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Database: UniProt
Entry: B2HPT9_MYCMM
LinkDB: B2HPT9_MYCMM
Original site: B2HPT9_MYCMM 
ID   B2HPT9_MYCMM            Unreviewed;       296 AA.
AC   B2HPT9;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Carbon monoxyde dehydrogenase (Medium chain), CoxM {ECO:0000313|EMBL:ACC39116.1};
GN   Name=coxM {ECO:0000313|EMBL:ACC39116.1};
GN   OrderedLocusNames=MMAR_0655 {ECO:0000313|EMBL:ACC39116.1};
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:ACC39116.1, ECO:0000313|Proteomes:UP000001190};
RN   [1] {ECO:0000313|EMBL:ACC39116.1, 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; ACC39116.1; -; Genomic_DNA.
DR   RefSeq; WP_012392614.1; NC_010612.1.
DR   AlphaFoldDB; B2HPT9; -.
DR   STRING; 216594.MMAR_0655; -.
DR   KEGG; mmi:MMAR_0655; -.
DR   eggNOG; COG1319; Bacteria.
DR   HOGENOM; CLU_058050_3_0_11; -.
DR   OrthoDB; 9793944at2; -.
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; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR036683; CO_DH_flav_C_dom_sf.
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; IPR002346; Mopterin_DH_FAD-bd.
DR   PANTHER; PTHR42659; XANTHINE DEHYDROGENASE SUBUNIT C-RELATED; 1.
DR   PANTHER; PTHR42659:SF2; XANTHINE DEHYDROGENASE SUBUNIT C-RELATED; 1.
DR   Pfam; PF03450; CO_deh_flav_C; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   SMART; SM01092; CO_deh_flav_C; 1.
DR   SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001190}.
FT   DOMAIN          2..179
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   296 AA;  31478 MW;  ABF69A51E07A4A19 CRC64;
     MQVPGPFEYE RATSVDHAIG LLDRLGEGAR LVAGGHSLLP MMKLRIANPE YLVDINDLAP
     ELGYVITDPT LVRIGAMARH REILESEALA AVCPIFRDAE RVIADPVVRN RGTLGGSLCQ
     ADPAEDLSTV CTVLDAVCLA RGSSGEREIA IDEFQAGPYE TTLAPSEMLV EVRIPVRHNT
     SSAYAKVERR VGDWAVTAAG AAVTLNNDTI TAARVGLTAV NPDPAALAEL AAALVGRPAN
     EDTFAEAGRR AGQACEPVTD IRGTADYKRH LAAELTIRTL RSAVGRVRNQ PAPEGN
//
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