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Database: UniProt
Entry: B3S1L1_TRIAD
LinkDB: B3S1L1_TRIAD
Original site: B3S1L1_TRIAD 
ID   B3S1L1_TRIAD            Unreviewed;       537 AA.
AC   B3S1L1;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=Proline dehydrogenase {ECO:0000256|RuleBase:RU364054};
DE            EC=1.5.5.2 {ECO:0000256|RuleBase:RU364054};
DE   Flags: Fragment;
GN   ORFNames=TRIADDRAFT_1010 {ECO:0000313|EMBL:EDV23248.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV23248.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV23248.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV23248.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
CC   -!- FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate.
CC       {ECO:0000256|RuleBase:RU364054}.
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|RuleBase:RU364054};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU364054};
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   -!- SIMILARITY: Belongs to the proline oxidase family.
CC       {ECO:0000256|ARBA:ARBA00005869, ECO:0000256|RuleBase:RU364054}.
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DR   EMBL; DS985247; EDV23248.1; -; Genomic_DNA.
DR   RefSeq; XP_002114158.1; XM_002114122.1.
DR   AlphaFoldDB; B3S1L1; -.
DR   STRING; 10228.B3S1L1; -.
DR   EnsemblMetazoa; TriadT1010; TriadP1010; TriadG1010.
DR   GeneID; 6755371; -.
DR   KEGG; tad:TRIADDRAFT_1010; -.
DR   CTD; 6755371; -.
DR   eggNOG; KOG0186; Eukaryota.
DR   HOGENOM; CLU_018202_3_1_1; -.
DR   InParanoid; B3S1L1; -.
DR   OMA; GPLKKYH; -.
DR   OrthoDB; 5473051at2759; -.
DR   PhylomeDB; B3S1L1; -.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR   GO; GO:0004657; F:proline dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0010133; P:proline catabolic process to glutamate; IBA:GO_Central.
DR   Gene3D; 3.20.20.220; -; 2.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR029041; FAD-linked_oxidoreductase-like.
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   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|RuleBase:RU364054};
KW   Flavoprotein {ECO:0000256|RuleBase:RU364054};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU364054};
KW   Proline metabolism {ECO:0000256|ARBA:ARBA00023062,
KW   ECO:0000256|RuleBase:RU364054};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009022}.
FT   DOMAIN          273..517
FT                   /note="Proline dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01619"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EDV23248.1"
FT   NON_TER         537
FT                   /evidence="ECO:0000313|EMBL:EDV23248.1"
SQ   SEQUENCE   537 AA;  62168 MW;  67237645CD4A5E5C CRC64;
     IKFDNYRIAY KDKTPLELLR GVLVYRSLTI DYLVDNAIWI MKKSRSLLGR TLFDKLMRAT
     IYGQFVAGEN RTEIMTKIHK MADCGVSPIL DYATEEDITR NQPSVYLNIF NSYRFYIYFY
     STTTVSTRVP VETQFQADER FADRRENVIC ARTYFYEGER KCDENLETFM RCIETAKGMG
     RRPLIAVKVT ALGEPRLLLQ LSATLNQTES LFNLIAIQAD DAMDRCITLE SFKKALDKLQ
     MPLTNEQATE VFSWIDINET GCVPIDWGRA LQPHMKVTNF FSKLKDATGK PLFVPLEEED
     LIQWKKVVHR LQALVECAIH RNVTLMVDAE QTYFQPAISC LTKDLQKVYN KEKGYVFNTY
     QCYLKNTPCA LATDLAEAKR ENYIFGVKLV RGAYMDQERL RAETLGYEDP VQPNIESTTQ
     CYNKMLTMIM NNIKNSEIIV ASHNEGTVKF AIEKMKELDI RKDENKVLFG QLYGMCDRIT
     YALGAAGYCA YKLVPYGPVD EVLPYLTRRA LENRGFVSGA TRERELMWKE FKHRYFS
//
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