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
//