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Database: UniProt
Entry: V2PXY1_9BACT
LinkDB: V2PXY1_9BACT
Original site: V2PXY1_9BACT 
ID   V2PXY1_9BACT            Unreviewed;       413 AA.
AC   V2PXY1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   28-FEB-2018, entry version 31.
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=N508_01410 {ECO:0000313|EMBL:ESJ97487.1};
OS   Mucispirillum schaedleri ASF457.
OC   Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae;
OC   Mucispirillum.
OX   NCBI_TaxID=1379858 {ECO:0000313|EMBL:ESJ97487.1, ECO:0000313|Proteomes:UP000017429};
RN   [1] {ECO:0000313|EMBL:ESJ97487.1, ECO:0000313|Proteomes:UP000017429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ASF457 {ECO:0000313|EMBL:ESJ97487.1,
RC   ECO:0000313|Proteomes:UP000017429};
RX   PubMed=24723722;
RA   Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT   "Draft genome sequences of the altered schaedler flora, a defined
RT   bacterial community from gnotobiotic mice.";
RL   Genome Announc. 2:e00287-14(2014).
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:ESJ97487.1}.
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DR   EMBL; AYGZ01000018; ESJ97487.1; -; Genomic_DNA.
DR   RefSeq; WP_023276238.1; NZ_KI530588.1.
DR   EnsemblBacteria; ESJ97487; ESJ97487; N508_01410.
DR   PATRIC; fig|1379858.3.peg.1411; -.
DR   OrthoDB; POG091H00OT; -.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000017429; 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:UP000017429};
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};
KW   Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_00412,
KW   ECO:0000256|SAAS:SAAS00789517};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017429}.
FT   DOMAIN        7    284       Aldedh. {ECO:0000259|Pfam:PF00171}.
FT   DOMAIN      313    375       Aldedh. {ECO:0000259|Pfam:PF00171}.
SQ   SEQUENCE   413 AA;  45550 MW;  464F234A552902B8 CRC64;
     MDLMAQLAKT KKDAHIFAVS PAPKRHAVLS NIALLLNERR EEIKKINKID IINAENMDLS
     SAMIDRLRLT DKEIDSMIKA VNEISMQKEV IGEVISGYTR PNGLKIRKVR VPLGVAGIIY
     ESRPNVTIDS AALCIKSGNG AVLRGGKEAI NSNKILAEII TDSLEKAGFS KDIIYFIQDT
     DRNIIKYMAQ AKGLIDVIIP RGGEGLINFV VDNACIPVIM HDKGVCHVFI DESAEYQQAL
     SIAFNAKVQR PSACNSMETL LIHKNISDKM LPEIAEIFQD VDVDLRGCPE TLKYVDCRPA
     IEEDYYTEYH DMILSIKVVE NIQEAVAHIN KYGSGHSDAI VTTDYNNAEK FLNEVDSAAV
     YVNASTRFTD GGEFGLGAEI GISTQKLHVR GPMGAEDLTT TKYLIYGSGQ LRG
//
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