ID PUTA_KLEAE STANDARD; PRT; 1312 AA. AC O52485; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE BIFUNCTIONAL PUTA PROTEIN [INCLUDES: PROLINE DEHYDROGENASE DE (EC 1.5.99.8) (PROLINE OXIDASE); DELTA-1-PYRROLINE-5-CARBOXYLATE DE DEHYDROGENASE (EC 1.5.1.12) (P5C DEHYDROGENASE)]. GN PUTA. OS Klebsiella aerogenes. OC Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Klebsiella. OX NCBI_TaxID=28451; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=EM450; RA Surber M.W., Maloy S.; RT "DNA sequence analysis of the putA gene in Klebsiella aerogenes."; RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: OXIDIZES PROLINE TO GLUTAMATE FOR USE AS A CARBON AND CC NITROGEN SOURCE AND ALSO FUNCTION AS A TRANSCRIPTIONAL REPRESSOR CC OF THE PUT OPERON (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: L-PROLINE + ACCEPTOR + H(2)O = (S)-1- CC PYRROLINE-5-CARBOXYLATE + REDUCED ACCEPTOR. CC -!- CATALYTIC ACTIVITY: 1-PYRROLINE-5-CARBOXYLATE + NAD(+) + H(2)O = CC L-GLUTAMATE + NADH. CC -!- COFACTOR: FAD. CC -!- PATHWAY: PROLINE UTILIZATION. CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; TO PROLINE DEHYDROGENASES. CC -!- SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO THE ALDEHYDE CC DEHYDROGENASES FAMILY. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF038838; AAB95478.1; -. DR HSSP; P20000; 1A4Z. DR INTERPRO; IPR002086; -. DR INTERPRO; IPR002872; -. DR PFAM; PF01619; Pro_dh; 1. DR PFAM; PF00171; aldedh; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. KW Multifunctional enzyme; Oxidoreductase; Flavoprotein; FAD; NAD; KW Transcription regulation; Repressor; DNA-binding; Proline metabolism. FT DOMAIN 228 574 PROLINE DEHYDROGENASE. FT DOMAIN 653 1119 ALDEHYDE DEHYDROGENASE. FT ACT_SITE 883 883 BY SIMILARITY. FT ACT_SITE 917 917 BY SIMILARITY. SQ SEQUENCE 1312 AA; 143856 MW; BAF3CA7FC5D18599 CRC64; MGTTTMGVKL DDATRERIKS AASRIDRTPH WLIKQAIFNY LEKLENDETL PELPALLSGA ANESDDASEP TEEPYQPFLE FAEQILPQSV RRAAITAAWR RPETDAVPML LEQARLPQPL GEQAHKLAYQ LAEKLRNQKT ASGRAGMVQS LLQEFSLSSQ EGVALMCLAE ALLRIPDKAT RDALIRDKIS NGNWQSHIGR SPSLFVNAAT WGLLFTGKLV STHNETSLSR SLNRIIGKSG EPLIRKGVDM AMRLMGEQFV TGETIAEALA NARKLEEKGF RYSYDMLGEA ALTAADAQAY MVSYQQAIHA IGKASNGRGI YEGPGISIKL SALHPRYSRA QYDRVMEELY PRLKSLTLLA RQYDIGINID AEEADRLEIS LDLLEKLCFE PELAGWNGIG FVIQAYQKRC PFVIDYLIDL ATRSRRRLMI RLVKGAYWDS EIKRAQMEGL EGYPVYTRKV YTDVSYLACA KKLLAVPNLI YPQFATHNAH TLAAIYQLAG QNYYPGQYEF QCLHGMGEPL YEQVVGKVAD GKLNRPCRIY APVGTHETLL AYLVRRLLEN GANTSFVNRI ADNTLPLDEL VADPVSAVEK LAQQEGQAGL PHPKIPLPRD LYGSGRSNSA GLDLANEHRL ASLSSSLLNS ALHKWQALPM LEQPVAEGEM QPVVNPAEPK DIVGYVREAS DAEVQQALTS AINNAPIWFA TPPQERAAIL ERAAVLMESQ MPTLMGILVR EAGKTFSNAI AEVREAVDFL HYYAGQVRDD FDNETHRPLG PVVCISPWNF PLAIFTGQIA AALAAGNSVL AKPAEQTPLI AAQGVAILLE AGVPPGVIQL LPGRGETVGA ALTSDERVRG VMFTGSTEVA TLLQRNIASR LDPQGRPTPL IAETGGMNAM IVDSSALTEQ VVIDVLASAF DSAGQRCSAL RVLCLQEEVA DHTLTMLRGA MSECRMGNPG RLTTDIGPVI DAEAKENIER HIQAMRAKGR TVYQAVRENS EDAREWRHGT FVPPTLIELD SFDELKKEVF GPVLHVVRYN RNELDKLVEQ INASGYGLTL GVHTRIDETI AQVTGSAKVG NLYVNRNMVG AVVGVQPFGG EGLSGTGPKA GGPLYLYRLL SSRPQDAVGV TFARQDAERP LDAQLKTLLE KPLQALQQWA AGRPELQALC QQYSEQAQSG TQRLLPGPTG ERNTLTLMPR ERVLCVADNE QDALIQLAAV LAVGCEVLWP DSALQRDLAK KLPREVSERI RFAKAEQLPV QAFDAVIYHG DSDQLRELCE QVAARDGAIV SVQGFARGET NLLLERLYIE RSLSVNTAAA GA //