO:0000256|HAMAP-Rule:MF_00087};
DE            EC=1.2.1.70 {ECO:0000256|HAMAP-Rule:MF_00087, ECO:0000256|RuleBase:RU000584};
GN   Name=hemA {ECO:0000256|HAMAP-Rule:MF_00087,
GN   ECO:0000313|EMBL:AHE70279.1};
GN   ORFNames=M942_11900 {ECO:0000313|EMBL:AHE70279.1};
OS   Enterobacter cloacae P101.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX   NCBI_TaxID=1354030 {ECO:0000313|EMBL:AHE70279.1, ECO:0000313|Proteomes:UP000018832};
RN   [1] {ECO:0000313|EMBL:AHE70279.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=P101 {ECO:0000313|EMBL:AHE70279.1};
RA   Humann J.L., Drew J.C., Triplett E.W., Main D., Schroeder B.K.;
RT   "Complete genome of the switchgrass endophyte Enterobacter cloacae
RT   P101.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-
CC       tRNA(Glu) to glutamate 1-semialdehyde (GSA). {ECO:0000256|HAMAP-
CC       Rule:MF_00087, ECO:0000256|SAAS:SAAS00030508}.
CC   -!- CATALYTIC ACTIVITY: L-glutamate 1-semialdehyde + NADP(+) +
CC       tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. {ECO:0000256|HAMAP-
CC       Rule:MF_00087, ECO:0000256|RuleBase:RU000584,
CC       ECO:0000256|SAAS:SAAS00041126}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-
CC       IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step
CC       1/2. {ECO:0000256|HAMAP-Rule:MF_00087,
CC       ECO:0000256|RuleBase:RU000584, ECO:0000256|SAAS:SAAS00041161}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00087,
CC       ECO:0000256|SAAS:SAAS00030462}.
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.
CC       {ECO:0000256|HAMAP-Rule:MF_00087}.
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. {ECO:0000256|HAMAP-
CC       Rule:MF_00087}.
CC   -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
CC   
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