ID J6EEB7_SACK1 Unreviewed; 480 AA.
AC J6EEB7;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
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 Name=YLR142W {ECO:0000313|EMBL:EJT41967.1};
GN ORFNames=SKUD_151804 {ECO:0000313|EMBL:EJT41967.1};
OS Saccharomyces kudriavzevii (strain ATCC MYA-4449 / AS 2.2408 / CBS 8840 /
OS NBRC 1802 / NCYC 2889) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=226230 {ECO:0000313|EMBL:EJT41967.1, ECO:0000313|Proteomes:UP000002753};
RN [1] {ECO:0000313|EMBL:EJT41967.1, ECO:0000313|Proteomes:UP000002753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889
RC {ECO:0000313|Proteomes:UP000002753};
RX PubMed=12775844; DOI=10.1126/science.1084337;
RA Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA Waterston R., Cohen B.A., Johnston M.;
RT "Finding functional features in Saccharomyces genomes by phylogenetic
RT footprinting.";
RL Science 301:71-76(2003).
RN [2] {ECO:0000313|Proteomes:UP000002753}
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889
RC {ECO:0000313|Proteomes:UP000002753};
RX PubMed=22384314; DOI=10.1534/g3.111.000273;
RA Scannell D.R., Zill O.A., Rokas A., Payen C., Dunham M.J., Eisen M.B.,
RA Rine J., Johnston M., Hittinger C.T.;
RT "The awesome power of yeast evolutionary genetics: New genome sequences and
RT strain resources for the Saccharomyces sensu stricto genus.";
RL G3 (Bethesda) 1:11-25(2011).
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:EJT41967.1}.
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DR EMBL; AACI03001824; EJT41967.1; -; Genomic_DNA.
DR AlphaFoldDB; J6EEB7; -.
DR STRING; 226230.J6EEB7; -.
DR HOGENOM; CLU_029274_0_0_1; -.
DR Proteomes; UP000002753; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
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:UP000002753};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 77..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 218..457
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
SQ SEQUENCE 480 AA; 53652 MW; 7DAAA268484699F0 CRC64;
MLQMIASRSS LLVTKSRLPS LCYPLVSRTY VSKTPTHSNT AANLMVETPA SSNTNGNSVM
APPNSINFLQ TLPKKELFQL GFIGIATLNS LFLNTIIGLF PYIPIPVIKF FVSSLYCGGE
NFKEVIECGE RLQKRGISNM MLSLTIENSE GTKSLTGASV DHIVQETISS VHNILLPNII
NQLESKPVND IAPGYIALKP SALVDNPHEV LYNFSNPAFK AQRDQLIDNC SKITKVVFEL
NQALLEKYPG RKAPFLVSTI DAEKYDLQEN GVYELQRILF QKFNPVSSRL ISCIGTWQLY
LRDSGDHLLH ELKLAQENSY RLGLKLVRGA YIHSEKDRNQ IIFGEKTDTD ENYDRVITQV
VNDLIINGED SYYGHLVVAS HNYQSQMLVT NLLKSAQDNS YAKSNIVLGQ LLGMADNVTH
DLITNHGAKN IIKYVPWGPP LETKDYLLRR LQENGDAVRS DNGWPLIKAI ARSIPKRLGL
//
