ID E4UUS1_ARTGP Unreviewed; 550 AA.
AC E4UUS1;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=D-lactate dehydrogenase 2 {ECO:0000313|EMBL:EFR01038.1};
GN ORFNames=MGYG_04041 {ECO:0000313|EMBL:EFR01038.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS989824; EFR01038.1; -; Genomic_DNA.
DR RefSeq; XP_003173868.1; XM_003173820.1.
DR AlphaFoldDB; E4UUS1; -.
DR STRING; 535722.E4UUS1; -.
DR GeneID; 10029152; -.
DR VEuPathDB; FungiDB:MGYG_04041; -.
DR eggNOG; KOG1232; Eukaryota.
DR HOGENOM; CLU_017779_4_1_1; -.
DR InParanoid; E4UUS1; -.
DR OMA; YNEDWMR; -.
DR OrthoDB; 1664005at2759; -.
DR Proteomes; UP000002669; 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:UP000002669}.
FT DOMAIN 116..295
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 550 AA; 60328 MW; 26F53361B4D3223D CRC64;
MSCSSRLSYA LRRAGTTGAR TTFANYPALR PAIAHFSSSA SRRLPETASA PTAKSTKYTT
DAYPKLSRNP NFAQLTGEHV QYFKGLLGEG SAVIDGVTTD ATDDIEPFNR DWMKKYRGHT
KLVLKPKTTE EVSKILQYCN SQKLAIVPQG GNTGLVGGSV PVFDEIVVNL SRMNNIRSFD
ENSGVLAVDA GVILEVADNY LAERKHIFPL DLGAKGSCQI GGNVATNAGG LRLLRYGSLH
GNVLGIEAVL PDGTIMEDMS LLRKNNTGYD LKHLFIGGEG TIGIITGVSI ICPQRPKATN
VAFFGLESFE HVRKAFLEAK GQLSEILSAF ELMDGQSQSI VRQVTGLKHP LEGSYPFYCL
VETSGSNGEH DNAKLEAFLE HVMGESIVAD GVLAQDESQA QALWRWREGV TESLSHLGGT
YKYDVSIPLT ELYQLVEDTR DRLSKARLIG NDDSFPVHEV VGYGHMGDSN LHLNVAVRQY
SKEVEKAIEP WVYEWIAKRN GSISAEHGLG IAKKEYIGYS KNEAMIKLMQ QLKKLYDPTP
SSPRENISYI
//
