ID A0A0M2HFI3_9MICO Unreviewed; 419 AA.
AC A0A0M2HFI3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative xylitol oxidase {ECO:0000313|EMBL:KJL43018.1};
DE EC=1.1.3.41 {ECO:0000313|EMBL:KJL43018.1};
GN Name=xyoA {ECO:0000313|EMBL:KJL43018.1};
GN ORFNames=RS81_00982 {ECO:0000313|EMBL:KJL43018.1};
OS Microbacterium ketosireducens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=92835 {ECO:0000313|EMBL:KJL43018.1, ECO:0000313|Proteomes:UP000033956};
RN [1] {ECO:0000313|EMBL:KJL43018.1, ECO:0000313|Proteomes:UP000033956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12510 {ECO:0000313|EMBL:KJL43018.1,
RC ECO:0000313|Proteomes:UP000033956};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KJL43018.1}.
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DR EMBL; JYIZ01000039; KJL43018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2HFI3; -.
DR STRING; 92835.RS81_00982; -.
DR PATRIC; fig|92835.4.peg.1002; -.
DR Proteomes; UP000033956; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050582; F:xylitol oxidase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2520; -; 1.
DR Gene3D; 3.30.70.2530; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR007173; ALO_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; IPR010031; FAD_lactone_oxidase-like.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR43762; L-GULONOLACTONE OXIDASE; 1.
DR PANTHER; PTHR43762:SF1; L-GULONOLACTONE OXIDASE; 1.
DR Pfam; PF04030; ALO; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR PIRSF; PIRSF000136; LGO_GLO; 2.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KJL43018.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033956};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 156..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..177
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 419 AA; 45079 MW; 8BAD03F7C7DCBC56 CRC64;
MSVARNWAGT HTYAAPRIVE ARSIDDVRRA VAETAPGPVH ALGTRHSFTD LPDTTGTLID
VTGIAPVFDL DEDARTVTVG AGTRYGVLAL WLHERGWALP NMGSLPHINV AGAAATGTHG
SGDGNRVLSA SVRALRYVGA DAEVHEVRAG DPDFDALVVG LGAFGVIVSV TLAIVPGFRL
RQDMYSGVTW DAALSDLDAV TGAGYSVSVF STWSPETLGV VWVKSRLDRD DDAIAETLLD
GRVDPDADPL PGLVDVTERG GVPGPWMLRL PHFRLDGEPS FGDEIQSEYF VSRADAPAAL
EAVRALGDGI RPLLFVTELR TMAGDDLWLS PAYRQNALAI HFTWFNRPDE VAAVLPAIEA
ALAPFGARPH WGKAHGFDRV AMERVHPRLG DARAVFERLD PDGRFVNDHL VRVGVREAR
//
