ID   P5CR_THET2              Reviewed;         261 AA.
AC   P54893;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-NOV-2008, entry version 51.
DE   RecName: Full=Pyrroline-5-carboxylate reductase;
DE            Short=P5C reductase;
DE            Short=P5CR;
DE            EC=1.5.1.2;
GN   Name=proC; OrderedLocusNames=TT_C0500;
OS   Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC   Thermus.
OX   NCBI_TaxID=262724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=94168609; PubMed=8123043; DOI=10.1006/bbrc.1994.1244;
RA   Hoshino T., Kosuge T., Hidaka Y., Tabata K., Nakahara T.;
RT   "Molecular cloning and sequence analysis of the proC gene encoding
RT   delta 1-pyrroline-5-carboxylate reductase from an extremely
RT   thermophilic eubacterium Thermus thermophilus.";
RL   Biochem. Biophys. Res. Commun. 199:410-417(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15064768; DOI=10.1038/nbt956;
RA   Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T.,
RA   Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R.,
RA   Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R.,
RA   Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT   "The genome sequence of the extreme thermophile Thermus
RT   thermophilus.";
RL   Nat. Biotechnol. 22:547-553(2004).
CC   -!- CATALYTIC ACTIVITY: L-proline + NAD(P)(+) = 1-pyrroline-5-
CC       carboxylate + NAD(P)H.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
CC       proline from L-glutamate 5-semialdehyde: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase
CC       family.
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DR   EMBL; D25413; BAA05001.1; -; Genomic_DNA.
DR   EMBL; AE017221; AAS80848.1; -; Genomic_DNA.
DR   RefSeq; YP_004475.1; -.
DR   GeneID; 2775949; -.
DR   GenomeReviews; AE017221_GR; TT_C0500.
DR   HOGENOM; P54893; -.
DR   BioCyc; TTHE262724:TT_C0500-MON; -.
DR   LinkHub; P54893; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro.
DR   InterPro; IPR004455; NADP_OxRdtase_F420.
DR   InterPro; IPR000304; P5CR.
DR   PANTHER; PTHR11645; P5CR; 1.
DR   Pfam; PF03807; F420_oxidored; 1.
DR   PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR   TIGRFAMs; TIGR00112; proC; 1.
DR   PROSITE; PS00521; P5CR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; NADP;
KW   Oxidoreductase; Proline biosynthesis.
FT   CHAIN         1    261       Pyrroline-5-carboxylate reductase.
FT                                /FTId=PRO_0000187309.
SQ   SEQUENCE   261 AA;  27819 MW;  3435C3A8F4299B3E CRC64;
     MRLAFVGLGK MGRSILKGAL ERGFLRPEEV GVLGRTPERS RELAEPFGVR PLTRADLGMA
     ERVLIAVQPR DFPALAPEIA HHRLGYISIM AGISTSVLAR RLDNRRVVRA MPNLAVVIGE
     SSTALTALKE AREAEDLAFA RALFATVGDV YEIPEHLFDA FTGMSASAPA YLAVVAEALA
     DAGVKMGMPR ALALRLAADA LAATGELLKG RHPAQVKDEV ASPGGTTIHG LHALEARAVR
     AAFYEAVEAA TRRGHELGES E
//