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Database: UniProt
Entry: A0A0J6YGS8_COCIT
LinkDB: A0A0J6YGS8_COCIT
Original site: A0A0J6YGS8_COCIT 
ID   A0A0J6YGS8_COCIT        Unreviewed;       606 AA.
AC   A0A0J6YGS8;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:KMP06093.1};
GN   ORFNames=CIRG_05774 {ECO:0000313|EMBL:KMP06093.1};
OS   Coccidioides immitis RMSCC 2394.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP06093.1, ECO:0000313|Proteomes:UP000054565};
RN   [1] {ECO:0000313|Proteomes:UP000054565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; DS028096; KMP06093.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J6YGS8; -.
DR   STRING; 404692.A0A0J6YGS8; -.
DR   Proteomes; UP000054565; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748:SF116; D-LACTATE DEHYDROGENASE (CYTOCHROME) (AFU_ORTHOLOGUE AFUA_7G02560); 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        84..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          173..350
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   606 AA;  66727 MW;  4938571FE2EFBCD6 CRC64;
     MFSSREVASK AARAAKRAQR ITTTVYNSTP KNRAHAKRSF GTTCARAEER PTFKGQLYES
     TQQRIQRERA ELERYARMQK DSSALRNTAI TFTVLVTALG CYYLGSLRPA ALPESSTTPL
     YSAPKPHHDT SPGNLQAAWS DFIHIVGKEN VSTDKVDLDA HAGSDWSSYT AKESERPFLV
     VFPSTTEEVS RIMKVCHDRR IPVTAFSGGT SLEGHFSPTR GGVCVDFARM GNIIALHEDD
     LDVVVQPAVG WEDLNEELAK RGLFFPPDPG PGAQIGGMVG TGCSGTNAYR YGTMREWVLS
     LTVVLADGTI IKTRQRPRKS SAGYDLTKLF IGSEGTLGLV TEATLKVTPK PKSESVAVAA
     FPSIHCAAEC VARVVGEGIQ VAGVEILDDV QMKCINDSQT TRRTWKEAPT IFFKFTGTPA
     GVKEQIKIVQ KIAKDTMGQS FEFAQGRDEM QELWSARKEA LWSVMAMKRD QNDHVWTTDV
     AVPISRLPDI IEQTKEDITK KGLLGGICGH VGDGNFHAIL LFNDSERNVA EGVVHRMVKR
     AVEMEGTVTG EHGVGLIKRD YLPHELGDSA VDTMRKIKQA LDPLCLLNCD KVVRMEPPKQ
     GEIKKW
//
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