ID   PROD2_BACNA             Reviewed;         304 AA.
AC   Q8L2I5;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Proline dehydrogenase 2;
DE            Short=PRODH 2;
DE            EC=1.5.5.2;
DE   AltName: Full=Proline oxidase 2;
OS   Bacillus subtilis subsp. natto.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=86029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 1088 / BCRC 14716 / NBRC 13169;
RA   Chang G.-N., Yeh C.-H., Huang T.-C.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate.
CC       {ECO:0000250|UniProtKB:Q8RMG1}.
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
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 dehydrogenase family. {ECO:0000305}.
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DR   EMBL; AF503437; AAM27443.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8L2I5; -.
DR   SMR; Q8L2I5; -.
DR   UniPathway; UPA00261; UER00373.
DR   GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR   GO; GO:0004657; F:proline dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0006562; P:proline catabolic process; ISS:UniProtKB.
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   3: Inferred from homology;
KW   FAD; Flavoprotein; Nucleotide-binding; Oxidoreductase; Proline metabolism.
FT   CHAIN           1..304
FT                   /note="Proline dehydrogenase 2"
FT                   /id="PRO_0000361668"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT   ACT_SITE        181
FT                   /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9RW55"
FT   BINDING         132
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT   BINDING         160
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT   BINDING         184..186
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT   BINDING         223..224
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT   BINDING         285..286
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9RW55"
FT   SITE            272
FT                   /note="Critical for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q72IB8"
SQ   SEQUENCE   304 AA;  35143 MW;  E748D9A7E0FD731B CRC64;
     MVITRDFFLF LSKSGFLNKM ARNWGSRIAA GKIIGGNDFN SSIPTIRQLN SQGLSVTVDH
     LGEFVNSAEV ARERTEECIQ TIATIADQEL NSHVSLKMTS LGLDIDMDLV YENMTKILQT
     AEKHKIMVTI DMEDEVRCQK TLDIFKDFRK KYEHVSTVLQ AYLYRTEKDI DDLDSLNPFL
     RLVKGAYKES EKVAFPEKSD VDENYKKIIR KQLLNGHYTA IATHDDKMID FTKQLAKEHG
     IANDKFEFQM LYGMRSQTQL SLVKEGYNMR VFLPYGEDWY GYFMRRLAER PSNIAFAFKG
     MTKK