ID A0A1J8QV42_9AGAM Unreviewed; 1177 AA.
AC A0A1J8QV42;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=AZE42_03039 {ECO:0000313|EMBL:OJA17257.1};
OS Rhizopogon vesiculosus.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX NCBI_TaxID=180088 {ECO:0000313|EMBL:OJA17257.1, ECO:0000313|Proteomes:UP000183567};
RN [1] {ECO:0000313|EMBL:OJA17257.1, ECO:0000313|Proteomes:UP000183567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM-OR11-056 {ECO:0000313|EMBL:OJA17257.1,
RC ECO:0000313|Proteomes:UP000183567};
RA Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA Barry K., Grigoriev I.V., Spatafora J.W.;
RT "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT divergence of the mating type B locus.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the universal ribosomal protein uL14 family.
CC {ECO:0000256|ARBA:ARBA00010745}.
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:OJA17257.1}.
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DR EMBL; LVVM01002142; OJA17257.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J8QV42; -.
DR STRING; 180088.A0A1J8QV42; -.
DR OrthoDB; 1664005at2759; -.
DR Proteomes; UP000183567; Unassembled WGS sequence.
DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 2.40.150.20; Ribosomal protein L14; 1.
DR HAMAP; MF_01367; Ribosomal_L14; 1.
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; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR000218; Ribosomal_uL14.
DR InterPro; IPR005745; Ribosomal_uL14_bac-type.
DR InterPro; IPR019972; Ribosomal_uL14_CS.
DR InterPro; IPR036853; Ribosomal_uL14_sf.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR NCBIfam; TIGR01067; rplN_bact; 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; PF00238; Ribosomal_L14; 1.
DR SMART; SM01374; Ribosomal_L14; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR SUPFAM; SSF50193; Ribosomal protein L14; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS00049; RIBOSOMAL_L14; 1.
PE 3: Inferred from homology;
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000183567};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980}.
FT DOMAIN 356..538
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 1177 AA; 130039 MW; C1E035E8611081B5 CRC64;
MIGLKSTLNV IDNSGALLIE CVNVLKQKVN NGWGSVGDEI VCIVKRARPV SAAAQASTTA
VKVRRGDVRR AVIVRTKKSV RRPDGRFIRF DDNAAVLLNN KREMLGTRIG GVVSADLRMK
GWGKIVSLAP KVCSSATPFQ QKPDRPLFRL FDATTAVVYY IPILISTIEF YGSSTSYLMC
GFDVYRALIL KYTAAAADTA SMKDFVCLLR YFRSLPFALD GATVVNTSPR MFPNCFRRLR
SSISLEINLA RSRTIRQHSL TFARPYSSSV PIGSSRSWSP IIIGSIASGF IGYSLSVFGT
PSLSSRAVGE AEPTYGTPKD FEQAIKELRA SIDSDEVVST HPEDLRVHGF SENDYHPSSP
HTVIVFPRNT EDVVKIVKTA VKYRMPITPF SGGTSLEGHY RGSSVGGICV DMSNMNKIIE
IHEADSDLVC QPGIGWMEIN EILQQKGIPL FFPLDPGPGA TIGGMMSTGC SGTNAVRYGT
AKGEWFLNAT VVLPSGEVIK TRQRARKSSA GFDATKLFIG AEGTLGIITE VTIRLAPVLP
TTVAVVHFPD VKHASEAVND VLNRGVGIQC VELCDSEFMR SVNLYGASQR KYPEQDSLFF
KFQGPTPASL AETAKIVKEI VQKHGGTGFE LARSEKEARD LWADRKNALY SGLALLEGSR
GWSTDVCVPV SKLPQLVYET KKDLEKVAIA SILVGHAGDG NFHTLLLFRN DEELAIVREA
VHRMVERAIK LEGTCTGEHG VGIGKREYLY EELGEGTVEL MRSIKKTVDP LGLFNPGKYI
SMMKEFGKKI LHGRLLSHRG INAKPITLSR VQLPLLLDYP EPLSITHSHP PSVDDSQSYI
NRLPVELLQQ IFLLIINDIP DYPCIFSVEG TTISANFNSP PLVFTRVCCR WRIIAHSTPD
VWSRIQVVLP GRVELKPFLP SLLQAWLARS GSRPLTLRIV SNRLPRLPHF PRPKIRYLSY
ADSQLADSQL IEILLSESWR WESATLMTSI YEWSHNFDTP QLRTLRCFLP DLSKFNAPNL
SRLCTSVLHV VDTNSEFNCT PTCKYIRHLH LREASTITMQ KILAMFPHLE TIVVNEIASP
YAYPSRGNPV TNSCLESMTL PLQPDGLHAI IDVLDELRLP KLQKLTVVGK LNQAGVDCIM
AVLAVPSCNV QVVDLQIGTA LDVDADMVEL WPCCPVP
//
