PUTA_KLEAE
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 25-MAY-2022, entry version 116.
DE RecName: Full=Bifunctional protein PutA;
DE Includes:
DE RecName: Full=Proline dehydrogenase;
DE EC=1.5.5.2;
DE AltName: Full=Proline oxidase;
DE Includes:
DE RecName: Full=Delta-1-pyrroline-5-carboxylate dehydrogenase;
DE Short=P5C dehydrogenase;
DE EC=1.2.1.88;
DE AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase;
GN Name=putA;
OS Klebsiella aerogenes (Enterobacter aerogenes).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=548;
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 of the
CC put operon. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a
CC quinol + H(+); Xref=Rhea:RHEA:23784, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17388, ChEBI:CHEBI:24646, ChEBI:CHEBI:60039,
CC ChEBI:CHEBI:132124; EC=1.5.5.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-
CC glutamate + NADH; Xref=Rhea:RHEA:30235, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58066; EC=1.2.1.88;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
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. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the aldehyde
CC dehydrogenase family. {ECO:0000305}.
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 AlphaFoldDB; O52485; -.
DR SMR; O52485; -.
DR STRING; 548.EAG7_02222; -.
DR PRIDE; O52485; -.
DR UniPathway; UPA00261; UER00373.
DR UniPathway; UPA00261; UER00374.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0004657; F:proline dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1220.10; -; 1.
DR Gene3D; 1.20.5.550; -; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR013321; Arc_rbn_hlx_hlx.
DR InterPro; IPR025703; Bifunct_PutA.
DR InterPro; IPR005933; Delta1-pyrroline-5-COlate_DH-3.
DR InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR InterPro; IPR041349; PRODH.
DR InterPro; IPR024090; PRODH_PutA_dom_I.
DR InterPro; IPR024089; PRODH_PutA_dom_I/II.
DR InterPro; IPR024082; PRODH_PutA_dom_II.
DR InterPro; IPR002872; Proline_DH_dom.
DR InterPro; IPR010985; Ribbon_hlx_hlx.
DR Pfam; PF00171; Aldedh; 1.
DR Pfam; PF01619; Pro_dh; 1.
DR Pfam; PF14850; Pro_dh-DNA_bdg; 1.
DR Pfam; PF18327; PRODH; 1.
DR PIRSF; PIRSF000197; Bifunct_PutA; 1.
DR SUPFAM; SSF47598; SSF47598; 1.
DR SUPFAM; SSF51730; SSF51730; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR SUPFAM; SSF81935; SSF81935; 1.
DR TIGRFAMs; TIGR01238; D1pyr5carbox3; 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
FT /note="Bifunctional protein PutA"
FT /id="PRO_0000056525"
FT REGION 228..574
FT /note="Proline dehydrogenase"
FT REGION 653..1119
FT /note="Aldehyde dehydrogenase"
FT ACT_SITE 883
FT /evidence="ECO:0000250"
FT ACT_SITE 917
FT /evidence="ECO:0000250"
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
