ID C1G1S1_PARBD Unreviewed; 549 AA.
AC C1G1S1;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=L-lactate dehydrogenase (Cytochrome) {ECO:0008006|Google:ProtNLM};
GN ORFNames=PADG_02087 {ECO:0000313|EMBL:EEH45937.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH45937.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH45937.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH45937.2,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR EMBL; KN275958; EEH45937.2; -; Genomic_DNA.
DR RefSeq; XP_010757199.1; XM_010758897.1.
DR AlphaFoldDB; C1G1S1; -.
DR STRING; 502780.C1G1S1; -.
DR GeneID; 22581633; -.
DR KEGG; pbn:PADG_02087; -.
DR VEuPathDB; FungiDB:PADG_02087; -.
DR eggNOG; KOG0537; Eukaryota.
DR eggNOG; KOG0538; Eukaryota.
DR HOGENOM; CLU_020639_1_1_1; -.
DR InParanoid; C1G1S1; -.
DR OMA; WSYVAGG; -.
DR OrthoDB; 1887365at2759; -.
DR Proteomes; UP000001628; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02922; FCB2_FMN; 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 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001628}.
FT DOMAIN 3..80
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 109..477
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
SQ SEQUENCE 549 AA; 59138 MW; 048BAB0D4FA39CE9 CRC64;
MGGRNLNAAE VAKHNTRDSC WVVLYGKVYD VTDFLPNHPG GANIILQLAG KDATEEFDPV
HPSGTLEDNL KPEACLGPID PKTSLPKAAS YSAESNHQTG AEQAFNETPP MSSLLNINDI
EAAATQKLSK KAWGYYYSAA DDLMSKSLNN TIYRSILLRP RVFIDCTNCD LSTSVLGYKL
GLPIYVSPAA MARLAHPAGE AGIAAACSKF NAMQLISNNA SMTPKEIVAN AAPDQVFGWQ
LYVQTDRKKS EAMLARINKL KSIKFVCLTL DAPVPGKREH DERTQTVTQT SSVTDIVKAS
GGTPLPSASG IGQQLFAGTD PSLTWSKTLP WLARHTDLPI VLKGVQTHED AYIASLHGPQ
VKAIILSNHG GRAMDTAPPA VHTLMEIRKY CPEVFDRVEV WVDGGIKRGT DVVKALCLGA
RCVGVGRAPL FGLGAGGVEG VERVLEILSS ETKTAMHLLG VGRVEDLGMQ HINARAVEQQ
IYDGPAGLHA LGHFINRITL GNEEYVGNNL GYRLKRQEQG EISALNQESV DPAIENVLGE
EGKNGNKSR
//
