ID A0A9P9R8C8_FUSRE Unreviewed; 440 AA.
AC A0A9P9R8C8;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 10.
DE RecName: Full=L-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00068515};
DE EC=1.1.2.3 {ECO:0000256|ARBA:ARBA00066458};
GN ORFNames=BKA55DRAFT_550663 {ECO:0000313|EMBL:KAH7270126.1};
OS Fusarium redolens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium redolens species complex.
OX NCBI_TaxID=48865 {ECO:0000313|EMBL:KAH7270126.1, ECO:0000313|Proteomes:UP000720189};
RN [1] {ECO:0000313|EMBL:KAH7270126.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MPI-CAGE-AT-0023 {ECO:0000313|EMBL:KAH7270126.1};
RA Mesny F., Miyauchi S., Thiergart T., Pickel B., Atanasova L., Karlsson M.,
RA Huettel B., Barry K.W., Haridas S., Chen C., Bauer D., Andreopoulos W.,
RA Pangilinan J., LaButti K., Riley R., Lipzen A., Clum A., Drula E.,
RA Henrissat B., Kohler A., Grigoriev I.V., Martin F.M., Hacquard S.;
RT "Genetic determinants of endophytism in the Arabidopsis root mycobiome.";
RL Nat. Commun. 0:0-0(2021).
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: Belongs to the cytochrome b5 family.
CC {ECO:0000256|RuleBase:RU362121}.
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:KAH7270126.1}.
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DR EMBL; JAGMUX010000001; KAH7270126.1; -; Genomic_DNA.
DR RefSeq; XP_046056894.1; XM_046191291.1.
DR AlphaFoldDB; A0A9P9R8C8; -.
DR GeneID; 70221245; -.
DR OrthoDB; 1925334at2759; -.
DR Proteomes; UP000720189; Unassembled WGS sequence.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004460; F:L-lactate dehydrogenase (cytochrome) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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 PANTHER; PTHR10578:SF82; CYTOCHROME B2, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G07200)-RELATED; 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; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU362121};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362121};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362121};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000720189}.
FT DOMAIN 2..79
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 103..440
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT REGION 78..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 440 AA; 47913 MW; C44E9E6715EDF867 CRC64;
MAKVFDAAEV AKHNTPESCW VILYGKVYDV TEFLPSHPGG KKIILKLAGK DATDEYDPVH
PPGTLEENLK PENILGEVNP ETLTDSQLTG EDTTRQSRDD QPPPMASLMN LDEIEEEATK
RISKKAWAYY FSAADDLFSK NYNNYVYKNI LLRPRVFVDC TACDLSTTLI GNKVGLPIFV
APAAMARLAH PDGEQGIAKA CSRFGAMQIV SNNASMTPEQ IIEGAKPGQT FGWQLYVQNQ
REKSEAMLKR INSMREYYKF ICLTLDAPVP GKRELDEKQN FDYSEPSPAS GESKPGAGGV
GQQLFFGTAA DLTWKTTLPW LAAHTDLPIV LKGLQTHEDA YLAAKYAPQV KAIILSNHGG
RAADTAPPAI HTLLEIRKYC PEILSKVQIW VDGGIKRGTD VVKALCLGAS GVGIGRGALF
GLGAGGQAGV ERTLESKLSL
//
