ID   A0A1U7QNG5_MESAU        Unreviewed;       599 AA.
AC   A0A1U7QNG5;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Proline dehydrogenase {ECO:0000256|RuleBase:RU364054};
DE            EC=1.5.5.2 {ECO:0000256|RuleBase:RU364054};
GN   Name=Prodh {ECO:0000313|RefSeq:XP_005077583.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005077583.1};
RN   [1] {ECO:0000313|RefSeq:XP_005077583.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00000978,
CC         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   RefSeq; XP_005077583.1; XM_005077526.3.
DR   AlphaFoldDB; A0A1U7QNG5; -.
DR   STRING; 10036.ENSMAUP00000013949; -.
DR   GeneID; 101838336; -.
DR   KEGG; maua:101838336; -.
DR   CTD; 5625; -.
DR   eggNOG; KOG0186; Eukaryota.
DR   OrthoDB; 5473051at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
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; -; 2.
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:UP000189706};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..599
FT                   /note="Proline dehydrogenase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010577108"
FT   DOMAIN          198..571
FT                   /note="Proline dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01619"
FT   REGION          148..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..182
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   599 AA;  68200 MW;  A582358F9E80A6D5 CRC64;
     MALRRVFLLR SVAPRVAGLS TEPQAREQPA ASSGAVRAWR AAEAVRRPVP VVDFGNTQEA
     YRSRRSSELV RNLLVLRLCA SRVLLAHHEQ LLRVARKLLG QRMFDRLMKM TFYGHFVAGE
     DQESIRPLIR HNKAFGVGSI LDYGVEEDLS PEEAERKEME SCTSEAEKNS SDTNKREKQY
     QVHPAFGDRR DGVISARTYF YASEAKCDNY MENLLKCIEA SGGASDGGFS AIKLTALGRP
     QFLLQFSDVL TRWRRFFHQM AAEQGQAGRA AVDTKLEVVV LQESIAKMGI ASRAEIEGWF
     TPETLGVSGT VDLLDWNSLI DSRTQLSRHL VVPNVQTGQL EPLLSRFTEE EEQQMKRMLQ
     RMDVLAKKGR EAGVRLMIDA EQSYFQPAIS RLTLEMQRRF NVDKPLIFNT FQCYLKDAYD
     NVTMDMELAR REGWCFGAKL VRGAYMAQER ARAAEIGYED PINPTYEATN VMYHRCLNYV
     LEELQHSPKA EVMVASHNED TVRFTLCRME ELGLHPDDGQ VSFGQLLGMC DQISFPLGQA
     GFPVYKYVPY GPVMEVLPYL SRRALENSSI MKGAQRERQL LRQELHRRLR TGNLFYHPA
//