ID B8IW07_METNO Unreviewed; 480 AA.
AC B8IW07;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:ACL62597.1};
GN OrderedLocusNames=Mnod_8493 {ECO:0000313|EMBL:ACL62597.1};
OS Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OG Plasmid pMNOD01 {ECO:0000313|EMBL:ACL62597.1,
OG ECO:0000313|Proteomes:UP000008207}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL62597.1, ECO:0000313|Proteomes:UP000008207};
RN [1] {ECO:0000313|Proteomes:UP000008207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC {ECO:0000313|Proteomes:UP000008207};
RC PLASMID=Plasmid pMNOD01 {ECO:0000313|Proteomes:UP000008207};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Marx C.J.,
RA Richardson P.;
RT "Complete sequence of plasmid 1 of Methylobacterium nodulans ORS 2060.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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DR EMBL; CP001350; ACL62597.1; -; Genomic_DNA.
DR RefSeq; WP_015934136.1; NC_011892.1.
DR AlphaFoldDB; B8IW07; -.
DR KEGG; mno:Mnod_8493; -.
DR HOGENOM; CLU_017779_4_1_5; -.
DR OrthoDB; 9809290at2; -.
DR Proteomes; UP000008207; Plasmid pMNOD01.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
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; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 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 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Plasmid {ECO:0000313|EMBL:ACL62597.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008207}.
FT DOMAIN 32..214
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 480 AA; 49778 MW; 634B47F4EEB5F956 CRC64;
MLEKLAAIVG ASGILSSAAD MAPFVEDWRG LSQGEALCVV LPATPEQAAE VVRLCARTGT
PVLPQGGNTS LCGGAVPPSG GPRPVIVGLQ RLRRIRAIDP VNDTITVDAG CVLATVQATA
AEHGRLYAVS LGAEGSCQVG GTIATNAGGT GVLRYGNTRD NVLGLEVVLP DGTIWDGLTA
LRKNNTGYDL KHLFIGSEGT LGLITGAVLK LHPLPTARSV AWLSVAEPQA AIEALSLFRA
SCGSRLSAFE MINDSQAALV VKHVPGRRIP VTGGGWHVLV ELADTGNEAS LDAAMQAVLE
DALDRGLVTD AVVGASEAQR EALWAVRHGV SEANKKEGVS LTSDTAVPIS AVPAFIASAT
AAVRAIIPGL TVLVVAHLGD GNVHFIPFFS FAAWEVLAER EAIVQRIRHA VDDAAMALGG
TFSAEHGVGA THLPEMARYK PPVELAMMRA IKQAFDPSDL FNSGRLLPLR ATAPTSASHS
//
