ID C3MKH9_SULIL Unreviewed; 467 AA.
AC C3MKH9;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:ACP36350.1};
DE EC=1.1.2.4 {ECO:0000313|EMBL:ACP36350.1};
GN OrderedLocusNames=LS215_2374 {ECO:0000313|EMBL:ACP36350.1};
OS Sulfolobus islandicus (strain L.S.2.15 / Lassen #1).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=429572 {ECO:0000313|EMBL:ACP36350.1, ECO:0000313|Proteomes:UP000001747};
RN [1] {ECO:0000313|EMBL:ACP36350.1, ECO:0000313|Proteomes:UP000001747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L.S.2.15 / Lassen #1 {ECO:0000313|Proteomes:UP000001747};
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001399; ACP36350.1; -; Genomic_DNA.
DR RefSeq; WP_012714267.1; NC_012589.1.
DR AlphaFoldDB; C3MKH9; -.
DR GeneID; 7798359; -.
DR KEGG; sis:LS215_2374; -.
DR HOGENOM; CLU_017779_9_2_2; -.
DR OrthoDB; 26910at2157; -.
DR Proteomes; UP000001747; 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 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 Oxidoreductase {ECO:0000313|EMBL:ACP36350.1}.
FT DOMAIN 31..203
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 467 AA; 51427 MW; 3B992F30F3CA53B7 CRC64;
MIEKLAEIVG EEWVISSDEA KLYSYPAFIP LKIEPPLVVL PGSEEEVISL VNFLNENNIK
YLVRGSGTSL SGATTPTQGE VIISLTRLNR IYSLDNFEIT VGPGLANFLI NKTLSNPNLF
YAPDPSSYVV SSIGGNISHD SGGMHTPKYG TTFDSVIKLR VLLSDGKVEE IGGNNFFDPT
SIFVGAEGTL GVILRATLRL FPKPEVSKTL LAAFNSIDNA GKAVVSVYKS GVTPAAMEFL
DKNSIIAIEN TQYKANYPMA EAILLIELDG YSANVEEEEA RVVKVVRENN GEVFIPKDDE
EKNRWWWGRK GAFPSFAYYS PAYLTLDANV PRSTLPTMLR FTYEIGKKYG LPVANSFHAG
DGTLHPLIGF DPKNVDETIN AIKAAEEITK LAIKLGGVPS GEHGIGIEKI KFMKLYYSED
DLTLMRRLKT VFDSKRLLNP CKLVPPAKNE ICNTVNRVHT YLLEGDI
//
