ID F0SKG1_RUBBR Unreviewed; 468 AA.
AC F0SKG1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=D-lactate dehydrogenase (Cytochrome) {ECO:0000313|EMBL:ADY61942.1};
DE EC=1.1.2.4 {ECO:0000313|EMBL:ADY61942.1};
GN OrderedLocusNames=Plabr_4369 {ECO:0000313|EMBL:ADY61942.1};
OS Rubinisphaera brasiliensis (strain ATCC 49424 / DSM 5305 / JCM 21570 / IAM
OS 15109 / NBRC 103401 / IFAM 1448) (Planctomyces brasiliensis).
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae; Rubinisphaera.
OX NCBI_TaxID=756272 {ECO:0000313|EMBL:ADY61942.1, ECO:0000313|Proteomes:UP000006860};
RN [1] {ECO:0000313|Proteomes:UP000006860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49424 / DSM 5305 / JCM 21570 / NBRC 103401 / IFAM 1448
RC {ECO:0000313|Proteomes:UP000006860};
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 Planctomyces brasiliensis DSM 5305.";
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 ---------------------------------------------------------------------------
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; CP002546; ADY61942.1; -; Genomic_DNA.
DR RefSeq; WP_013630647.1; NC_015174.1.
DR AlphaFoldDB; F0SKG1; -.
DR STRING; 756272.Plabr_4369; -.
DR KEGG; pbs:Plabr_4369; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_2_0; -.
DR OrthoDB; 9767256at2; -.
DR Proteomes; UP000006860; Chromosome.
DR GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IEA:UniProtKB-EC.
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 PANTHER; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR PANTHER; PTHR42934:SF1; GLYCOLATE OXIDASE SUBUNIT GLCD; 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 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:ADY61942.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006860}.
FT DOMAIN 44..222
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 468 AA; 50253 MW; BDF2F653D3E5C5B6 CRC64;
MSVTAPSSAP SALVSALRNV LPDAQILVDE AERLVYEADG YLVERRIPDL VVFPHSAEQL
AAVLKACQEQ KVSVIPRGAG TSLAGGCLPV GGGVMVCLSQ MRTIHEINLA DRYAIVDAGV
VNARLNQQLT GTGLHFAPDP SSAGASTIGG NVATNAGGPH TLKYGVTSNH VLGLEVVLAD
GRILQLGGVN GCGYDWDLAG LFTGSEGTLG FCTKAIVRLE LTPESWQTRL VIFDSLDDAV
RVVTDIIGAG IVPAALELMD QGMLTAIEDR YHHGLPTDAG AVLIIEVDGP CCATDAEIKA
IDTICDAGSC REIRKATTPA ERDALWKCRK QAFGAIGKLS TSFCTQDGVV PRTRLPELLR
HVLEVAEKYQ LKIFNVFHAG DGNIHPILLF DERDREQVQR VLDASGEILS KCLEFGGTVT
GEHGIGVEKL EFMTQMFDET DMMVFQNLRR IFDPDLRLAR GKLLPQVD
//
