ID U6STQ3_9BACI Unreviewed; 452 AA.
AC U6STQ3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=A33I_03775 {ECO:0000313|EMBL:ERN55069.1};
OS Alkalihalophilus marmarensis DSM 21297.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalihalophilus.
OX NCBI_TaxID=1188261 {ECO:0000313|EMBL:ERN55069.1, ECO:0000313|Proteomes:UP000017170};
RN [1] {ECO:0000313|EMBL:ERN55069.1, ECO:0000313|Proteomes:UP000017170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21297 {ECO:0000313|EMBL:ERN55069.1,
RC ECO:0000313|Proteomes:UP000017170};
RX PubMed=24285666;
RA Wernick D.G., Choi K.Y., Tat C.A., Lafontaine Rivera J.G., Liao J.C.;
RT "Genome Sequence of the Extreme Obligate Alkaliphile Bacillus marmarensis
RT Strain DSM 21297.";
RL Genome Announc. 1:e00967-e00913(2013).
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:ERN55069.1}.
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DR EMBL; ATAE01000003; ERN55069.1; -; Genomic_DNA.
DR RefSeq; WP_022626574.1; NZ_ATAE01000003.1.
DR AlphaFoldDB; U6STQ3; -.
DR PATRIC; fig|1188261.3.peg.162; -.
DR Proteomes; UP000017170; Unassembled WGS sequence.
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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128}.
FT DOMAIN 34..211
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 452 AA; 49423 MW; CFFB49A29575EEF0 CRC64;
MDHVKELSKL LTEDQVTTNQ TMREQHSRDE SYHIPSLPDM VIFPKRTEDV QKVINYANTY
EIPVVPFGLG SSLEGNAIPY KGGISLDMSL MNQVLEVRPN DFLIKVQPGI TRLQLNKELK
KYGLFFTVDP GADATLGGMA ATNASGTTSV RYGIMRDQVR DLEVVLASGE VIHTGGLSAK
SSSGLHLNGL MVGSEGTLGV ITELTLKVHG IPECIMAARA TFPDPGRAVE AVTSILAANI
PVARMEFVDE HSIRQVNIAN ERNYELKPTL FLEFHGNEAG LKQDVEFMKE IVSDLGCMDI
HFEMDTKSRA ELWEARHNLA YSFIHGHPGK KLMVTDVSLP ITELAGAILH ARESIENTGL
VGAVVGHVGD GNYHALVMVD LADQAEVEKA KELNELIVLY ALERGGTCTG EHGVGVGKVK
YQQKEHGAAY EVMKSIKHTL DPKGIMNPGK IF
//
