ID   A0A1Y6B5C0_9PROT        Unreviewed;       789 AA.
AC   A0A1Y6B5C0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Carbon-monoxide dehydrogenase large subunit {ECO:0000313|EMBL:SME90367.1};
GN   ORFNames=SAMN05428998_101304 {ECO:0000313|EMBL:SME90367.1};
OS   Tistlia consotensis USBA 355.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Fodinicurvataceae; Tistlia.
OX   NCBI_TaxID=560819 {ECO:0000313|EMBL:SME90367.1, ECO:0000313|Proteomes:UP000192917};
RN   [1] {ECO:0000313|EMBL:SME90367.1, ECO:0000313|Proteomes:UP000192917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USBA 355 {ECO:0000313|EMBL:SME90367.1,
RC   ECO:0000313|Proteomes:UP000192917};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FWZX01000001; SME90367.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y6B5C0; -.
DR   STRING; 560819.SAMN05428998_101304; -.
DR   Proteomes; UP000192917; Unassembled WGS sequence.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR   Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4.
DR   InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR   InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR   InterPro; IPR016208; Ald_Oxase/xanthine_DH-like.
DR   InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR   InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
DR   InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR   PANTHER; PTHR11908:SF164; DEHYDROGENASE, MOLYBDENUM BINDING SUBUNIT-RELATED; 1.
DR   PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR   Pfam; PF01315; Ald_Xan_dh_C; 1.
DR   Pfam; PF02738; MoCoBD_1; 1.
DR   Pfam; PF20256; MoCoBD_2; 1.
DR   SMART; SM01008; Ald_Xan_dh_C; 1.
DR   SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR   SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000192917}.
FT   DOMAIN          35..155
FT                   /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT                   hammerhead"
FT                   /evidence="ECO:0000259|SMART:SM01008"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   789 AA;  81914 MW;  AAD3C14C56675A02 CRC64;
     MSPAESSVPP FRPDDGRPDA GHPAAGRLED RRLATGHGRY TADMAVPGML HAAFVRSPYA
     SARLAGLDSS AARALPGIVA VLTAADLAAD GIAPFSVPMA IEGPGGRSYR QTPRPLLVGE
     RVRFVGEPLA LVVAETASAA LDGAEAVAFE LEPEPVVATL DQAARPDAPL LWDEAPGNLA
     YHWRRGDWQA VGAALRASHR VTRLEARVSR VSAAPMEPRG ALAVPQPDGR TSLYASVQAA
     QGLKATLATM FGLEAGSIRV VAPDVGGSFG MKAGPLREEC LVFWAARRLG RPLRWVAERG
     EALLSDEAGR DVRIVAELGL DGEGLFTALA VSMEVNVGAY ASGRSTVPIM NIGGIAGVYR
     TPLIAGEVLG RFTNAAPTAP YRGAGRPDAT FAVERVIDQA AREAGIDAFE LRRRNLVPAS
     AMPYRTPFIF TYDAGDFART MELAAARADY AGFAARRAEA GRRGRLRGIG IANPIEVAGG
     PFAKPGQDFA TLRAAADGTV TLYCGAMSAG QGLETAMIGL AAERLGLSTD RFRYVQGDSD
     AVPQGKGMGG SSAMTTAGSA VLRGVERLLE EGRQIAADEL EAAAADLEYE NGLFRIVGTD
     RVLSLAEVAR IAERRAGDGA GGLAGQGDFT PGAPTYPNGC HICEVEIDPE TGSCEVVSYV
     GVEDIGRVLF PQLAAGQVHG GVAQGLGQVL CEELRLDAEG QLLAGSFMDY AMPRAEDLPA
     YDCAFAETAT GLNPLGVKGV GEAGTVGALA AGMNAVCDAL ASAGVERFDM PASPQRVWAA
     LAAAKAASD
//