PROA_THEMA
ID PROA_THEMA Reviewed; 415 AA.
AC Q9WYC9;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Gamma-glutamyl phosphate reductase {ECO:0000255|HAMAP-Rule:MF_00412};
DE Short=GPR {ECO:0000255|HAMAP-Rule:MF_00412};
DE EC=1.2.1.41 {ECO:0000255|HAMAP-Rule:MF_00412};
DE AltName: Full=Glutamate-5-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412};
DE AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412};
DE Short=GSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412};
GN Name=proA {ECO:0000255|HAMAP-Rule:MF_00412}; OrderedLocusNames=TM_0293;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of L-glutamate 5-
CC phosphate into L-glutamate 5-semialdehyde and phosphate. The product
CC spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
CC {ECO:0000255|HAMAP-Rule:MF_00412}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + L-
CC glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:19541,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58066, ChEBI:CHEBI:58274, ChEBI:CHEBI:58349; EC=1.2.1.41;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00412};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-glutamate: step 2/2. {ECO:0000255|HAMAP-
CC Rule:MF_00412}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00412}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase family.
CC {ECO:0000255|HAMAP-Rule:MF_00412}.
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DR EMBL; AE000512; AAD35381.1; -; Genomic_DNA.
DR PIR; E72394; E72394.
DR RefSeq; NP_228105.1; NC_000853.1.
DR RefSeq; WP_004083010.1; NZ_CP011107.1.
DR PDB; 1O20; X-ray; 2.00 A; A=1-415.
DR PDBsum; 1O20; -.
DR AlphaFoldDB; Q9WYC9; -.
DR SMR; Q9WYC9; -.
DR STRING; 243274.THEMA_03260; -.
DR EnsemblBacteria; AAD35381; AAD35381; TM_0293.
DR KEGG; tma:TM0293; -.
DR eggNOG; COG0014; Bacteria.
DR InParanoid; Q9WYC9; -.
DR OMA; PGVCNAM; -.
DR OrthoDB; 223669at2; -.
DR BRENDA; 1.2.1.41; 6331.
DR UniPathway; UPA00098; UER00360.
DR EvolutionaryTrace; Q9WYC9; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IBA:GO_Central.
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; -; 1.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm; NADP; Oxidoreductase;
KW Proline biosynthesis; Reference proteome.
FT CHAIN 1..415
FT /note="Gamma-glutamyl phosphate reductase"
FT /id="PRO_0000189802"
FT HELIX 3..18
FT /evidence="ECO:0007829|PDB:1O20"
FT HELIX 23..39
FT /evidence="ECO:0007829|PDB:1O20"
FT HELIX 41..57
FT /evidence="ECO:0007829|PDB:1O20"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:1O20"
FT HELIX 72..87
FT /evidence="ECO:0007829|PDB:1O20"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:1O20"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:1O20"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:1O20"
FT HELIX 126..137
FT /evidence="ECO:0007829|PDB:1O20"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:1O20"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1O20"
FT HELIX 151..165
FT /evidence="ECO:0007829|PDB:1O20"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:1O20"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:1O20"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:1O20"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:1O20"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:1O20"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:1O20"
FT HELIX 205..214
FT /evidence="ECO:0007829|PDB:1O20"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:1O20"
FT HELIX 237..249
FT /evidence="ECO:0007829|PDB:1O20"
FT STRAND 257..264
FT /evidence="ECO:0007829|PDB:1O20"
FT HELIX 265..281
FT /evidence="ECO:0007829|PDB:1O20"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:1O20"
FT HELIX 290..295
FT /evidence="ECO:0007829|PDB:1O20"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:1O20"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:1O20"
FT STRAND 313..323
FT /evidence="ECO:0007829|PDB:1O20"
FT HELIX 324..334
FT /evidence="ECO:0007829|PDB:1O20"
FT STRAND 337..343
FT /evidence="ECO:0007829|PDB:1O20"
FT HELIX 347..356
FT /evidence="ECO:0007829|PDB:1O20"
FT STRAND 359..366
FT /evidence="ECO:0007829|PDB:1O20"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:1O20"
FT TURN 373..377
FT /evidence="ECO:0007829|PDB:1O20"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:1O20"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:1O20"
FT STRAND 401..408
FT /evidence="ECO:0007829|PDB:1O20"
SQ SEQUENCE 415 AA; 46404 MW; 95BD703ACBE6F2AA CRC64;
MDELLEKAKK VREAWDVLRN ATTREKNKAI KKIAEKLDER RKEILEANRI DVEKARERGV
KESLVDRLAL NDKRIDEMIK ACETVIGLKD PVGEVIDSWV REDGLRIARV RVPIGPIGII
YESRPNVTVE TTILALKSGN TILLRGGSDA LNSNKAIVSA IREALKETEI PESSVEFIEN
TDRSLVLEMI RLREYLSLVI PRGGYGLISF VRDNATVPVL ETGVGNCHIF VDESADLKKA
VPVIINAKTQ RPGTCNAAEK LLVHEKIAKE FLPVIVEELR KHGVEVRGCE KTREIVPDVV
PATEDDWPTE YLDLIIAIKV VKNVDEAIEH IKKYSTGHSE SILTENYSNA KKFVSEIDAA
AVYVNASTRF TDGGQFGFGA EIGISTQRFH ARGPVGLREL TTYKFVVLGE YHVRE
