ID B2HJB2_MYCMM Unreviewed; 479 AA.
AC B2HJB2;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:ACC38581.1};
GN OrderedLocusNames=MMAR_0110 {ECO:0000313|EMBL:ACC38581.1};
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:ACC38581.1, ECO:0000313|Proteomes:UP000001190};
RN [1] {ECO:0000313|EMBL:ACC38581.1, 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; CP000854; ACC38581.1; -; Genomic_DNA.
DR RefSeq; WP_012392113.1; NC_010612.1.
DR AlphaFoldDB; B2HJB2; -.
DR STRING; 216594.MMAR_0110; -.
DR KEGG; mmi:MMAR_0110; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_018354_10_2_11; -.
DR OrthoDB; 9775082at2; -.
DR Proteomes; UP000001190; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR012951; BBE.
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; IPR006093; Oxy_OxRdtase_FAD_BS.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS00862; OX2_COVAL_FAD; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001190};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..479
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039075122"
FT DOMAIN 70..242
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 479 AA; 49011 MW; 083C37A28C69DF4B CRC64;
MAREISRQAF LRGAAGALAA GAVFGSVRAA AEPNPSGWEG LSSALGGKVL RPDDGPQFAT
AKQVFNTNYN DFTPAAVVTP TSAADVQKAM AFATAHNLKV APRSGGHSYI GASTANGAMV
LDLRQLPGDI NYDAATGQVT VTPSTGLYEM HQVLAGAGRG IPTGTCPSVG AAGHALGGGL
GAHSRHAGLL CDALTSAAVV LPSGQAVTAS AASNPDLFWA LRGGGGGNFG VTTSLTFATF
ATKDLDAVNL DFPPESFAQV LLGWQQWLRT ADRNNWALAD ATVDQMGTHC RILATCPVGS
GGSVASAITS AVGVQPIGTD HHTFNYLDLV RYLAVGNLNP APLGYVGGSD VLPTINAGAA
KGIASAIDAF PRGAGRALAI MHALDGALAT VAPGATAFPW RRQSALVQWY VETPGSPAAA
SGWLNTAHQA VQPYSAGGYV NYLEANQPAS RYFGPNLSRL SAVRQKYDPG RVMFSGLNL
//
