ID A0A0P1G3I2_9RHOB Unreviewed; 461 AA.
AC A0A0P1G3I2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=TRM7557_00773 {ECO:0000313|EMBL:CUH76219.1};
OS Tritonibacter multivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tritonibacter.
OX NCBI_TaxID=928856 {ECO:0000313|EMBL:CUH76219.1, ECO:0000313|Proteomes:UP000052022};
RN [1] {ECO:0000313|EMBL:CUH76219.1, ECO:0000313|Proteomes:UP000052022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7557 {ECO:0000313|EMBL:CUH76219.1,
RC ECO:0000313|Proteomes:UP000052022};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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}.
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DR EMBL; CYSD01000012; CUH76219.1; -; Genomic_DNA.
DR RefSeq; WP_058288874.1; NZ_JAQIPA010000005.1.
DR AlphaFoldDB; A0A0P1G3I2; -.
DR STRING; 928856.SAMN04488049_1037; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000052022; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 Oxidoreductase {ECO:0000313|EMBL:CUH76219.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052022}.
FT DOMAIN 39..216
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 461 AA; 49627 MW; 4D3F82645D47F25C CRC64;
MTQDTISLAL SELRALLGDR LSTGQSVREI HGRDEAYSEP ALPDAVAFPD NTEEVSAIMK
ICSAHKVPVV PFGIGTSLEG HVIPIHGGIS VDTSRMNKVL DIHQSDLDAV VQPGVTRKQL
NDDLRATGLM FTVDPGANAT LGGMTSTRAS GTNTVRYGTM RENVMALEVV LPDGRVINTG
SRARKSSAGY DLTHLFVGSE GTLGIITELT VRLFGRPDSE LSATCAFDTI DDAVNTVITA
IQMGLPMARI ELLDDVQMKG MNIFNPDLNL PEKPHLFIEF HGSEAGVKEQ VDLFESVAEE
FGVSGFDWAT KLEDRERLWQ ARHNAYYAGK SLRKGCEGLV TDCCVPISAL ADCIARTKEL
IAESGLIAPI VGHVGDGNYH LLILVDPDNG DEMARAKQLA SDVSRTALSF GGTVTGEHGV
GTGKKKYMPE EHGEAYLLMA QLKQSIDPLN IMNPGKLVSV N
//
