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Database: UniProt
Entry: F0C6L3_9XANT
LinkDB: F0C6L3_9XANT
Original site: F0C6L3_9XANT 
ID   F0C6L3_9XANT            Unreviewed;       361 AA.
AC   F0C6L3;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Aerobic-type carbon monoxide dehydrogenase, middle subunit CoxM/CutM-like protein {ECO:0000313|EMBL:EGD18860.1};
GN   ORFNames=XGA_2547 {ECO:0000313|EMBL:EGD18860.1};
OS   Xanthomonas hortorum ATCC 19865.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas; Xanthomonas hortorum pv. gardneri.
OX   NCBI_TaxID=925777 {ECO:0000313|EMBL:EGD18860.1, ECO:0000313|Proteomes:UP000005023};
RN   [1] {ECO:0000313|EMBL:EGD18860.1, ECO:0000313|Proteomes:UP000005023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19865 {ECO:0000313|EMBL:EGD18860.1,
RC   ECO:0000313|Proteomes:UP000005023};
RX   PubMed=21396108; DOI=10.1186/1471-2164-12-146;
RA   Potnis N., Krasileva K., Chow V., Almeida N.F., Patil P.B., Ryan R.P.,
RA   Sharlach M., Behlau F., Dow J.M., Momol M.T., White F.F., Preston J.F.,
RA   Vinatzer B.A., Koebnik R., Setubal J.C., Norman D.J., Staskawicz B.J.,
RA   Jones J.B.;
RT   "Comparative genomics reveals diversity among xanthomonads infecting tomato
RT   and pepper.";
RL   BMC Genomics 12:146-146(2011).
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:EGD18860.1}.
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DR   EMBL; AEQX01000229; EGD18860.1; -; Genomic_DNA.
DR   RefSeq; WP_006450814.1; NZ_AEQX01000229.1.
DR   AlphaFoldDB; F0C6L3; -.
DR   PATRIC; fig|925777.8.peg.3076; -.
DR   Proteomes; UP000005023; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 2.
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:SF10; OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR42659; 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   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827}.
FT   DOMAIN          7..239
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   361 AA;  38411 MW;  86CFD44752494CB5 CRC64;
     MDARDGAGMI PLTYTRPDNV DAALTALAVR GDPQPVPAEA PVRLIAGGTN LTDLMKLQVM
     RPSRLVDINR LPLDSISTQP DGGLRLGALA RNADTAYHPE VETRYPLLSA AILAGASPQI
     RNMASNGGNL LQRTRCVYFY DHATPCNKRE PGTGCSAIGG LTKYHAILGA SAHCIATHPS
     DMCTALAALD AVVHVQGPNG ERDIPFAQFH RLPGDHPELD STLAPDELIV HIDLPDAQRF
     AAHSAYLKIR ERLSYAFALV SVAAALELAE DGSIREVRVA LGGVAHKPWR NPEAEAQLAG
     KPATAESFGS LADALLQGAQ SQGENAFKLP LARRAIVRAL DVAREGTIDN RGRTSALEES
     P
//
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