ID A3LTY9_PICST Unreviewed; 612 AA.
AC A3LTY9;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 2.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN Name=DLD3 {ECO:0000313|EMBL:ABN66496.2};
GN ORFNames=PICST_31583 {ECO:0000313|EMBL:ABN66496.2};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN66496.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN66496.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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; CP000498; ABN66496.2; -; Genomic_DNA.
DR RefSeq; XP_001384525.2; XM_001384488.1.
DR AlphaFoldDB; A3LTY9; -.
DR STRING; 322104.A3LTY9; -.
DR GeneID; 4838615; -.
DR KEGG; pic:PICST_31583; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_017779_3_3_1; -.
DR InParanoid; A3LTY9; -.
DR OMA; GQGFEWA; -.
DR OrthoDB; 1664005at2759; -.
DR Proteomes; UP000002258; Chromosome 4.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IEA:UniProtKB-EC.
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:SF111; D-LACTATE DEHYDROGENASE, MITOCHONDRIAL-RELATED; 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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABN66496.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258}.
FT DOMAIN 149..332
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 612 AA; 67045 MW; 3AF626CDB3AE901C CRC64;
MFSKLANIPR PGVSRSFLKN LAKNSSLKPF NVPVAKYSTT SVKSATSDNH NGSQESKSST
FGYASVGTVF LAVGTYIGTK LNFDPDSPDR STTPVDALTS PQYANDDEFK KGLAEIVAIV
GAENTNLDKT VLDAHSDTFY STHHPPKPHL NHPSAVIYPA GTEQVSAILK VAHKYRIPVV
ANSGLTSLEG QNMHTRGPNS ISLSFAHLNQ ILEFHPEDLD VVVQAGVGWQ DLDEFLKGRE
DGKHLLFGPD PGMGATIAGM VSTSASGTNA FKYGTMKENV VNLTVVLADG TIVKTKQRPR
KSSAGYDTTR LFIGAEGTLG IITEVTVKLH VKPVHELVSI ATFPTIKDAA ATAQEIISRS
GLQPNAIEIL DDTMMSFVNE SADAAGKKFI EKPTLFFKLG GPTKSSIDEQ IKVIKKIASS
NSLIKFENSH NEEENAILWS ARRQGLWSTF QYGSKILEDK NDVQIWTTDI AIPISNLSQV
IAETNDDLNN SGYYKRFSVM GHIGDGNCHF LILYNSKDYR KTQKVIDRMV ERALKYEGTS
TGEHGVGVGK RRYLNLELGK STVDLMRQIK LSLDPRRILN PDKIFIIDPN DDLDQLLEAG
HIAEVNKHDC CH
//
