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Database: UniProt
Entry: A0A1Q9LNN2_9PSEU
LinkDB: A0A1Q9LNN2_9PSEU
Original site: A0A1Q9LNN2_9PSEU 
ID   A0A1Q9LNN2_9PSEU        Unreviewed;       317 AA.
AC   A0A1Q9LNN2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-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=BJP25_15240 {ECO:0000313|EMBL:OLR93628.1};
OS   Actinokineospora bangkokensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinokineospora.
OX   NCBI_TaxID=1193682 {ECO:0000313|EMBL:OLR93628.1, ECO:0000313|Proteomes:UP000186040};
RN   [1] {ECO:0000313|EMBL:OLR93628.1, ECO:0000313|Proteomes:UP000186040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=44EHW {ECO:0000313|EMBL:OLR93628.1,
RC   ECO:0000313|Proteomes:UP000186040};
RA   Greule A., Intra B., Flemming S., Rommel M.G., Panbangred W., Bechthold A.;
RT   "The Draft Genome Sequence of Actinokineospora bangkokensis 44EHWT reveals
RT   the biosynthetic pathway of antifungal compounds Thailandins with unusual
RT   extender unit butylmalonyl-CoA.";
RL   Submitted (OCT-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OLR93628.1}.
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DR   EMBL; MKQR01000009; OLR93628.1; -; Genomic_DNA.
DR   RefSeq; WP_075974524.1; NZ_MKQR01000009.1.
DR   AlphaFoldDB; A0A1Q9LNN2; -.
DR   STRING; 1193682.BJP25_15240; -.
DR   OrthoDB; 9773461at2; -.
DR   UniPathway; UPA00261; UER00373.
DR   Proteomes; UP000186040; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186040}.
FT   DOMAIN          55..306
FT                   /note="Proline dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01619"
FT   BINDING         107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
FT   BINDING         173
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT   BINDING         195..197
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT   BINDING         233..234
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT   BINDING         295
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
FT   BINDING         296
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
SQ   SEQUENCE   317 AA;  34263 MW;  38D85A8950D7700D CRC64;
     MPLAGVLRPA LLAAARSPKA ERAITRVPAT KSLVDRFVAG TSTPDAVAAT RDVLSTGRFV
     TIDHLGEDVT DAQQATANVE HYLDLLDALS AISDAAAVTR PTEISLKLSA LGQSLPRDGH
     KVALENARTL CTAAEAAGAW VTVDAEDHTT TDSTLSIVAE LREDFPSLGT VLQAYLKRTE
     ADCAELSWSR IRLCKGAYRE PASVAHQGAA VDEAYVRCLR VLMNGTGYPM VATHDPAMIA
     AATRLALAAG RTTRDFEFQM LHGIRDAEQR TLVADNHRLR VYLPYGDQWY GYFMRRLAER
     PANLAFFLRA VAGSAGR
//
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