ID B0RGU3_CLAMS Unreviewed; 475 AA.
AC B0RGU3;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:CAQ01277.1};
GN OrderedLocusNames=CMS1162 {ECO:0000313|EMBL:CAQ01277.1};
OS Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744
OS / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Clavibacter.
OX NCBI_TaxID=31964 {ECO:0000313|EMBL:CAQ01277.1, ECO:0000313|Proteomes:UP000001318};
RN [1] {ECO:0000313|EMBL:CAQ01277.1, ECO:0000313|Proteomes:UP000001318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1
RC {ECO:0000313|Proteomes:UP000001318};
RX PubMed=18192393; DOI=10.1128/JB.01598-07;
RA Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA Parkhill J., Ishimaru C.A.;
RT "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT sepedonicus suggests recent niche adaptation.";
RL J. Bacteriol. 190:2150-2160(2008).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; AM849034; CAQ01277.1; -; Genomic_DNA.
DR RefSeq; WP_012298558.1; NZ_MZMN01000003.1.
DR AlphaFoldDB; B0RGU3; -.
DR STRING; 31964.CMS1162; -.
DR KEGG; cms:CMS1162; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_2_11; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000001318; 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 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:SF2; 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;
FT DOMAIN 50..229
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 475 AA; 48747 MW; 17548306AED71802 CRC64;
MIDDDVIRTP HTPADADAVR AELVAALGDV VATDPASLED ARSDRSGYRS PAAPIAVVHA
TEVDHVVTTL RIASATGTPV VTRGAGTGLA GGATATAGEI VLSVRGMDRI LEVSEADELA
VVEPGVLNDD LNARLAPLGL WYSPDPASKA ISTIGGNIAT NAGGLLCAKY GVTREAVLAL
TVVLADGRVV DTGHRTVKGV TGYDLTALMI GSEGTLGVLV RATVRLRPLP TATPSTVAAF
FPDSASAAAA ASAITAARIR PAAMELLDGG ALEAIDAFLG TDHSTRGSAH LLVRCDGPDA
ADEAARVVEV VVAGGGTADV TDDADEGERL LAIRRAFHPA LAARGRVLIE DVAVPRSRLA
DMLTRIREIE RETGLAIPTV AHAGDGNLHP NFLLPEDPTT PDGDATGIPD AVWHAADLLF
HAAVDLGGTL TGEHGVGLLK RRWLADELGD DVMGLAAGIR RVFDPQGILN PGKAA
//
