ID K2MXR2_TRYCR Unreviewed; 566 AA.
AC K2MXR2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 03-MAY-2023, entry version 29.
DE RecName: Full=Proline dehydrogenase {ECO:0000256|ARBA:ARBA00012695, ECO:0000256|RuleBase:RU364054};
DE EC=1.5.5.2 {ECO:0000256|ARBA:ARBA00012695, ECO:0000256|RuleBase:RU364054};
GN ORFNames=MOQ_004239 {ECO:0000313|EMBL:EKF31920.1};
OS Trypanosoma cruzi marinkellei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=85056 {ECO:0000313|EMBL:EKF31920.1, ECO:0000313|Proteomes:UP000007350};
RN [1] {ECO:0000313|EMBL:EKF31920.1, ECO:0000313|Proteomes:UP000007350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7 {ECO:0000313|EMBL:EKF31920.1,
RC ECO:0000313|Proteomes:UP000007350};
RX PubMed=23035642; DOI=10.1186/1471-2164-13-531;
RA Franzen O., Talavera-Lopez C., Ochaya S., Butler C.E., Messenger L.A.,
RA Lewis M.D., Llewellyn M.S., Marinkelle C.J., Tyler K.M., Miles M.A.,
RA Andersson B.;
RT "Comparative genomic analysis of human infective Trypanosoma cruzi lineages
RT with the bat-restricted subspecies T. cruzi marinkellei.";
RL BMC Genomics 13:531-531(2012).
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 -!- SIMILARITY: Belongs to the proline oxidase family.
CC {ECO:0000256|ARBA:ARBA00005869, ECO:0000256|RuleBase:RU364054}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKF31920.1}.
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DR EMBL; AHKC01010536; EKF31920.1; -; Genomic_DNA.
DR AlphaFoldDB; K2MXR2; -.
DR EnsemblProtists; EKF31920; EKF31920; MOQ_004239.
DR OrthoDB; 5473051at2759; -.
DR Proteomes; UP000007350; 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; 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; PS50222; EF_HAND_2; 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:UP000007350}.
FT DOMAIN 258..293
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 566 AA; 64942 MW; 0BC5D56346B68041 CRC64;
MFRGYARFAS KYAQNVSPTS RTIQPVNFND DTVFRTKSFW WLMRALFVLR ICQISFFSKN
AVYLMKKSES VLGPFLIYNT LVKMTAYGHF CAGEDERGLK NTVKALERQG IGSVLDYAAE
ADVAGFVPPP GLEEAPNLSM ASLVHKTTVN YPSYGELYDE NMKLYVMCVM HASLNQPVNG
VGLAAVKVTG MCDPQLLARV SAILHSVHAG WLQNFTNEKP PPIEECRVVM GTNKEYQLYI
TYDQLRKGLM AYGSARKYTE EEVEAVIKAL DEKNEGKVNY YQFKKVVSEA VLSMEPTPVQ
KLIVEKLPKL TEEERELWRA LQRRLSVIVR TAKDLRVRVL FDAEQTFYQL AIDNIVLQFQ
RQFNLEEPTV YNTYQCYLTY TEDRVFNDLT RSEHEGWVWG GKIVRGAYMV QERETASKYS
YKSPVWPTYE ETNACYRACA KRILKEFTRL PNTPFEVLFG THNKESVEEI SEAILKLPPV
RGLAVFAQLY GMADHLTIPL QKAGFRVFKY LPYGPVKETI HYLGRRATEN ASVLANGGSE
EVELMKKELR RRLFWFKSYL EKGVKA
//
