ID A0A0H5SCE5_BRUMA Unreviewed; 609 AA.
AC A0A0H5SCE5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Proline dehydrogenase {ECO:0000256|RuleBase:RU364054};
DE EC=1.5.5.2 {ECO:0000256|RuleBase:RU364054};
GN Name=Bm1845 {ECO:0000313|WBParaSite:Bm1845a.1};
GN ORFNames=Bm1845 {ECO:0000313|EMBL:CRZ25761.1}, BM_Bm1845
GN {ECO:0000313|EMBL:CRZ25761.1};
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279 {ECO:0000313|EMBL:CRZ25761.1};
RN [1] {ECO:0000313|EMBL:CRZ25761.1, ECO:0000313|Proteomes:UP000006672}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CRZ25761.1,
RC ECO:0000313|Proteomes:UP000006672};
RX PubMed=17885136; DOI=10.1126/science.1145406;
RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA Pop M., White O., Barton G.J., Carlow C.K., Crawford M.J., Daub J.,
RA Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.W.,
RA Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA Blaxter M.L., Scott A.L.;
RT "Draft genome of the filarial nematode parasite Brugia malayi.";
RL Science 317:1756-1760(2007).
RN [2] {ECO:0000313|EMBL:CRZ25761.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CRZ25761.1};
RA Gao Y.W., Fan S.T., Sun H.T., Wang Z., Gao X.L., Li Y.G., Wang T.C.,
RA Zhang K., Xu W.W., Yu Z.J., Xia X.Z.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:Bm1845a.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2019) 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 EMBL; LN857014; CRZ25761.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H5SCE5; -.
DR STRING; 6279.A0A0H5SCE5; -.
DR EnsemblMetazoa; Bm1845a.1; Bm1845a.1; WBGene00222106.
DR WBParaSite; Bm1845a.1; Bm1845a.1; WBGene00222106.
DR InParanoid; A0A0H5SCE5; -.
DR OMA; GPLKKYH; -.
DR OrthoDB; 5473051at2759; -.
DR Proteomes; UP000006672; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
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; SSF47473; EF-hand; 1.
DR SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
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:UP000006672}.
FT DOMAIN 301..336
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 609 AA; 69601 MW; 2DE3CDE583B4891C CRC64;
MPAILLRPNN FTSVLNFRLL AHLSYRMAST EVSSSQASAA VNIDEIKECY NKLDLDFKST
KAAFKGKKTS ELLRSLIVLP LCTVQTLRTR EELLLVGLKK IFGEKLYAKL LKSTFFGQFV
GGETIDEVQQ TMKRLKSCGV KSILDYCVEA DISSDEAEKK AVEGIVGGEA KIEPVGSVVD
KATVEKTLQR YTVHKEFGDR RKDVVSARTY FYESEVQCDK NCDIFCASVD AITSAIGSWG
INCIKLTALG RPQLLLKLSE LIAQSNNFYK TLIGSSWDDL LLNKIKKEEF LKRIEDHGVQ
IDEIMMQKWL ETVDFDENGF VDFYDWRKLI EEHQRLDQIF QVYNVKTKRM EPLLNCLTEA
ESRETVNMMD RIVRTIEYAK KHNLRTMIDA EQTYFQAAIS RLAMAMMRKY NKEDAIVFST
YQAYLKSCLR NVELDLHLAR REGFHFGCKV VRGAYMEQER KRAAALNYDD PVNPNIEATA
EMYRKVMQRI IKESQERSPG SISVMAATHN EQSTKNVVEM MREANISPSS ETVSFAQLYG
MCDQISYSLG NAGYSVYKYV PYGSIDKVLP YLSRRAQENA SVLGKIRREV GLMSRELLRR
IFTFGGRFD
//
