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Database: UniProt
Entry: S9W699_9TRYP
LinkDB: S9W699_9TRYP
Original site: S9W699_9TRYP 
ID   S9W699_9TRYP            Unreviewed;       401 AA.
AC   S9W699;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   03-MAY-2023, entry version 27.
DE   RecName: Full=Proline dehydrogenase {ECO:0000256|ARBA:ARBA00012695, ECO:0000256|RuleBase:RU364054};
DE            EC=1.5.5.2 {ECO:0000256|ARBA:ARBA00012695, ECO:0000256|RuleBase:RU364054};
GN   ORFNames=STCU_03432 {ECO:0000313|EMBL:EPY31485.1};
OS   Strigomonas culicis.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Strigomonadinae; Strigomonas.
OX   NCBI_TaxID=28005 {ECO:0000313|EMBL:EPY31485.1, ECO:0000313|Proteomes:UP000015354};
RN   [1] {ECO:0000313|EMBL:EPY31485.1, ECO:0000313|Proteomes:UP000015354}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23560078;
RA   Motta M.C., Martins A.C., de Souza S.S., Catta-Preta C.M., Silva R.,
RA   Klein C.C., de Almeida L.G., de Lima Cunha O., Ciapina L.P., Brocchi M.,
RA   Colabardini A.C., de Araujo Lima B., Machado C.R., de Almeida Soares C.M.,
RA   Probst C.M., de Menezes C.B., Thompson C.E., Bartholomeu D.C., Gradia D.F.,
RA   Pavoni D.P., Grisard E.C., Fantinatti-Garboggini F., Marchini F.K.,
RA   Rodrigues-Luiz G.F., Wagner G., Goldman G.H., Fietto J.L., Elias M.C.,
RA   Goldman M.H., Sagot M.F., Pereira M., Stoco P.H., de Mendonca-Neto R.P.,
RA   Teixeira S.M., Maciel T.E., de Oliveira Mendes T.A., Urmenyi T.P.,
RA   de Souza W., Schenkman S., de Vasconcelos A.T.;
RT   "Predicting the Proteins of Angomonas deanei, Strigomonas culicis and Their
RT   Respective Endosymbionts Reveals New Aspects of the Trypanosomatidae
RT   Family.";
RL   PLoS ONE 8:E60209-E60209(2013).
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   -!- SIMILARITY: Belongs to the proline oxidase family.
CC       {ECO:0000256|ARBA:ARBA00005869, ECO:0000256|RuleBase:RU364054}.
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:EPY31485.1}.
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DR   EMBL; ATMH01003432; EPY31485.1; -; Genomic_DNA.
DR   AlphaFoldDB; S9W699; -.
DR   EnsemblProtists; EPY31485; EPY31485; STCU_03432.
DR   OrthoDB; 5473051at2759; -.
DR   Proteomes; UP000015354; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004657; F:proline dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006562; P:proline catabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.220; -; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR002048; EF_hand_dom.
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.
DR   PROSITE; PS50222; EF_HAND_2; 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:UP000015354}.
FT   DOMAIN          102..137
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
SQ   SEQUENCE   401 AA;  46341 MW;  AF00A3EA2432FF38 CRC64;
     MFDENMKLYM MSTMHASINP PASGPGVIAV KVSGMCNPQL LARMNAILMS IHQSWCQHFT
     QEEAPRLEEC RVLMGLERKH RMTITHDQLR EGFKRRLGDK PLDESLVAEM IQALDPTNKG
     TIHYLDYVSL LTDAVSEVDP CSLKERIAAL LPPFNPTEKR LWRDINTRLH LIASTAQRLD
     VRVMIDAEQS FYQLAIDVLT LHLQMEFNRE AAIVYNTYQC YLTYAEDRIA ADLLRAEKLG
     FQWGGKIVRG AYMIQERKTA QEYDYTSPIW PTLEATAKCY EDSAKRIFAA MERNPDKKYE
     VFFGTHNEKV IRDLAKRVYE TPALQAHTTF GQLYGMRDNI TFPLAKCGFC VYKYLPYGPA
     RETIHYLGRR AVENSSILAD KNSTEVRLMR EELRRRLTFR S
//
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