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Database: UniProt
Entry: A0A143HEG9_9BACL
LinkDB: A0A143HEG9_9BACL
Original site: A0A143HEG9_9BACL 
ID   A0A143HEG9_9BACL        Unreviewed;       324 AA.
AC   A0A143HEG9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=proline dehydrogenase {ECO:0000256|ARBA:ARBA00012695};
DE            EC=1.5.5.2 {ECO:0000256|ARBA:ARBA00012695};
GN   ORFNames=ATY39_12150 {ECO:0000313|EMBL:AMX00103.1};
OS   Rummeliibacillus stabekisii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Rummeliibacillus.
OX   NCBI_TaxID=241244 {ECO:0000313|EMBL:AMX00103.1, ECO:0000313|Proteomes:UP000076021};
RN   [1] {ECO:0000313|EMBL:AMX00103.1, ECO:0000313|Proteomes:UP000076021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PP9 {ECO:0000313|EMBL:AMX00103.1,
RC   ECO:0000313|Proteomes:UP000076021};
RX   PubMed=27231360;
RA   da Mota F.F., Vollu R.E., Jurelevicius D., Seldin L.;
RT   "Whole-Genome Sequence of Rummeliibacillus stabekisii Strain PP9 Isolated
RT   from Antarctic Soil.";
RL   Genome Announc. 4:0-0(2016).
RN   [2] {ECO:0000313|Proteomes:UP000076021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PP9 {ECO:0000313|Proteomes:UP000076021};
RA   Ploux O.;
RL   Submitted (MAR-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}.
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DR   EMBL; CP014806; AMX00103.1; -; Genomic_DNA.
DR   RefSeq; WP_066790140.1; NZ_CP014806.1.
DR   AlphaFoldDB; A0A143HEG9; -.
DR   STRING; 241244.ATY39_12150; -.
DR   KEGG; rst:ATY39_12150; -.
DR   OrthoDB; 9773461at2; -.
DR   UniPathway; UPA00261; UER00373.
DR   Proteomes; UP000076021; Chromosome.
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:UP000076021}.
FT   DOMAIN          42..289
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;  37534 MW;  01749C9A994E3DA4 CRC64;
     MSLKDFFIAL SENQFLNNNA KKYGLKMGAA SVVAGTNINE MIKSIKELNS HGISCTIDNL
     GEFVHDKAEA TAAKNQILAV IEAVHETGVD AHISLKPSQL GLDIDYDFCY ENLKEIVELA
     DRYDIFVNFD MENYARLQPS FDLLEELSRE HDNIGTVIQA YFFRAKEDIE KYKNYRLRIV
     KGAYKEPSEV AYQTKEEIDR NYIELLEYHL LNGKFTSIAT HDHNVINHMK QFIAAHNIPK
     EKYEFQMLYG FRRDMQLELA KEGYNFCTYV PFGQDWYGYF MRRLAERPQN LELVVKQVFN
     KKTNTLIGLT AAGFALGRLT KRRK
//
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