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Database: UniProt
Entry: R4KUF3_9FIRM
LinkDB: R4KUF3_9FIRM
Original site: R4KUF3_9FIRM 
ID   R4KUF3_9FIRM            Unreviewed;       289 AA.
AC   R4KUF3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Aerobic-type carbon monoxide dehydrogenase, middle subunit CoxM/CutM-like protein {ECO:0000313|EMBL:AGL03256.1};
GN   ORFNames=Desgi_3974 {ECO:0000313|EMBL:AGL03256.1};
OS   Desulfoscipio gibsoniae DSM 7213.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC   Desulfoscipio.
OX   NCBI_TaxID=767817 {ECO:0000313|EMBL:AGL03256.1, ECO:0000313|Proteomes:UP000013520};
RN   [1] {ECO:0000313|EMBL:AGL03256.1, ECO:0000313|Proteomes:UP000013520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7213 {ECO:0000313|EMBL:AGL03256.1,
RC   ECO:0000313|Proteomes:UP000013520};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Parshina S.,
RA   Plugge C., Muyzer G., Kuever J., Ivanova A., Nazina T., Klenk H.-P.,
RA   Brambilla E., Spring S., Stams A.F., Woyke T.;
RT   "Complete sequence of Desulfotomaculum gibsoniae DSM 7213.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP003273; AGL03256.1; -; Genomic_DNA.
DR   RefSeq; WP_006523841.1; NC_021184.1.
DR   AlphaFoldDB; R4KUF3; -.
DR   STRING; 767817.Desgi_3974; -.
DR   KEGG; dgi:Desgi_3974; -.
DR   eggNOG; COG1319; Bacteria.
DR   HOGENOM; CLU_058050_0_1_9; -.
DR   OrthoDB; 9789842at2; -.
DR   Proteomes; UP000013520; 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   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013520}.
FT   DOMAIN          1..178
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   289 AA;  30931 MW;  972158AB74B40C89 CRC64;
     MFLPDFEYYM PASVQEACAL LAEKGPTAKI LSGGTDLLNK MKHGLVAPEV LISLKQLDQL
     TSIAYVPDKG VVIGARATHN DICNSLLLQE KYLSLCEAAH HMANNQIRNV GTIGGNIVNA
     VPSADLPPIL MALGASITLV GRQGERVMAL EDFFVGPGKT RIAQDEIVAE IVIPDQPLTG
     STYIKFGLRR SGALAVVGVA VAVTMEGNVC KDARIALGAV GPVPMRAPKA EAMIIGKTVN
     EELLEEVGVC ASTECKPISD IRGSEEYRRD MVRVFTKRAL RKAIDEGHV
//
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