ID A0A1D3CWK5_9EIME Unreviewed; 710 AA.
AC A0A1D3CWK5;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=FAD malate-dehydrogenase {ECO:0000313|EMBL:OEH75582.1};
GN ORFNames=cyc_00723 {ECO:0000313|EMBL:OEH75582.1};
OS Cyclospora cayetanensis.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Cyclospora.
OX NCBI_TaxID=88456 {ECO:0000313|EMBL:OEH75582.1, ECO:0000313|Proteomes:UP000095192};
RN [1] {ECO:0000313|EMBL:OEH75582.1, ECO:0000313|Proteomes:UP000095192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHN_HEN01 {ECO:0000313|EMBL:OEH75582.1,
RC ECO:0000313|Proteomes:UP000095192};
RX PubMed=27129308; DOI=10.1186/s12864-016-2632-3;
RA Liu S., Wang L., Zheng H., Xu Z., Roellig D.M., Li N., Frace M.A., Tang K.,
RA Arrowood M.J., Moss D.M., Zhang L., Feng Y., Xiao L.;
RT "Comparative genomics reveals Cyclospora cayetanensis possesses coccidia-
RT like metabolism and invasion components but unique surface antigens.";
RL BMC Genomics 17:316-316(2016).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC {ECO:0000256|ARBA:ARBA00005163}.
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:OEH75582.1}.
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DR EMBL; JROU02001686; OEH75582.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D3CWK5; -.
DR VEuPathDB; ToxoDB:cyc_00723; -.
DR VEuPathDB; ToxoDB:LOC34617845; -.
DR InParanoid; A0A1D3CWK5; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000095192; Unassembled WGS sequence.
DR GO; GO:0008924; F:malate dehydrogenase (quinone) activity; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR006231; MQO.
DR PANTHER; PTHR43104; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43104:SF2; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF06039; Mqo; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000095192};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..710
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008913961"
SQ SEQUENCE 710 AA; 79417 MW; 5DFA4CCB55D4F110 CRC64;
MLSGCALVAM CKLLEMLGML SEGSYAPPSC PAPLMSKAQE AWVGEGEISS FVKRNRMRLR
VKFEVSSEHI AIAGWGLPAA GSTCMQDGKG MYKTDNLSRL PRRELGRQQL RPPLQNLHRA
LVPRGRGLPA VESHTMSSSL GEASRARRFC MSSQPSRVRV LLTNGLGQKG QPRVKPVTQL
CRCRVMAGLS VNALDAHGCT VSSSEEVDRG RACVVQGGRK GVYGRRLQAV ECMDVFIRVS
VLLRGVREDL RRLGLVERRS AFGVVQSNPR NNSQTIHCGD IETNYTLREL FLASSERGTC
LRGTDNVEKA RVVKRQADML RNFATKLPPS VRDKVVFRFP KMALAVGPEE CDFMEKRFKI
FRELFTSLQL INKQQICEVE PRVGLRSSNF ERPEEVCAMY VPNEYTGVDY VHLAEAFVEQ
AKALGSDKAS ARAEPLMHLK YIHKIDLGLN TEVLEIRRER EDLFSIRTNR GVKQARFVVV
SACGHSLLFA QRMGYGLQYS CLPMAGSFYF TERMLNGKVY TVQDSRLPFA AVHGDPDVVA
QGLTRFGPTA LPLPLLERFN ICTLPDFLRV VNPDLNLLKV YIELLNTRHM RNYVLRNFLF
EVPVLNHHLF AKDVSKIVPS IKPEDLKYAK GFGGVRPQLI DKEQKKLLLG EGKIMTGENI
IFNITPSPGG TTCLGTAQTD LKEIVKQLGA EFNEKAFNKT LLDGEYPVVY
//
