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Database: UniProt
Entry: A0A0M3QZA6_DROBS
LinkDB: A0A0M3QZA6_DROBS
Original site: A0A0M3QZA6_DROBS 
ID   A0A0M3QZA6_DROBS        Unreviewed;       703 AA.
AC   A0A0M3QZA6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Proline dehydrogenase {ECO:0000256|RuleBase:RU364054};
DE            EC=1.5.5.2 {ECO:0000256|RuleBase:RU364054};
GN   ORFNames=Dbus_chrXg895 {ECO:0000313|EMBL:ALC49039.1};
OS   Drosophila busckii (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC49039.1, ECO:0000313|Proteomes:UP000494163};
RN   [1] {ECO:0000313|EMBL:ALC49039.1, ECO:0000313|Proteomes:UP000494163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole larvae {ECO:0000313|EMBL:ALC49039.1};
RA   Zhou Q., Bachtrog D.;
RT   "Ancestral chromatin configuration constrains chromatin evolution on
RT   differentiating sex chromosomes in Drosophila.";
RL   Submitted (AUG-2015) 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   -!- 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   EMBL; CP012528; ALC49039.1; -; Genomic_DNA.
DR   RefSeq; XP_017851812.1; XM_017996323.1.
DR   AlphaFoldDB; A0A0M3QZA6; -.
DR   STRING; 30019.A0A0M3QZA6; -.
DR   GeneID; 108606315; -.
DR   OMA; GPLKKYH; -.
DR   OrthoDB; 5473051at2759; -.
DR   Proteomes; UP000494163; Chromosome x 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; -; 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:UP000494163}.
FT   DOMAIN          224..672
FT                   /note="Proline dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01619"
FT   REGION          249..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   703 AA;  80169 MW;  7C67F9589208F361 CRC64;
     MALLRVLSAQ RSTVYLVYCR NSVNKSNLAA ATAVANCRRD QRRQHSGKAA SCASNSISDE
     EYALLSALDA LPQRQHQHHQ HHHHQQQRKQ LLQILAAGHG TVRGVHSMPR QQQAQLAAAE
     LAVEDKQRVH LEPAKPNPAG TPQRDPLDVS FNDPIAAFKS KTTWELLRAY LVYMICSSEK
     LVEHNMQLMK ICKQIFGAKL FTMMMKATFY GHFVAGEDQI KIIPTLERLR SFGVKPILDY
     SVEEDISQEE AEKREVEASV SSAGDSVKDE GSMPQYHVDK SFADRRYKVS SARTYFYLNE
     ATCERNMETF IKCLEAVSGA TFGTGITAIK LTALGRPQLL LQLSEVIMRT RKYMEDLVGG
     QGNVLTHHKT IKDLEKYYAT VGDNKDVQHF LKNVTSDKEG ILHLFPWSGI VDEDSQLSDT
     FRVPDPKTGQ MRRLISQIPP KEEEMFRNMI RRLNTIVKTA ADLDVRIMID AEQTYFQPAI
     SRITLEMMRK YNKDKAIVFN TYQCYLRESF REVGTDLEQA KRQNFYFGAK LVRGAYMEQE
     RARAQALGYP DPVNPNYEAT TDMYHKTLAE CLRRIKVLKD CGDDAKKIGI MVASHNEDTV
     RFAIEKMKEI GISPEDKVIC FGQLLGMCDY ITFPLGQAGY SAYKYIPYGP VEEVLPYLSR
     RAQENKGVLK KIQKEKRLLL AEIRRRLMRG QLFYTPKGNY VPI
//
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