ID A0A074WXW0_9PEZI Unreviewed; 460 AA.
AC A0A074WXW0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=L-lactate dehydrogenase {ECO:0000313|EMBL:KEQ74582.1};
GN ORFNames=M436DRAFT_71994 {ECO:0000313|EMBL:KEQ74582.1};
OS Aureobasidium namibiae CBS 147.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ74582.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ74582.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ74582.1,
RC ECO:0000313|Proteomes:UP000027730};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR EMBL; KL584707; KEQ74582.1; -; Genomic_DNA.
DR RefSeq; XP_013428742.1; XM_013573288.1.
DR AlphaFoldDB; A0A074WXW0; -.
DR STRING; 1043004.A0A074WXW0; -.
DR GeneID; 25415038; -.
DR HOGENOM; CLU_020639_1_1_1; -.
DR OrthoDB; 1887365at2759; -.
DR Proteomes; UP000027730; Unassembled WGS sequence.
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; IPR000262; FMN-dep_DH.
DR InterPro; IPR037396; FMN_HAD.
DR InterPro; IPR037458; L-MDH/L-LDH_FMN-bd.
DR PANTHER; PTHR10578:SF104; CYTOCHROME B2-LIKE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07020)-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; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000027730}.
FT DOMAIN 1..78
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 100..450
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
SQ SEQUENCE 460 AA; 50594 MW; 716DEF3850F90354 CRC64;
MAIVEGAELV KHNSRQSCWL AIHGEVWDAT NFLEQHPGGA NLILNVAGTD ASDEYELFHN
AELVQETLGS DAKMGTIDVL SILPKMDKKP DPVLEVKKSP PLSSMISVDD FEKVAEKTMT
PTAWAYVSSG ADDEISMREN STAYQKVFLR GRILRKVGRV DCSTNILGYH STLPIYTSPV
GLAKLVHPSG ECAIAAAAGN MPIEDIMGAR IAQDQVIFWQ LYADKDLEKS KTFIKRVERA
GVSAIWLTVD SPVVGNRERD ERSKSVVDIE EKLEEIVETP QSIGIAKANT GFINADLDWN
MIDWLRKSTR LPIVIKGIQS VEDAVSAFHH KVDGIVLSNH GGRSQDTAQP PLLTLLEIDQ
YAPHILGKHM QVFVDGGIRR GTDIIKALAL GATAVGIGRP VLYSMSGGYA EHGIRRMIQI
LRNELQTNMA FIGASNVKEI ERSMVNTRKL ERMMVGSVKL
//
