GenomeNet

Database: UniProt
Entry: G6ERV1_STRTR
LinkDB: G6ERV1_STRTR
Original site: G6ERV1_STRTR 
ID   G6ERV1_STRTR            Unreviewed;       416 AA.
AC   G6ERV1;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   28-FEB-2018, entry version 37.
DE   RecName: Full=Gamma-glutamyl phosphate reductase {ECO:0000256|HAMAP-Rule:MF_00412};
DE            Short=GPR {ECO:0000256|HAMAP-Rule:MF_00412};
DE            EC=1.2.1.41 {ECO:0000256|HAMAP-Rule:MF_00412};
DE   AltName: Full=Glutamate-5-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00412};
DE   AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00412};
DE            Short=GSA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00412};
GN   Name=proA {ECO:0000256|HAMAP-Rule:MF_00412};
GN   ORFNames=STHE1630_01849 {ECO:0000313|EMBL:EHE87052.1};
OS   Streptococcus thermophilus CNCM I-1630.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1042404 {ECO:0000313|EMBL:EHE87052.1, ECO:0000313|Proteomes:UP000004150};
RN   [1] {ECO:0000313|EMBL:EHE87052.1, ECO:0000313|Proteomes:UP000004150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNCM I-1630 {ECO:0000313|EMBL:EHE87052.1,
RC   ECO:0000313|Proteomes:UP000004150};
RX   PubMed=22030749;
RA   McNulty N.P., Yatsunenko T., Hsiao A., Faith J.J., Muegge B.D.,
RA   Goodman A.L., Henrissat B., Oozeer R., Cools-Portier S., Gobert G.,
RA   Chervaux C., Knights D., Lozupone C.A., Knight R., Duncan A.E.,
RA   Bain J.R., Muehlbauer M.J., Newgard C.B., Heath A.C., Gordon J.I.;
RT   "The impact of a consortium of fermented milk strains on the gut
RT   microbiome of gnotobiotic mice and monozygotic twins.";
RL   Sci. Transl. Med. 3:106RA106-106RA106(2011).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of L-glutamate
CC       5-phosphate into L-glutamate 5-semialdehyde and phosphate. The
CC       product spontaneously undergoes cyclization to form 1-pyrroline-5-
CC       carboxylate. {ECO:0000256|HAMAP-Rule:MF_00412,
CC       ECO:0000256|SAAS:SAAS00806217}.
CC   -!- CATALYTIC ACTIVITY: L-glutamate 5-semialdehyde + phosphate +
CC       NADP(+) = L-glutamyl 5-phosphate + NADPH. {ECO:0000256|HAMAP-
CC       Rule:MF_00412, ECO:0000256|SAAS:SAAS00789550}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
CC       glutamate 5-semialdehyde from L-glutamate: step 2/2.
CC       {ECO:0000256|HAMAP-Rule:MF_00412, ECO:0000256|SAAS:SAAS00789481}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00412,
CC       ECO:0000256|SAAS:SAAS00806220}.
CC   -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00412,
CC       ECO:0000256|SAAS:SAAS00750599}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EHE87052.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AGFN01000374; EHE87052.1; -; Genomic_DNA.
DR   EnsemblBacteria; EHE87052; EHE87052; STHE1630_01849.
DR   PATRIC; fig|1042404.3.peg.2146; -.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000004150; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07079; ALDH_F18-19_ProA-GPR; 1.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 2.
DR   HAMAP; MF_00412; ProA; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR020593; G-glutamylP_reductase_CS.
DR   InterPro; IPR012134; Glu-5-SA_DH.
DR   InterPro; IPR000965; GPR_dom.
DR   Pfam; PF00171; Aldedh; 2.
DR   PIRSF; PIRSF000151; GPR; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   TIGRFAMs; TIGR00407; proA; 1.
DR   PROSITE; PS01223; PROA; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00412,
KW   ECO:0000256|SAAS:SAAS00789523};
KW   Complete proteome {ECO:0000313|Proteomes:UP000004150};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00412,
KW   ECO:0000256|SAAS:SAAS00806221};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00412, ECO:0000256|SAAS:SAAS00789553};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00412,
KW   ECO:0000256|SAAS:SAAS00789546, ECO:0000313|EMBL:EHE87052.1};
KW   Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_00412,
KW   ECO:0000256|SAAS:SAAS00789517};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004150}.
FT   DOMAIN        4    283       Aldedh. {ECO:0000259|Pfam:PF00171}.
FT   DOMAIN      316    378       Aldedh. {ECO:0000259|Pfam:PF00171}.
SQ   SEQUENCE   416 AA;  45354 MW;  8F3D23FDC89F7778 CRC64;
     MTYVDTLGQQ AKVASRQIAK LSTAAKNDLL NQVAKALVAE SDYIITENAK DMANASENGI
     SKIMQDRLLL TEDRIAGIAE GVRQVADLQD PIGQVVRGYT NLDGLKIVQK RVPIGVIAMI
     FESRPNVSID AFSLAFKTNN AIILRGGRDA INSNKALVTV ARKALKNAGI TADAVQFVED
     TSHEVAEELM VATKYVDLLI PRGGARLIQT VKEKAKVPVI ETGVGNCHIY VDKYANLDMA
     TQIVINAKTQ RPSVCNAAES LVVHADIVEE FLPNLEKAIS KIQSVEFRAD ERALKLMEKA
     VPASPEDFAT EFLDYIMSVK VVDSLDEAIN WINTYTTSHS EAIVTQDICR AEQFQDDVDA
     AAVYVNASTR FTDGFVFGLG AEIGISTQKM HARGPMGLEA LTSTKFYING QGQIRE
//
DBGET integrated database retrieval system