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Database: UniProt
Entry: A0A095E9G7_CRYGR
LinkDB: A0A095E9G7_CRYGR
Original site: A0A095E9G7_CRYGR 
ID   A0A095E9G7_CRYGR        Unreviewed;       593 AA.
AC   A0A095E9G7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=L-lactate dehydrogenase {ECO:0000313|EMBL:KGB74228.1};
GN   ORFNames=CNBG_0066 {ECO:0000313|EMBL:KGB74228.1};
OS   Cryptococcus gattii serotype B (strain R265) (Filobasidiella gattii)
OS   (Cryptococcus bacillisporus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus gattii species complex.
OX   NCBI_TaxID=294750 {ECO:0000313|EMBL:KGB74228.1, ECO:0000313|Proteomes:UP000029445};
RN   [1] {ECO:0000313|EMBL:KGB74228.1, ECO:0000313|Proteomes:UP000029445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R265 {ECO:0000313|EMBL:KGB74228.1};
RX   PubMed=21304167; DOI=10.1128/mBio.00342-10;
RA   D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA   Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA   McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA   Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA   Schein J., Krzywinski M., Kwon-Chung K.J., Varma A., Wang J., Brunham R.,
RA   Fyfe M., Ouellette B.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA   Birren B.W., Galagan J.E., Cuomo C.A.;
RT   "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT   immunocompetent hosts.";
RL   MBio 2:E342-E342(2011).
RN   [2] {ECO:0000313|EMBL:KGB74228.1, ECO:0000313|Proteomes:UP000029445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R265 {ECO:0000313|EMBL:KGB74228.1};
RX   PubMed=29507212;
RA   Yadav V., Sun S., Billmyre R.B., Thimmappa B.C., Shea T., Lintner R.,
RA   Bakkeren G., Cuomo C.A., Heitman J., Sanyal K.;
RT   "RNAi is a critical determinant of centromere evolution in closely related
RT   fungi.";
RL   Proc. Natl. Acad. Sci. 115:3108-3113(2018).
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR   EMBL; CP025762; KGB74228.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A095E9G7; -.
DR   STRING; 294750.A0A095E9G7; -.
DR   VEuPathDB; FungiDB:CNBG_0066; -.
DR   HOGENOM; CLU_020639_1_1_1; -.
DR   OMA; ANDDRDM; -.
DR   Proteomes; UP000029445; Chromosome 4.
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; IPR008259; FMN_hydac_DH_AS.
DR   InterPro; IPR037458; L-MDH/L-LDH_FMN-bd.
DR   PANTHER; PTHR10578:SF101; DEHYDROGENASE, PUTATIVE-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   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   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}.
FT   DOMAIN          88..167
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          204..593
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
SQ   SEQUENCE   593 AA;  65488 MW;  D7463FF4CEA165EE CRC64;
     MSIRTTVLQK AARLSRNRPV FARGLTSRIA PNTSSKTVSS KFLIGAGVAL AVPTYMYLNR
     AHLDSQQVVE TAVPDKPQAL EQEKKQEGKK VSIKEVLEHK DGDRVWVVIQ GHVYDMTDFL
     EDHPGGKDII AENRSKDVTF IFNPRHPSDQ LEADNLPPNV QHLGTLDTAS ASDEEKEKLK
     LKISKDEQDE TERIERKRKE IEEQGLGSVV NMRDFEKLAE DMCTSVGWAY YASAADDELT
     KNENNTSYRK IHFRPRVLRK VAEADASTTI LGYKSSLPVM ISPAAMAKLG HPLGEVNMTR
     GAANTGIIQC ISSFASCSLE EICAARSDNQ PLFFQLYVNS KRDLAAEVLK RVNRLNLNAI
     LLTVDAAVGG KRERDLRLKG NFEPPKTGAF EKHDDTKGVS EAMFAGVDPD LCWDDIKWIR
     SQTKLPLLIK GVQTVEDAIL AYRMGADGVV LSNHGGRQLD TTHTGIDTLL EIRKHAPYLL
     RPEYRGPIGL QPAALEHPEN LTPPDPQGKP TDRPFEIWVD GGIWRGSDAV KALCLGANAV
     GAGRGFLYAN AVGGQQGVEH AVNIFSAEIL TTMRLLGVNK VDQLRPSMVE IKE
//
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