ID A0AAE0WWD9_9PEZI Unreviewed; 503 AA.
AC A0AAE0WWD9;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE RecName: Full=L-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00068515};
DE EC=1.1.2.3 {ECO:0000256|ARBA:ARBA00066458};
GN Name=CYB2 {ECO:0000313|EMBL:KAK3679227.1};
GN ORFNames=LTR78_000788 {ECO:0000313|EMBL:KAK3679227.1};
OS Recurvomyces mirabilis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Recurvomyces.
OX NCBI_TaxID=574656 {ECO:0000313|EMBL:KAK3679227.1, ECO:0000313|Proteomes:UP001274830};
RN [1] {ECO:0000313|EMBL:KAK3679227.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCFEE 5485 {ECO:0000313|EMBL:KAK3679227.1};
RA Coleine C., Stajich J.E., Selbmann L.;
RT "Black Yeasts Isolated from many extreme environments.";
RL Submitted (JUL-2023) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactate + 2 Fe(III)-[cytochrome c] = 2 Fe(II)-[cytochrome
CC c] + pyruvate + 2 H(+); Xref=Rhea:RHEA:19909, Rhea:RHEA-COMP:10350,
CC Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16651, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.1.2.3;
CC Evidence={ECO:0000256|ARBA:ARBA00052399};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19910;
CC Evidence={ECO:0000256|ARBA:ARBA00052399};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000256|ARBA:ARBA00004569}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the FMN-dependent
CC alpha-hydroxy acid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00061137}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the cytochrome b5
CC family. {ECO:0000256|ARBA:ARBA00061589}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAK3679227.1}.
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DR EMBL; JAUTXT010000002; KAK3679227.1; -; Genomic_DNA.
DR RefSeq; XP_064696620.1; XM_064835570.1.
DR AlphaFoldDB; A0AAE0WWD9; -.
DR GeneID; 89960103; -.
DR Proteomes; UP001274830; Unassembled WGS sequence.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0004460; F:L-lactate dehydrogenase (cytochrome) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006089; P:lactate metabolic process; IEA:TreeGrafter.
DR CDD; cd02922; FCB2_FMN; 1.
DR FunFam; 3.20.20.70:FF:000062; Cytochrome b2, mitochondrial, putative; 1.
DR FunFam; 3.10.120.10:FF:000012; Mitochondrial cytochrome b2, putative; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR000262; FMN-dep_DH.
DR InterPro; IPR037396; FMN_HAD.
DR InterPro; IPR008259; FMN_hydac_DH_AS.
DR InterPro; IPR037458; L-MDH/L-LDH_FMN-bd.
DR PANTHER; PTHR10578:SF148; L-LACTATE DEHYDROGENASE (CYTOCHROME); 1.
DR PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF01070; FMN_dh; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; Heme {ECO:0000256|ARBA:ARBA00022617};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KAK3679227.1};
KW Reference proteome {ECO:0000313|Proteomes:UP001274830}.
FT DOMAIN 10..87
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 113..475
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT REGION 284..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 503 AA; 55962 MW; AB088CF1B16E4E2B CRC64;
MNHSSNDTQA VKLTGEEVAK HNTREDCWVI INGRAYDVTE FMPEHPGGPK IILKYAGKDG
TEEYAPIHPP DTLDKYLDKS KHLGEVDMST VQQEEKKEDP DEAERQERIQ RMPILEQCYN
LMDFEAVARR VMKKTAWAYY SSGADDEITM RENHSAYHKI WFRPRVLVNV ESIDTSTTML
GTKVSIPFYV TATALGKLGN PEGEVVLTRG AKKHNVIQMI PTLASCSFDE IVDAKEGDQV
QWLQLYVNKD RAITKKIIEH AEKRGCKGLF ITVDAPQLGR REKDMRSKFS DVGSNVQNTG
GDNVDRSQGA ARAISSFIDP SLSWKDIPWF LSVTKMPILL KGVQRVEDVI QAIAAGVHGV
VLSNHGGRQL DFARSGIEVL AEVMPELRRL GLDKKIEIYV DGGVRRATDI IKALCLGATG
VGIGRPFLYA MSAYGLPGVD RAMQLLKDEM EMNMRLIGCS SVDELGPDLV DTRGLSMHTT
TITDTLGLNV YDPLVGPQEK ARL
//
