ID F0S8T1_PSESL Unreviewed; 939 AA.
AC F0S8T1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN OrderedLocusNames=Pedsa_1858 {ECO:0000313|EMBL:ADY52412.1};
OS Pseudopedobacter saltans (strain ATCC 51119 / DSM 12145 / JCM 21818 / CCUG
OS 39354 / LMG 10337 / NBRC 100064 / NCIMB 13643) (Pedobacter saltans).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pseudopedobacter.
OX NCBI_TaxID=762903 {ECO:0000313|EMBL:ADY52412.1, ECO:0000313|Proteomes:UP000000310};
RN [1] {ECO:0000313|EMBL:ADY52412.1, ECO:0000313|Proteomes:UP000000310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51119 / DSM 12145 / JCM 21818 / LMG 10337 / NBRC 100064 /
RC NCIMB 13643 {ECO:0000313|Proteomes:UP000000310};
RX PubMed=22180808; DOI=10.4056/sigs.2154937;
RA Liolios K., Sikorski J., Lu M., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Huntemann M., Ivanova N., Pagani I., Mavromatis K., Ovchinikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M.,
RA Kotsyurbenko O., Rohde M., Tindall B.J., Abt B., Goker M., Detter J.C.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA Kyrpides N.C.;
RT "Complete genome sequence of the gliding, heparinolytic Pedobacter saltans
RT type strain (113).";
RL Stand. Genomic Sci. 5:30-40(2011).
RN [2] {ECO:0000313|Proteomes:UP000000310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51119 / DSM 12145 / JCM 21818 / LMG 10337 / NBRC 100064 /
RC NCIMB 13643 {ECO:0000313|Proteomes:UP000000310};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Lu M.,
RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Tindall B., Pomrenke H.G., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Pedobacter saltans DSM 12145.";
RL Submitted (FEB-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}.
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DR EMBL; CP002545; ADY52412.1; -; Genomic_DNA.
DR RefSeq; WP_013632900.1; NC_015177.1.
DR AlphaFoldDB; F0S8T1; -.
DR STRING; 762903.Pedsa_1858; -.
DR KEGG; psn:Pedsa_1858; -.
DR eggNOG; COG0247; Bacteria.
DR eggNOG; COG0277; Bacteria.
DR eggNOG; COG0479; Bacteria.
DR HOGENOM; CLU_013688_0_0_10; -.
DR OrthoDB; 9767256at2; -.
DR Proteomes; UP000000310; Chromosome.
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; 3.30.70.2190; -; 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; 1.
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:UP000000310}.
FT DOMAIN 33..261
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 527..556
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 939 AA; 103961 MW; 1A2F7F7E770A6A4F CRC64;
MNIGELLKAI IPADRIKDRL IDVVSYAADA GFYHLTPKAV VRPIAVDEVI ALFRFSHQHQ
VPMTFRTGGT SLSGQSITDG ILVDLSQYWD KAHVENGGLQ IRVQPGIIGA AVNNKLKSFG
KKIGPDPSSI NSAMMGGILS NNSSGMCCGV HANSYHTTKY IKFVLPNGKC FSTENQSDYE
RFEKECNDIF ETLTGLRSQI ISNPDLFNII RHKYQTKNTV GYSVNSFIDY EHPLDILAHL
LIGGEGTLGF IAEAVMNTVD DYKEKSTALL YFPDIYEACK AIIPLTASGA EAVELMDRAS
LRSIEHIKGV PDILKTLPEA AAALLIEYQA NTNDELNVKI NQFLSLSEEL SLLSPAVFTQ
VPGEQAFLWT LRKGMFPSVG AVRASGSTVI LEDIAFPVET LGDAILDLQK LFKAYDYTNA
IIFGHAKDGN IHFVVTQSFQ SQQEIERYDR FLKDVVLLVV EKYRGTLKAE HGTGRNMAPF
IATEWGTEIY AIMKRLKEVI DPKNLLNPGV IINDNTKAHI TNLKDLPTVE HEVDKCMECG
YCEHVCPSRN ITLTPRRRIV VRRELTILKK KGEKAKYEEL LDQYQYDGLD TCAVDGLCAS
ACPVDINTGD LVKRLRRENH SDFANSVALQ IAKNFAFASS ATEFGVKAAN GINGVLGGNA
LTKITKAVKE VIPAIPQWSN QIKSTGNITS KYKQQSVDAV VYMPTCISRM MGGAAIDGKK
NIIDTIASIS AKVGISFKIP DKIGSMCCGQ MFSSKGYQKA FEYSVNRTVE QIWEESNKGQ
LPVMLDVSSC THTLQGARNY LTEENKKRLD TLRIIDSIEY IDEFIIPRVS LQRKKQRIVL
HPVCSLKKMG LNAKFKKVAD FFAEEVVMPF NANCCGMAGD RGFLFPELTQ SATEMEAREI
NTCGSFDGYY SSSKTCEMSL SDAVGKNYES IVYLVDDCI
//
