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Database: UniProt
Entry: I3ZH67_TERRK
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ID   I3ZH67_TERRK            Unreviewed;       348 AA.
AC   I3ZH67;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Aerobic-type carbon monoxide dehydrogenase, middle subunit CoxM/CutM-like protein {ECO:0000313|EMBL:AFL88585.1};
GN   OrderedLocusNames=Terro_1958 {ECO:0000313|EMBL:AFL88244.1}, Terro_2324
GN   {ECO:0000313|EMBL:AFL88585.1};
OS   Terriglobus roseus (strain DSM 18391 / NRRL B-41598 / KBS 63).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Terriglobus.
OX   NCBI_TaxID=926566 {ECO:0000313|EMBL:AFL88585.1, ECO:0000313|Proteomes:UP000006056};
RN   [1] {ECO:0000313|EMBL:AFL88585.1, ECO:0000313|Proteomes:UP000006056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18391 {ECO:0000313|EMBL:AFL88585.1}, and DSM 18391 / NRRL
RC   B-41598 / KBS 63 {ECO:0000313|Proteomes:UP000006056};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Munk A.C.C.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "Complete genome of Terriglobus roseus DSM 18391.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP003379; AFL88244.1; -; Genomic_DNA.
DR   EMBL; CP003379; AFL88585.1; -; Genomic_DNA.
DR   RefSeq; WP_014785813.1; NC_018014.1.
DR   AlphaFoldDB; I3ZH67; -.
DR   STRING; 926566.Terro_1958; -.
DR   KEGG; trs:Terro_1958; -.
DR   KEGG; trs:Terro_2324; -.
DR   PATRIC; fig|926566.3.peg.1932; -.
DR   eggNOG; COG1319; Bacteria.
DR   HOGENOM; CLU_058050_1_0_0; -.
DR   OrthoDB; 9774454at2; -.
DR   Proteomes; UP000006056; 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; -; 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:SF1; BLR6160 PROTEIN; 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   Reference proteome {ECO:0000313|Proteomes:UP000006056}.
FT   DOMAIN          1..230
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   348 AA;  36342 MW;  F8559B0088692CAA CRC64;
     MNPFAYERAT APEGAVHSLA ADKNAKLLGG GTNLVDLMKQ DVERPSTLID ITRLSALAHI
     EAVEGGHRVG ALVRNSDLAN DGDVRKTYPL LSQALLAGAS AQLRNLATTG GNLMQRTRCY
     YFYDSALPAC NKRAPGSGCG AVEGFNRVHA VLGQTDEGPA GAHTCIATNP SDMNVALAAL
     HAVVEISGPK GKRTMPVREF HRLVGKTPQL DTNLQHDELI TGVHLPASAA KFAANSYYLK
     ARDRQSYAFA LVSVAAGLEM DGGSIKSVAL ALGGVAHKPW TSEAAEKAMI GKPATEETFK
     AAAAAAMQGA KGYEHNAFKI ELAKSCIVRA FTLAAQGTGN HGAEGAAA
//
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