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Database: UniProt
Entry: E1IHB4_9CHLR
LinkDB: E1IHB4_9CHLR
Original site: E1IHB4_9CHLR 
ID   E1IHB4_9CHLR            Unreviewed;       479 AA.
AC   E1IHB4;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=D-lactate dehydrogenase (Cytochrome) {ECO:0000313|EMBL:EFO79589.1};
GN   ORFNames=OSCT_2715 {ECO:0000313|EMBL:EFO79589.1};
OS   Oscillochloris trichoides DG-6.
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Oscillochloridaceae; Oscillochloris.
OX   NCBI_TaxID=765420 {ECO:0000313|EMBL:EFO79589.1, ECO:0000313|Proteomes:UP000054010};
RN   [1] {ECO:0000313|EMBL:EFO79589.1, ECO:0000313|Proteomes:UP000054010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG-6 {ECO:0000313|EMBL:EFO79589.1,
RC   ECO:0000313|Proteomes:UP000054010};
RX   PubMed=21037015; DOI=10.1128/JB.00931-10;
RA   Kuznetsov B.B., Ivanovsky R.N., Keppen O.I., Sukhacheva M.V.,
RA   Bumazhkin B.K., Patutina E.O., Beletsky A.V., Mardanov A.V., Baslerov R.V.,
RA   Panteleeva A.N., Kolganova T.V., Ravin N.V., Skryabin K.G.;
RT   "Draft genome sequence of the anoxygenic filamentous phototrophic bacterium
RT   Oscillochloris trichoides subsp. DG-6.";
RL   J. Bacteriol. 193:321-322(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:EFO79589.1}.
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DR   EMBL; ADVR01000112; EFO79589.1; -; Genomic_DNA.
DR   RefSeq; WP_006563278.1; NZ_GL501404.1.
DR   AlphaFoldDB; E1IHB4; -.
DR   STRING; 765420.OSCT_2715; -.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_017779_9_2_0; -.
DR   OrthoDB; 9767256at2; -.
DR   Proteomes; UP000054010; 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; 3.30.70.2190; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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; IPR016167; FAD-bd_PCMH_sub1.
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; 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   Reference proteome {ECO:0000313|Proteomes:UP000054010}.
FT   DOMAIN          37..215
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   479 AA;  50944 MW;  456CBACA6B70417D CRC64;
     MHRPDLIDEL RRIVGLRGVV ADPHALMTYD ADGCVLDTGN PVVVVLPTTT EQVSAVVRLA
     ARAGLPLVPR GAGTGLTGGA TAMSGGIMIS SARMDKILEV DVRNGRVLCQ PGVINYELSQ
     YLKPYGFQFA PDPSSQKACT VGGNIANNSG GPHCLKYGIT ASHVYGVEMV LADGTVMWSG
     DGSPAPPGYD LTGVITGSEG TFGMVTAAWL KLTRLPEAVR VVLALFPDIA GASSTVSQVI
     ASGLLPAALE IMDRLAIKAV NEMYRLGLPE QAGAALLIEV DGVEDGLDEL LHDVTAICWR
     NGALDVRPAR TQAEQNQVWA ARKNAFGAMG RLAPTYYLVD TVVPRTRLPY TMEQVGKISR
     TFDLPIANVF HAGDGNLHPI ILFDRRNRSQ NQRALEAASG VLQVSIEQGG VISGEHGIGV
     EKRDYMTLLF STEDLAAMAG LHQSFDPHDL FNPGKIFPKG RGCGELAALR RSGLRGEVA
//
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