ID PUTA_KLEAE Reviewed; 1312 AA. AC O52485; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 19-JAN-2010, entry version 59. DE RecName: Full=Bifunctional protein putA; DE Includes: DE RecName: Full=Proline dehydrogenase; DE EC=1.5.99.8; DE AltName: Full=Proline oxidase; DE Includes: DE RecName: Full=Delta-1-pyrroline-5-carboxylate dehydrogenase; DE Short=P5C dehydrogenase; DE EC=1.5.1.12; GN Name=putA; OS Klebsiella aerogenes. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=28451; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 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 = (S)-1-pyrroline-5- CC carboxylate + reduced acceptor. CC -!- CATALYTIC ACTIVITY: (S)-1-pyrroline-5-carboxylate + NAD(P)(+) + 2 CC H(2)O = L-glutamate + NAD(P)H. CC -!- COFACTOR: FAD. CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L- CC glutamate; L-glutamate from L-proline: step 1/2. CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L- CC glutamate; L-glutamate from L-proline: step 2/2. CC -!- SIMILARITY: In the N-terminal section; belongs to the proline CC dehydrogenase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the aldehyde CC dehydrogenase 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; -; Genomic_DNA. DR SMR; O52485; 2-49, 87-612, 655-1113. DR BRENDA; 1.5.1.12; 366. DR BRENDA; 1.5.99.8; 366. DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase act...; IEA:EC. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0004657; F:proline dehydrogenase activity; IEA:EC. DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro. DR GO; GO:0006562; P:proline catabolic process; IEA:InterPro. DR GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW. DR GO; GO:0006350; P:transcription; IEA:UniProtKB-KW. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH. DR InterPro; IPR005933; d-1-pyrroline-5-COlate_DH-3. DR InterPro; IPR002872; Proline_DH. DR Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1. DR PANTHER; PTHR11699; Aldehyde_dehyd; 1. DR Pfam; PF00171; Aldedh; 1. DR Pfam; PF01619; Pro_dh; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 3: Inferred from homology; KW DNA-binding; FAD; Flavoprotein; Multifunctional enzyme; NAD; KW Oxidoreductase; Proline metabolism; Repressor; Transcription; KW Transcription regulation. FT CHAIN 1 1312 Bifunctional protein putA. FT /FTId=PRO_0000056525. FT REGION 228 574 Proline dehydrogenase. FT REGION 653 1119 Aldehyde dehydrogenase. FT ACT_SITE 883 883 By similarity. FT ACT_SITE 917 917 By similarity. SQ SEQUENCE 1312 AA; 143857 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 //