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Database: UniProt
Entry: A0A182TMD4_9DIPT
LinkDB: A0A182TMD4_9DIPT
Original site: A0A182TMD4_9DIPT 
ID   A0A182TMD4_9DIPT        Unreviewed;       477 AA.
AC   A0A182TMD4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Proline dehydrogenase {ECO:0000256|RuleBase:RU364054};
DE            EC=1.5.5.2 {ECO:0000256|RuleBase:RU364054};
OS   Anopheles melas.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=34690 {ECO:0000313|EnsemblMetazoa:AMEC004953-PA, ECO:0000313|Proteomes:UP000075902};
RN   [1] {ECO:0000313|Proteomes:UP000075902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM1001059 {ECO:0000313|Proteomes:UP000075902};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles melas CM1001059_A (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AMEC004953-PA}
RP   IDENTIFICATION.
RC   STRAIN=CM1001059 {ECO:0000313|EnsemblMetazoa:AMEC004953-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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|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   AlphaFoldDB; A0A182TMD4; -.
DR   STRING; 34690.A0A182TMD4; -.
DR   EnsemblMetazoa; AMEC004953-RA; AMEC004953-PA; AMEC004953.
DR   VEuPathDB; VectorBase:AMEC004953; -.
DR   Proteomes; UP000075902; Unassembled WGS 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; -; 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          141..446
FT                   /note="Proline dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01619"
FT   REGION          18..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   477 AA;  54700 MW;  9DFFFAB313A42F14 CRC64;
     LRSFGVKPIL DYSVEEDLSQ EEAEKREVEA SVSSAGTNLS EDSADSLPQY SVDKTFADRR
     YKVQSARTYF YLNEATCERN METFLECLDA VKGATFGTGI TAIKLTALGR PQLLLQVSEV
     IMQARRYMMD LAGSTGNILT HHKTIQDLER YLGNVSDKAE VKQFLEKVTS DKDGILHLFP
     WTGIINEDCQ LSETFRVPDP VTGQMRRLIS KIPPKEEEMF RNMIRRLNTI VKTAQDLDVR
     IMIDAEQTYF QPAISRITLE MMRKYNTEKA IVFNTYQCYL KDTYKEVCTD LEQAKRQNFY
     FGAKLVRGAY IEQERARAAA LGYEDPTNPS FEATTEMYHK TLTECLRRIR ILKDANIDPK
     KIAIMVASHN EDTVRFAIEK MQEIGIHPED KVICFGQLLG MCDYITFPLG QAGYSAYKYI
     PYGPVNEVLP YLSRRAQENK GVLQKIKKEK RLLLSEITKR LAKGQLFYKP KGKYVPI
//
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