ID   PUTA_KLEPN              Reviewed;          26 AA.
AC   P23725;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 79.
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;
DE   Flags: Fragment;
GN   Name=putA;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1987164; DOI=10.1128/jb.173.2.783-790.1991;
RA   Chen L.M., Maloy S.;
RT   "Regulation of proline utilization in enteric bacteria: cloning and
RT   characterization of the Klebsiella put control region.";
RL   J. Bacteriol. 173:783-790(1991).
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.
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   -!- INDUCTION: By proline, autorepression and catabolite repression, and is
CC       potentially nitrogen controlled.
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DR   EMBL; M63160; AAA25139.1; -; Genomic_DNA.
DR   AlphaFoldDB; P23725; -.
DR   SMR; P23725; -.
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:0004657; F:proline dehydrogenase activity; IEA:RHEA.
DR   GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway.
PE   2: Evidence at transcript level;
KW   DNA-binding; FAD; Flavoprotein; Multifunctional enzyme; NAD;
KW   Oxidoreductase; Proline metabolism; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..>26
FT                   /note="Bifunctional protein PutA"
FT                   /id="PRO_0000056526"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         26
SQ   SEQUENCE   26 AA;  2824 MW;  BB332D0DE504CE19 CRC64;
     MGTTTMGVKL DDATRERIKS AASRID