ID A0A9P8VGP7_9PEZI Unreviewed; 496 AA.
AC A0A9P8VGP7;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, 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 ORFNames=F5X68DRAFT_149827 {ECO:0000313|EMBL:KAH6691708.1};
OS Plectosphaerella plurivora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Plectosphaerella.
OX NCBI_TaxID=936078 {ECO:0000313|EMBL:KAH6691708.1, ECO:0000313|Proteomes:UP000770015};
RN [1] {ECO:0000313|EMBL:KAH6691708.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MPI-SDFR-AT-0117 {ECO:0000313|EMBL:KAH6691708.1};
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:KAH6691708.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JAGSXJ010000005; KAH6691708.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9P8VGP7; -.
DR OrthoDB; 1925334at2759; -.
DR Proteomes; UP000770015; 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 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; IPR037458; L-MDH/L-LDH_FMN-bd.
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:UP000770015}.
FT DOMAIN 2..79
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 105..474
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT REGION 286..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 496 AA; 54071 MW; D21C385610EB9374 CRC64;
MAKVFEADEV AKHNTRESCW VVLYGNVYDV TDFLSEHPGG AKIILKLAGK DATEEYDPVH
PPGTLEDNLK PEAKLGSINP ESLARSEAKA AASASVQAAD ENTPVRLETL LNIDDIEQAA
TKRISKKAHA YYFSAGDDLF SKSFNNQVYR RILLRPRVFV DCTSCDSSTT ILGHKVDLPI
FVAPAAMARL AHPDGERGIA KAAARFGAMQ CISNNASMTP EQIVEGAIPG QMFGWQLYVQ
NERKKSEAML RRIHAMPDQY KYICLTLDAP VPGKRELDER QQFEGAFTVE SESNSKDTSE
TRPGGGGVGQ QLFFGTAADL TWKTTLPWLA KHTHLPIVLK GLQTHEDAYL AAQHAPQVKA
IILSNHGGRA LDTAPPAVHT LLEIRKYCPE VFSKIEVWVD GGIKRGTDVV KALCLGATAV
GVGRAALFGL GAGGQQGVER MFEILKGETE TCMRLLGAKT VADLGPRFIN TRAVEQDIYD
GEPGLDKQGL WTKSKL
//
