ID H3A2W5_LATCH Unreviewed; 455 AA.
AC H3A2W5;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN Name=LDHD {ECO:0000313|Ensembl:ENSLACP00000003986.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000003986.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000003986.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR EMBL; AFYH01126547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01126548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01126549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01126550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01126551; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7897.ENSLACP00000003986; -.
DR Ensembl; ENSLACT00000004022.1; ENSLACP00000003986.1; ENSLACG00000003550.1.
DR eggNOG; KOG1231; Eukaryota.
DR GeneTree; ENSGT00940000158705; -.
DR HOGENOM; CLU_017779_3_0_1; -.
DR InParanoid; H3A2W5; -.
DR OMA; GQGFEWA; -.
DR TreeFam; TF314122; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000003550; Expressed in chordate pharynx and 6 other cell types or tissues.
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:1903457; P:lactate catabolic process; IEA:Ensembl.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2740; -; 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; IPR016171; Vanillyl_alc_oxidase_C-sub2.
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 SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672}.
FT DOMAIN 36..213
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 455 AA; 49859 MW; D98EA0D12687582F CRC64;
VTSKIIEALR AVVGSHNVST ATAVREQHGR DESVHRCQPP DAVVWPQDVK QVSELARVCN
QNHIPIIPFG TGTGLEGGVT AVTSPLSLXL SKMDRILDLN AEDFDVTVEP GVTRKTLNSY
LRDCGLWFPV GMSTVLDLCL TTAGGGGGGW EIRVEDHAIC RTFCFRVTFL FTTRQPMSQS
LKTAAGYNLT NLFVGSEGTL GIITKATLRL YGVPEAMVSA VCSFPSVQAA VSSTVQILQC
GIPIARIEFL DDVMMDACNR FSKLSYPISP TLFLEFHGTE NSLEEQVRLA EELTKGNGGS
DFAWARDQET RNWLWTARHN AWYAAKALRP GCKAYSTDVC VPISRLPEII VETKEDLVRS
KLTGPIAGHV GDGNFHCFMV LDPEDEDEER RVREFTDRLA RRALALSGTC TGEHGVGLGK
RALLAEEIGN PAMEVMKQIK STLDPHDIMN PQKVL
//
