ID   A0A1R3T312_9BACT        Unreviewed;       942 AA.
AC   A0A1R3T312;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-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=PSM36_3296 {ECO:0000313|EMBL:SCD22081.1};
OS   Proteiniphilum saccharofermentans.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC   Proteiniphilum.
OX   NCBI_TaxID=1642647 {ECO:0000313|EMBL:SCD22081.1, ECO:0000313|Proteomes:UP000187464};
RN   [1] {ECO:0000313|EMBL:SCD22081.1, ECO:0000313|Proteomes:UP000187464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M3/6 {ECO:0000313|EMBL:SCD22081.1};
RA   Seilhamer J.J.;
RL   Submitted (AUG-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}.
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DR   EMBL; LT605205; SCD22081.1; -; Genomic_DNA.
DR   RefSeq; WP_076931784.1; NZ_LT605205.1.
DR   AlphaFoldDB; A0A1R3T312; -.
DR   STRING; 1642647.PSM36_3296; -.
DR   KEGG; psac:PSM36_3296; -.
DR   Proteomes; UP000187464; Chromosome i.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_dom.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR009051; Helical_ferredxn.
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; PF02754; CCG; 2.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187464}.
FT   DOMAIN          36..264
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          528..559
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   942 AA;  104387 MW;  2AA6F50BCA74C873 CRC64;
     MEVKQLRNRL LQLLPQDQVF TDELSRLVKG TDAGLYRLIP KAVVRVNSED EVIRLLEFCR
     TENMPVTFKA AGTSLSGQTI SDSILMEAGN GFEFSTITDK GATATFGCAL TGAAANRILI
     RYKRKLGPKP ASINSAKIGG IIANNASGSS YGIRYNSYNT IRSMRIIFAD GSLLDTADKE
     SCRAFIADHP QLIAEIEQLH KETVNNEAIR EKITSKFQLK NTCGYGVNSL IDFSDPIQII
     QHLMIGSEGT LGFVSQATFE TVHDAPLKAT AMIYFSNLHD VSNTIIPLRS CQVSAAELMD
     RNALRAVEDQ EGMPEELRSL PEGAAALLID TSADDEGTLL AQMAEIEEKL AHIDTLTPIR
     FTTDKHLYNL YWNVRNGLFT SAAATRPPRT ASIIEDIAFR AESLGDALTD VRELLVRTGY
     GNAVMWGHLL DGNVHFTVFP DINVPEEVEK YAVFMQELCE LVAVKHNGSL KAEHGTGRNM
     APFVEKEWGG EVYGLMKRIK KAFDPENILN PGVLINDDHE IFIKNLKRIP EANPIIDKCI
     ECGFCEVSCP SKDLTLTPRQ RIIAYRHLSE QAVSGNKKKD PVQEQLRNIS YPMEETCATD
     GLCGIACPVG IDTGKLIKEL RWQQNNRLAN RVADTIADNM AGMTSLLRRL LPIPHYIGKS
     VGYRTMESVT KGLYRLGDGA FPLWTRHTPS GSKKIKRNIF PATNPDAPMV VYFPACITRA
     MGGPSSGYEE KEDIPQKMLS VLKKAGYAVI IPEGKDDLCC GMAFSSKGFR KQAQKKENEL
     NEALLKASRN GELPIVCDMS PCLLHMRETL DKRLRLYDQV EFIHDFLLDR LQFTLQPISI
     AIHTTCSSTK MHLEEKLRAV ASRCAEKVII PENINCCGWA GDRGFFYPEL NNSALAPLRQ
     GIRDATEGYS NSRTCEIGLS INSGISYKSM IYLVDKASSG KS
//