ID U1HSL4_ENDPU Unreviewed; 558 AA.
AC U1HSL4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:ERF73540.1};
GN ORFNames=EPUS_07745 {ECO:0000313|EMBL:ERF73540.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF73540.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
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; KE720948; ERF73540.1; -; Genomic_DNA.
DR RefSeq; XP_007800841.1; XM_007802650.1.
DR AlphaFoldDB; U1HSL4; -.
DR GeneID; 19242625; -.
DR eggNOG; KOG1232; Eukaryota.
DR HOGENOM; CLU_017779_4_1_1; -.
DR OMA; YNEDWMR; -.
DR OrthoDB; 1664005at2759; -.
DR Proteomes; UP000019373; 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:UP000019373}.
FT DOMAIN 126..305
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 558 AA; 61397 MW; 2290DFE6AC05A29E CRC64;
MAAHCPRALA RFVRQLHRTG ALQCRSPGRA IPCLSRHFSR SVPSQQTSEA TTTADTDAVA
SHSKQIKYTS ESYPGLKRDP KYSEISSEHV EFFKGILGGD TAVLDGVTRD AGDDLEGYNS
DWMRKYRGHT RLVVKPKSTE EVSKVLKYCN DNMLAVVPQG GNSGLVGGSV PVFDEIVIST
SRMNNIRSFD EVSGILVVDA GCILEVVDNF LAGKNHIFPL DLGAKGSCHI GGNVATNAGG
LRLLRYGSLH GNVLGIEAVL PDGTIVDDLS KLRKNNTGYD LKQLFIGGEG TIGLITAVSV
VCPQRPKAIN VAYFGLESFE KVQQAYIEAK SQLSEILSAF ELMDGQTQDY VHQVTGNKRP
LEGRHPFYCL VETSGSNTEH DNEKLEHFLE SVMGSEIVSD GVIAQDETQV RSLWGWREGI
TEAIGHFGGT YKYDLSIPLP ELYSLVEETR ERLSSAGLVG KDDSHPCVGV MGYGHMGDSN
LHLNVAVRRY AREVEQALEP WVYEWIKKRN GSISAEHGLG VAKKAYIGYS RSETMIRLMK
QIKDLYDPKG IMNPYKYI
//
