ID B2HMI7_MYCMM Unreviewed; 463 AA.
AC B2HMI7;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:ACC43756.1};
GN OrderedLocusNames=MMAR_5352 {ECO:0000313|EMBL:ACC43756.1};
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:ACC43756.1, ECO:0000313|Proteomes:UP000001190};
RN [1] {ECO:0000313|EMBL:ACC43756.1, 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).
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DR EMBL; CP000854; ACC43756.1; -; Genomic_DNA.
DR RefSeq; WP_012396856.1; NC_010612.1.
DR AlphaFoldDB; B2HMI7; -.
DR STRING; 216594.MMAR_5352; -.
DR KEGG; mmi:MMAR_5352; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_032465_0_0_11; -.
DR OrthoDB; 143770at2; -.
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 Gene3D; 3.30.465.10; -; 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; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR PANTHER; PTHR13878:SF91; L-GULONOLACTONE OXIDASE 3; 1.
DR Pfam; PF04030; ALO; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001190}.
FT DOMAIN 19..196
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 463 AA; 50152 MW; 4AEF478C37EA98A7 CRC64;
MFSAPVPTTP TRLTGWGRTA PSVAEVLRTP DPEVIATAVA RVADSGARGV IARGLGRSYG
DNAQNGGGLV IDMSPLNKIH SISADSKLVD VDAGVNLDQL MKAALPLGLW VPVLPGTRQV
TIGGAIACDI HGKNHHSAGS FGNHVRSLDL LTADGEVRHL TPTGTETADT ALFWATVGGN
GLTGIILRAT IEMTPTETAY FIADGDVTAS LDETIALHSD GSEGNYTYSS AWFDAISGPP
KLGRAAVSRG CLATIDQLPT KLQRDPLKFD APQLLTFPDV FPNGLANKYT FGPIGELWYR
KSGTYRGKVQ NLTQFYHPLD MFGEWNRAYG PAGFLQYQFV VPTEAVDEFK RIIGDIQASG
HYSFLNVFKL FGAGNQAPLS FPIPGWNICV DFPIKAGLNE FVSELDRRVM EFGGRLYTAK
DSRTTAETFH AMYPRIDEWI AVRRKVDPCG VFASDMARRL ELL
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