ID V5HS90_BYSSN Unreviewed; 957 AA.
AC V5HS90;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=PVAR5_0875 {ECO:0000313|EMBL:GAD92285.1};
OS Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD92285.1, ECO:0000313|Proteomes:UP000018001};
RN [1] {ECO:0000313|Proteomes:UP000018001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA Oka T., Ekino K., Fukuda K., Nomura Y.;
RT "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL Genome Announc. 2:E0116213-E0116213(2014).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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:GAD92285.1}.
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DR EMBL; BAUL01000020; GAD92285.1; -; Genomic_DNA.
DR AlphaFoldDB; V5HS90; -.
DR eggNOG; KOG1231; Eukaryota.
DR eggNOG; KOG4777; Eukaryota.
DR HOGENOM; CLU_308352_0_0_1; -.
DR InParanoid; V5HS90; -.
DR OrthoDB; 1664005at2759; -.
DR Proteomes; UP000018001; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR005676; Asp_semi-ald_DH_pep-lack.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR NCBIfam; TIGR00978; asd_EA; 1.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748:SF111; D-LACTATE DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR Pfam; PF02774; Semialdhyde_dhC; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000018001}.
FT DOMAIN 138..315
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 32..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 957 AA; 104210 MW; 4CBE67E1B73A0A8F CRC64;
MKSSLLRGCP AKLPRHLRPL LRPQTACRSP LTCRGNSGSA NVKAPETSSG RTTSQSTFWT
TGRVLLFSAL ASGAAYAYAS SGAGSVTAKS SRQPQYGSLQ DMEKAIAELR IKLGEDTIST
DEDDLQEHGY SEWSTVNAER LPVAIAYPKS TEDVSEIAKV CSKYRMPMVP FSGGSSLEAN
FSAPYGGMTI DFAFMDRIIE LHEEDMDVVV QPSIQWMELN EQLKDTGLFF PVDPGPSAKI
GGMVGTNCSG TNAVRYGTMK DWVINLTVVL ADGRVIKTRK RPRKTSAGYN LTGLFVGSEG
TLGIVTEITL KLAATPEKTR VGVVSFPSIR EAASTAMQVI RKGVIVQSME ILDDVQMDVI
NRAGGTGRTW KKLPTLFFKF SGTSAGVDDS INLVKTIAKQ NKAQSFDFAK DDREAHDLWS
ARKQSLWSML ALRKEGSEVW STDVAVPISR LPDIIEVSKK EMDELGIFAS ILGHIGDGNF
HESIMYNRHD PVEKERVEKC VHDMVDRALE MEGSCTGEHG IGLGKKESLL KELGVDTIDI
MRSIKLSLDP QWIMNPGKIF DFSREVKTLD TSEVESARLT GAKRGDRSDH IGKMSSPVAK
KKCGVLGATG SVGQRFILLL ADHPFLVLHA VGASSRSAGK AYKDAVRWKQ SMPMSKQLGE
LVVRECTAEN FKDCDIVFSG LDSDVAGEVE MEFIRADIPV FSNAKNHRKN PIVPLVVPTV
NLQHLDLVHH QRKQLGMKKG FLVCNSNCAV IGVVIPFAAL QAKFGPVEYV EVFTEQAVSG
AGYPGVPSMD IMDNVIPFIS GEEDKLENEA QKILGSINAD ATAFEEQSDL KVGATCTRVG
VTDGHMAYVS LRFKNHPAPT AEQVKEAMRE YKSEAQKLGC HSAPEQAIVV FDEPDRPQPR
LDRNLSNGYA VSVGRVREAP AGGYFDLRFA CLSHNTVIGA AGSSILNAEA CVIKGLI
//
