ID P5CR_TREPA Reviewed; 263 AA. AC P27771; O83775; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 25-NOV-2008, entry version 63. DE RecName: Full=Pyrroline-5-carboxylate reductase; DE Short=P5C reductase; DE Short=P5CR; DE EC=1.5.1.2; GN Name=proC; OrderedLocusNames=TP_0797; OS Treponema pallidum. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=160; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Nichols; RX MEDLINE=90264287; PubMed=2188947; RA Gherardini F.C., Hobbs M.M., Stamm L.V., Bassford P.J. Jr.; RT "Complementation of an Escherichia coli proC mutation by a gene cloned RT from Treponema pallidum."; RL J. Bacteriol. 172:2996-3002(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nichols; RX MEDLINE=98332770; PubMed=9665876; DOI=10.1126/science.281.5375.375; RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G., RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A., RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D., RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., RA Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D., RA Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M., RA Weidman J.F., Smith H.O., Venter J.C.; RT "Complete genome sequence of Treponema pallidum, the syphilis RT spirochete."; RL Science 281:375-388(1998). 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 (By similarity). CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M73825; AAA27478.1; -; Genomic_DNA. DR EMBL; AE000520; AAC65760.1; -; Genomic_DNA. DR PIR; D71281; D71281. DR RefSeq; NP_219234.1; -. DR IntAct; P27771; -. DR GeneID; 2610812; -. DR GenomeReviews; AE000520_GR; TP_0797. DR KEGG; tpa:TP0797; -. DR NMPDR; fig|243276.1.peg.793; -. DR TIGR; TP_0797; -. DR HOGENOM; P27771; -. DR BioCyc; TPAL243276:TP_0797-MON; -. 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; IPR016040; NAD(P)-bd. DR InterPro; IPR004455; NADP_OxRdtase_F420. DR InterPro; IPR000304; P5CR. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. 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 1 263 Pyrroline-5-carboxylate reductase. FT /FTId=PRO_0000187310. FT CONFLICT 1 65 MNVGFLGFGAMGRALAEGLVHAGALQAAQVYACALNQEKLR FT AQCTSLGIGACASVQELVQKSEWI -> MTWDFWVLEQWDG FT RWQKGWCTQERCKRSSVRLCVKSGKVACAVYIFGHRCLRVS FT SGTGTEKVNGF (in Ref. 1). FT CONFLICT 77 93 VLRDRQSFQGKVLISLA -> GTARSPIFQESAISC (in FT Ref. 1; AAA27478). FT CONFLICT 256 260 VRAAL -> CRWLS (in Ref. 1). SQ SEQUENCE 263 AA; 27645 MW; ED4AD7C54BAF9D61 CRC64; MNVGFLGFGA MGRALAEGLV HAGALQAAQV YACALNQEKL RAQCTSLGIG ACASVQELVQ KSEWIFLAVK PSQISTVLRD RQSFQGKVLI SLAAGMSCAA YEALFAADPH QGIRHLSLLP NLPCQVARGV IIAEARHTLH HDEHAALLAV LRTVAQVEVV DTAYFAIAGV IAGCAPAFAA QFIEALADAG VRYGLARDQA YRLAAHMLEG TAALIQHSGV HPAQLKDRVC SPAGSTIRGV LALEEQGLRR AVIHAVRAAL SSS //