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Database: UniProt
Entry: C6IXD8_9BACL
LinkDB: C6IXD8_9BACL
Original site: C6IXD8_9BACL 
ID   C6IXD8_9BACL            Unreviewed;       306 AA.
AC   C6IXD8;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=proline dehydrogenase {ECO:0000256|ARBA:ARBA00012695};
DE            EC=1.5.5.2 {ECO:0000256|ARBA:ARBA00012695};
GN   Name=fadM {ECO:0000313|EMBL:EES74535.1};
GN   ORFNames=POTG_00815 {ECO:0000313|EMBL:EES74535.1};
OS   Paenibacillus sp. oral taxon 786 str. D14.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=621372 {ECO:0000313|EMBL:EES74535.1, ECO:0000313|Proteomes:UP000003981};
RN   [1] {ECO:0000313|EMBL:EES74535.1, ECO:0000313|Proteomes:UP000003981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D14 {ECO:0000313|EMBL:EES74535.1,
RC   ECO:0000313|Proteomes:UP000003981};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA   Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA   Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA   White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C., White A.,
RA   Lander E., Nusbaum C., Galagan J., Birren B.;
RT   "The Genome Sequence of Paenibacillus sp. D14.";
RL   Submitted (MAR-2009) 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; GG695971; EES74535.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6IXD8; -.
DR   eggNOG; COG0506; Bacteria.
DR   HOGENOM; CLU_061158_0_0_9; -.
DR   UniPathway; UPA00261; UER00373.
DR   Proteomes; UP000003981; 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   ECO:0000313|EMBL:EES74535.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003981}.
FT   DOMAIN          46..300
FT                   /note="Proline dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01619"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
FT   BINDING         135
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT   BINDING         163
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT   BINDING         187..189
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT   BINDING         201
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT   BINDING         226..227
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
FT   BINDING         289
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
SQ   SEQUENCE   306 AA;  34697 MW;  595F205CE90E2A4E CRC64;
     MPMDALLRTL FQSFAKSQSV GRMARRYGLR FGAGRFVAGE TIDGAIEAVR ALNATGRVAT
     LDHLGEFVST EAEAELSMRM CLKTLDAINE AGVEANLSLK LTSLGLGISD EICLRNLTTI
     LNRARMYGLF VRIDMEDFAH CEKTISIYKQ LREQTDNVGI VIQAYLYRSL EDVEDLKPLK
     PNLRLVKGAY KESPKVAYPA KPDVDENFKR LISTHLMNGG YAAIATHDSQ IIDYAKKTIQ
     DLAIPPDRYE FQMLYGIRED LQLALVREGY KVRVYVPFGS DWFGYFMRRL AERPANVWFV
     LKNLFK
//
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