ID W6MH62_9ASCO Unreviewed; 466 AA.
AC W6MH62;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=KUCA_T00001253001 {ECO:0000313|EMBL:CDK25286.1};
OS Kuraishia capsulata CBS 1993.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK25286.1};
RN [1] {ECO:0000313|EMBL:CDK25286.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK25286.1};
RA Genoscope - CEA;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDK25286.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK25286.1};
RA Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA Gabaldon T., Wincker P., Dujon B.;
RT "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT features among budding yeasts (/Saccharomycotina/).";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG793125; CDK25286.1; -; Genomic_DNA.
DR AlphaFoldDB; W6MH62; -.
DR STRING; 1382522.W6MH62; -.
DR HOGENOM; CLU_029274_0_0_1; -.
DR OrthoDB; 7218at2759; -.
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}.
FT DOMAIN 200..438
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
SQ SEQUENCE 466 AA; 52294 MW; D973BAB91BCA3E73 CRC64;
MLSTRSMYRS TAFLRVGLVL NRRTLISSKT TKTVMPVTYD STPEPSNREK SPGYLEALTT
PELLSYGLIG LATLNKGTLD MAIKAFPFIP TWMLKVFLYK NYCGGEDFEQ VKATGARLAK
RGIKNMMISL TIEAAEVHGD AEPIDIGYIV RETKKSVSEV LVPHTLSMIS ESGDLNSVPP
GYVALKPTGL IDDAVNVLTN YEHPDYSVKF EELVANCSEI CEIVRTANAR LAKEHPERIA
PFVVATIDAE KFTLQRGVYE LQRRLFARFN VSEEPISVVG TIQMYLKESQ DLLASEYKLA
QQNRYRVGWK LVRGAYIHTE PDRSVIHDTK ENTDDNYNRG ISRTIDQIVK QEKNTGVVGH
LVVASHNYDS QLFAEEIIKS SAQKSNITLA QLLGMADDVT HDLIHAHGVN NIIKYVPWGP
PKETKDYLLR RLEENGDAVR SDSGWPLLKG IVSVIGRRWF TQKQSL
//
