ID L0IDW4_HALRX Unreviewed; 476 AA.
AC L0IDW4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN OrderedLocusNames=Halru_1802 {ECO:0000313|EMBL:AGB16401.1};
OS Halovivax ruber (strain DSM 18193 / JCM 13892 / XH-70).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halovivax.
OX NCBI_TaxID=797302 {ECO:0000313|EMBL:AGB16401.1, ECO:0000313|Proteomes:UP000010846};
RN [1] {ECO:0000313|Proteomes:UP000010846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18193 / JCM 13892 / XH-70
RC {ECO:0000313|Proteomes:UP000010846};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA Anderson I., Woyke T.;
RT "Complete sequence of Halovivax ruber XH-70.";
RL Submitted (SEP-2011) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003050; AGB16401.1; -; Genomic_DNA.
DR AlphaFoldDB; L0IDW4; -.
DR STRING; 797302.Halru_1802; -.
DR KEGG; hru:Halru_1802; -.
DR eggNOG; arCOG00337; Archaea.
DR HOGENOM; CLU_017779_9_2_2; -.
DR OrthoDB; 26910at2157; -.
DR Proteomes; UP000010846; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
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:UP000010846}.
FT DOMAIN 39..218
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 447..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 476 AA; 50580 MW; DDA10C7949138812 CRC64;
MTYDIEFCFE LGLADDQISV SEGRRESHAA DWGASQLDEG VVPDVVVWPE STADVSALLA
AATDHGVPVT PYAAGTGLEG NAVPAHGGIS LDLMRLNAVV DYRPDDFQID VQPGLLGSAV
DEHVADDGRF FPPLPSSGNI STIGGMIATD ASGMQTVKYG EVADWVLGLE AVLADGTVIR
TGSRAVKTSS GYNLTELLIG SEGTLAVVTE VTLELAGRPA QKRGVRAIFE TLDAATAAVS
DTVRSGVDVA RIEVVDGLSA RMANAYQGSD LPDAPMVFLE FHANHGVDEE VALCRSIFEE
YALERFETDD DGTEMADLWA ARRDLAYAVA SYDADLDPLH PGDVTVPISA YPEIVRETKR
LADEADLLVP CFGHAGDGNL HYSVLVDRSD PPMVERGEEL YAAVVERAIE LGGTATGEHG
IGQGKREYLE PEHGDGAVDA MRSIKRALDP TGTLNPGKIF PETESGERVR DPVSEG
//
