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
//