ID B2HSS0_MYCMM Unreviewed; 428 AA.
AC B2HSS0;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:ACC41094.1};
GN OrderedLocusNames=MMAR_2648 {ECO:0000313|EMBL:ACC41094.1};
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC41094.1, ECO:0000313|Proteomes:UP000001190};
RN [1] {ECO:0000313|EMBL:ACC41094.1, ECO:0000313|Proteomes:UP000001190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
CC -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005147}.
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DR EMBL; CP000854; ACC41094.1; -; Genomic_DNA.
DR AlphaFoldDB; B2HSS0; -.
DR STRING; 216594.MMAR_2648; -.
DR KEGG; mmi:MMAR_2648; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_003896_4_3_11; -.
DR OrthoDB; 9800184at2; -.
DR UniPathway; UPA00132; -.
DR Proteomes; UP000001190; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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:0019853; P:L-ascorbic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2520; -; 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; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR010031; FAD_lactone_oxidase-like.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR NCBIfam; TIGR01679; bact_FAD_ox; 1.
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; 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.
DR PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE 4: Predicted;
KW Ascorbate biosynthesis {ECO:0000256|ARBA:ARBA00022644};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001190}.
FT DOMAIN 12..179
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 428 AA; 48127 MW; 9487402D5F4F190A CRC64;
MKTVWRNWAG EQYCAPSEIV RPASEAELAE LVAKAGQRGE RVRAVGSGHS FTDCACTDGV
MVDMAGMQRI VNVDPEAGLA TVEGGAKLRP LFSQLAEHGL ALENQGDIDK QSITGATATA
THGTGARFAN VSAQIVALRL VTASGEVLEL SEGDDYLAAR VSIGALGVIS QLTLKVVPLF
TLHRDDELKP LAETLERLDE HVDNNDHFEF FVFPYAETAL TRTTRRSEEP PMPVPEWRRR
VGDQFENVGL GLVCRTGRQF PSTAPKLNRL LTSLMSPSSV QDRGWKVYPS PRNVKFTEME
YAIPRENARE AVRRVIEVVR RRDLPIMYPL EVRFSAPDDA FLSTAYERDT CYIAVHQYTG
MEFETYFRAV EAIMDEYGGR PHWGKRHYQR AASLRERYPA WDRFTAVRDR LDPNRVFLND
YTRRVLGA
//
