ID   PROD1_BACNA             Reviewed;         302 AA.
AC   Q8RMG1;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Proline dehydrogenase 1;
DE            Short=PRODH 1;
DE            EC=1.5.5.2;
DE   AltName: Full=Proline oxidase 1;
GN   Name=fadM; Synonyms=yusM;
OS   Bacillus subtilis subsp. natto.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=86029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=DSM 1088 / BCRC 14716 / NBRC 13169;
RX   PubMed=17536821; DOI=10.1021/jf0700576;
RA   Huang T.-C., Huang Y.-W., Hung H.-J., Ho C.-T., Wu M.-L.;
RT   "Delta1-pyrroline-5-carboxylic acid formed by proline dehydrogenase from
RT   the Bacillus subtilis ssp. natto expressed in Escherichia coli as a
RT   precursor for 2-acetyl-1-pyrroline.";
RL   J. Agric. Food Chem. 55:5097-5102(2007).
CC   -!- FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate.
CC       {ECO:0000269|PubMed:17536821}.
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         Evidence={ECO:0000269|PubMed:17536821};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5-8. {ECO:0000269|PubMed:17536821};
CC       Temperature dependence:
CC         Optimum temperature is 25 degrees Celsius. Loses 70% of activity upon
CC         activation at 45 degrees Celsius for 15 minutes.
CC         {ECO:0000269|PubMed:17536821};
CC   -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC       glutamate; L-glutamate from L-proline: step 1/2.
CC   -!- SIMILARITY: Belongs to the proline oxidase 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; AF497244; AAM16152.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8RMG1; -.
DR   SMR; Q8RMG1; -.
DR   BRENDA; 1.5.99.B2; 658.
DR   UniPathway; UPA00261; UER00373.
DR   GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR   GO; GO:0004657; F:proline dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR   InterPro; IPR008219; PRODH_bac_arc.
DR   InterPro; IPR002872; Proline_DH_dom.
DR   InterPro; IPR015659; Proline_oxidase.
DR   PANTHER; PTHR13914; PTHR13914; 2.
DR   Pfam; PF01619; Pro_dh; 1.
DR   PIRSF; PIRSF000196; Pro_dehydrog; 1.
DR   SUPFAM; SSF51730; SSF51730; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Nucleotide-binding; Oxidoreductase; Proline metabolism.
FT   CHAIN           1..302
FT                   /note="Proline dehydrogenase 1"
FT                   /id="PRO_0000361667"
FT   ACT_SITE        129
FT                   /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT   ACT_SITE        179
FT                   /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9RW55"
FT   BINDING         130
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT   BINDING         158
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT   BINDING         182..184
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT   BINDING         221..222
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT   BINDING         283..284
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9RW55"
FT   SITE            270
FT                   /note="Critical for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q72IB8"
SQ   SEQUENCE   302 AA;  34510 MW;  B39468A37A1C873E CRC64;
     MLRHVFLFLS QNKTLTKFAK AYGTRLGARR FVAGDTIESA VKTVKRLNRS GLCATIDYLG
     EYAASEKEAN QVAEECKKAI QAIAEHQLDS ELSLKLTSIG LDLSEELALT HLRAILSVAK
     QYDVAVTIDM EDYSHYEQTL SIYRQCKQEF EKLGTVIQAY LYRAAEDIKK MRDLKPNLRL
     VKGAYKESAA VAFPDKRGTD LHFQSLIKLQ LLSGNYTAVA THDDDIIKFT KQLVAEHRIP
     ASQFEFQMLY GIRPERQKEL AKEGYRMRVY VPYGTDWFSY FMRRIAERPA NAAFVLKGIL
     KK