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Database: UniProt
Entry: A0A0Q2R4Q5_MYCGO
LinkDB: A0A0Q2R4Q5_MYCGO
Original site: A0A0Q2R4Q5_MYCGO 
ID   A0A0Q2R4Q5_MYCGO        Unreviewed;       318 AA.
AC   A0A0Q2R4Q5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=proline dehydrogenase {ECO:0000256|ARBA:ARBA00012695};
DE            EC=1.5.5.2 {ECO:0000256|ARBA:ARBA00012695};
GN   ORFNames=AO501_21275 {ECO:0000313|EMBL:KQH79118.1};
OS   Mycobacterium gordonae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1778 {ECO:0000313|EMBL:KQH79118.1, ECO:0000313|Proteomes:UP000051677};
RN   [1] {ECO:0000313|EMBL:KQH79118.1, ECO:0000313|Proteomes:UP000051677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CTRI 14-8773 {ECO:0000313|EMBL:KQH79118.1,
RC   ECO:0000313|Proteomes:UP000051677};
RA   Ustinova V., Smirnova T., Blagodatskikh K., Varlamov D., Larionova E.,
RA   Chernousova L.;
RT   "Mycobacterium gordonae draft genome assembly.";
RL   Submitted (OCT-2015) 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:KQH79118.1}.
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DR   EMBL; LKTM01000113; KQH79118.1; -; Genomic_DNA.
DR   RefSeq; WP_055577968.1; NZ_LKTM01000113.1.
DR   AlphaFoldDB; A0A0Q2R4Q5; -.
DR   STRING; 1778.A9W97_10435; -.
DR   OrthoDB; 9773461at2; -.
DR   UniPathway; UPA00261; UER00373.
DR   Proteomes; UP000051677; 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:UP000051677}.
FT   DOMAIN          49..310
FT                   /note="Proline dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01619"
FT   BINDING         110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
FT   BINDING         176
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT   BINDING         200..202
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT   BINDING         239..240
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT   BINDING         299
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
FT   BINDING         300
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
SQ   SEQUENCE   318 AA;  34771 MW;  1E720C94FFDBCCF0 CRC64;
     MSGVFAHTMR PAMLAASRAD RLRHVVERSA LTQRVVRRFV PGETLSGVLE VVAALRDSGR
     SISIDYLGEN VADADGAAAT VQAYLDLLDA LGRRDDRVFD GVRPLEVSVK LSALGQSLDR
     DGQKIALDNA RTICERAEAV GAWVTVDAED HTTTDSTLSI SGDLRVDFPW LGTVLQAYLR
     RTPGDCAELA SVGARVRLCK GAYDEPASVA YRAAADVTDS YLRCLRVLMA GRGYPMVASH
     DPAIIDAVSA LASEFGCDAY EYQMLYGIRD DEQLRLAGDG NRVRVYVPFG TQWYGYFMRR
     LAERPANLAF FLRALSAH
//
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