ID A0A1T5H3S4_9BACI Unreviewed; 324 AA.
AC A0A1T5H3S4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=proline dehydrogenase {ECO:0000256|ARBA:ARBA00012695};
DE EC=1.5.5.2 {ECO:0000256|ARBA:ARBA00012695};
GN ORFNames=SAMN06295926_12954 {ECO:0000313|EMBL:SKC15312.1};
OS Lysinibacillus sp. AC-3.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1680467 {ECO:0000313|EMBL:SKC15312.1, ECO:0000313|Proteomes:UP000190941};
RN [1] {ECO:0000313|EMBL:SKC15312.1, ECO:0000313|Proteomes:UP000190941}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC-3 {ECO:0000313|EMBL:SKC15312.1,
RC ECO:0000313|Proteomes:UP000190941};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000978};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000196-2};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000196-2};
CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 1/2.
CC {ECO:0000256|ARBA:ARBA00004739}.
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DR EMBL; FUYW01000029; SKC15312.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5H3S4; -.
DR STRING; 1680467.SAMN06295926_12954; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000190941; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0004657; F:proline dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.220; -; 1.
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:SF0; PROLINE DEHYDROGENASE 1, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13914; PROLINE OXIDASE; 1.
DR Pfam; PF01619; Pro_dh; 1.
DR PIRSF; PIRSF000196; Pro_dehydrog; 1.
DR SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|PIRSR:PIRSR000196-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000196-2};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000196-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 43..292
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
FT BINDING 131
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 159
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 181..183
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 195
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 220..221
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
SQ SEQUENCE 324 AA; 37323 MW; 1179E245E137823F CRC64;
MLLRDFFIHL SENQLLNSTA KKYGLKLGAQ SVVAGTNIEE TIASIKELNA HNISCTVDNL
GEFVSTEEEA TKAKEQILAV IEAIHENSVD AHISLKPSQL GLDIDVDFCY DNLYEIVEKA
AAYDIFVNFD MEDYDRLQTS FDMVEELSKT FNNVGTVIQS YFYRAKDDIE KFQDYRLRIV
KGAYKEPVEV AFQDKLDIDL NFIELIEYHL LHGKFTSIAT HDHNVIAHVK RFVEDNNIPL
DKFEFQMLYG FRTDLQKELA KEGYNFCVYV PFGEDWYGYF MRRLAERPQN LNLVTKQVFT
KKTNTVLAVA AGAFVLGRLT KRKK
//
