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Database: UniProt
Entry: A0A1B7TII3_9ASCO
LinkDB: A0A1B7TII3_9ASCO
Original site: A0A1B7TII3_9ASCO 
ID   A0A1B7TII3_9ASCO        Unreviewed;       453 AA.
AC   A0A1B7TII3;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=HANVADRAFT_54872 {ECO:0000313|EMBL:OBA28488.1};
OS   Hanseniaspora valbyensis NRRL Y-1626.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX   NCBI_TaxID=766949 {ECO:0000313|EMBL:OBA28488.1, ECO:0000313|Proteomes:UP000092321};
RN   [1] {ECO:0000313|Proteomes:UP000092321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-1626 {ECO:0000313|Proteomes:UP000092321};
RX   PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA   Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA   Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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:OBA28488.1}.
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DR   EMBL; LXPE01000003; OBA28488.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B7TII3; -.
DR   OrthoDB; 7218at2759; -.
DR   Proteomes; UP000092321; Unassembled WGS sequence.
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; 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; 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:UP000092321}.
FT   DOMAIN          177..434
FT                   /note="Proline dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01619"
SQ   SEQUENCE   453 AA;  50963 MW;  CCD5ADBF2B67D39A CRC64;
     MVASIPSATH PFNNQLLDKE ETEKLAQLKA PLPDAFLSKI PKRDLFSLFL IGCCSLNKPI
     LDLVIKIFPI VPLPLIKYFI YNLYCGGENF KEVLETGAKL QSTGVNNMML SLTIEDSEGT
     KNIDINYIVE ETSKSIEGIL KPHLLKQLDA IVASGKSNIN DIPPGYIALK PSALVKDPFN
     TLLNYDINSP NEHWKKQSLD LFNNCAKITQ VIRDLNEELS KQYPDRKTPF FVSTIDAEKY
     DLQKNGVYKL QTQLFKKFNK VTDKHISVIG TWQLYLKDSQ KDLLDDFKAA EKDGSYKIGC
     KLVRGAYIHS ETNRNQIIYE NQKGTDENYN STLAIVANDL LANKDSKFGH LVVASHNYNS
     QLIISAKLAA AKKTGAEGQY KIVLGQLLGM ADNVTDDLVH NHGVKNIIKY VPWSTDSYET
     KDYLLRRLQE NGDAVRSDNG LPLLKSIFRS LKL
//
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