ID B1Y4K0_LEPCP Unreviewed; 529 AA.
AC B1Y4K0;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:ACB33439.1};
GN OrderedLocusNames=Lcho_1170 {ECO:0000313|EMBL:ACB33439.1};
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Leptothrix.
OX NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB33439.1, ECO:0000313|Proteomes:UP000001693};
RN [1] {ECO:0000313|EMBL:ACB33439.1, ECO:0000313|Proteomes:UP000001693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC {ECO:0000313|Proteomes:UP000001693};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP001013; ACB33439.1; -; Genomic_DNA.
DR AlphaFoldDB; B1Y4K0; -.
DR STRING; 395495.Lcho_1170; -.
DR KEGG; lch:Lcho_1170; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_2_4; -.
DR OrthoDB; 8712194at2; -.
DR Proteomes; UP000001693; Chromosome.
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; 3.30.70.2740; -; 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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Reference proteome {ECO:0000313|Proteomes:UP000001693}.
FT DOMAIN 82..260
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 529 AA; 55824 MW; F1C33692D27AD736 CRC64;
MQSPAPCDTT GGSTGSLTAL VQADNATASS RETKQALLAQ EQLRAARQAE VLAALRGVLP
ASSLLSRNED TTPYECDGLT AYRQRPMLVV LPETDAQVAA VLRTCHALGV PVVARGAGTG
LSGGAMPHAL GVTMSLARLN KIVQLDAEAG FAVVQCGVRN LAISEAAAPH DLYYAPDPSS
QIACTIGGNV AENSGGVHCL KYGLTLHNVL QVKGYTAAGE PITFGSLASD APGLDLLSVV
VGSEGMLAVV TEVTVKLIPK PALARCIMAS FASVEAAGEA VAAVIAAGII PAGLELMDQR
MTAAVEDYVH AGYDLDAAAI LLCESDGTPE EVAEEIERMR EVLSGCGATR LEVSRDEAQR
LRFWSGRKNA FPASGRISPD YMCMDSTIPR KRLAEILRAI EAMEVTYGLR CANVFHAGDG
NLHPLIMFDA NDPDQLHRCE RFGADILETS VRLGGTVTGE HGVGVEKLNS MCVQFSPLEL
AQMLALKSAF DPAGVLNPGK AVPELHRCAE YGRMHVKRGL LPFPELPRF
//
