ID A6QSJ3_AJECN Unreviewed; 551 AA.
AC A6QSJ3;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=D-lactate dehydrogenase 2, mitochondrial {ECO:0000313|EMBL:EDN02485.1};
GN ORFNames=HCAG_00349 {ECO:0000313|EMBL:EDN02485.1};
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN02485.1, ECO:0000313|Proteomes:UP000009297};
RN [1] {ECO:0000313|Proteomes:UP000009297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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DR EMBL; CH476655; EDN02485.1; -; Genomic_DNA.
DR AlphaFoldDB; A6QSJ3; -.
DR STRING; 339724.A6QSJ3; -.
DR VEuPathDB; FungiDB:HCAG_00349; -.
DR HOGENOM; CLU_017779_4_1_1; -.
DR OMA; YNEDWMR; -.
DR OrthoDB; 1664005at2759; -.
DR Proteomes; UP000009297; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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; IPR016167; FAD-bd_PCMH_sub1.
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; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 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 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000009297}.
FT DOMAIN 119..298
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 551 AA; 60363 MW; C4213856350E87B6 CRC64;
MSGARGVSLA IRRGGSSRIR TGSFRPNFCD ARSMRFSTSA SLLGAQEISV TATPPKSQSK
YTTDAYPNLK RNPNFSELTS THVQHFKTLL KSPSAVIDGF TTDATDDIEP FNCDWMRKYR
GHAKLVLKPQ NTKQMSDVLK YCNENKLAVV PQGGNTGLVG GGVPVFDEVI INTARMNNIR
SFDENSGVLV VDAGVILEVA DKYLAERNHI FPLDLGAKGS CHIGGNVATN AGGLRLLRYG
SLHGNVLGIE AVLPDGTIID DLSTLRKNNT GYDLKQLFIG GEGTIGIITG VSIICPQRPK
AVNVAFFGIE SYKQALAAFL EAKGHLSEIL SAFELMDGRS QDMVHGVTGL KKPLDGSYPF
YCLVETSGSN GEHDNEKLEG FLEHVMGESI VADGVLAQDE TQAQALWRWR EGITEALSHL
GGTYKYDVSI PLAELYQLVD DTRDRLTSAG LVGDDENYPV REVLGYGHMG DSNLHLNIAV
RQYNKQVEEL IEPWVYEWIA KRNGSISAEH GLGIAKKEFI GYSKSETMIK LMAQLKKLYD
PNGIMNPYKY V
//
