ID A0A2C9CUB4_9RHOB Unreviewed; 767 AA.
AC A0A2C9CUB4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Carbon-monoxide dehydrogenase large subunit {ECO:0000313|EMBL:SOH94956.1};
GN ORFNames=SAMN06273572_106107 {ECO:0000313|EMBL:SOH94956.1};
OS Monaibacterium marinum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Monaibacterium.
OX NCBI_TaxID=1690039 {ECO:0000313|EMBL:SOH94956.1, ECO:0000313|Proteomes:UP000220034};
RN [1] {ECO:0000313|EMBL:SOH94956.1, ECO:0000313|Proteomes:UP000220034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7 {ECO:0000313|EMBL:SOH94956.1,
RC ECO:0000313|Proteomes:UP000220034};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; OCTN01000006; SOH94956.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9CUB4; -.
DR OrthoDB; 9763985at2; -.
DR Proteomes; UP000220034; 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:SF132; ALDEHYDE OXIDASE 1-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;
FT DOMAIN 21..136
FT /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT hammerhead"
FT /evidence="ECO:0000259|SMART:SM01008"
SQ SEQUENCE 767 AA; 81667 MW; C8F3756EFBD5BF65 CRC64;
MAQGSLIGQS LPRVEDDRLL DGAGCYIDDV ALPGMMHMAI LRSSDAHGRI TALDCSAARL
VPGVIDVFTA EDWPQDMPVI PMRLIPLESS VPFLQRPLAQ GKVRYVGEPV AVVVARDRRT
AEDALEFLEL EIEALPPVVT RDQALAATGD ALMVPEVGTN ISAQYQIGRG DIEDAFARAD
VTLKKTFQSH RHTAVPLETR GTIAVFDIAA GKLTIHGASK VTFFNRAELA KAFNLRNDQV
DLITSDIGGG FGVRGELYPE YYLAAEASRR TGRPVKWIED RREHFAATNH SRDVDCELEI
AALKDGTILG MRGQVRADMG AYIRTNGNVV PAKAGQFLPG PYRVPAFACE VLALVTNKTP
VGTYRGPGRI EANFFRERML DCLADELGMD PAALRMKNLL GAAEMPFDTG DLLPNAQKVV
FDSGDYPATF RKLLDECDWD APAQVHSDGR LHAMGLACFN ESSGGGLYEN ARISVAASGQ
ITVSTGSSSM GQGVETAIRQ ICADALSMAP ERITVALSST TLLSDGVGSF HSRSTVMAGS
AVGQAAAELL DQARGEAGRR LNAAPAELDY SDGVFRVMGQ SDRSIRLSDL SAMLSDQGGL
DVESRYEQAP LGFSFGAHAA HVAIDPGTGD IEVLDYWVVE DVGRVLNPAL VEGQTIGGVV
QGLGDALYGE LVYDDMGQLL TASFADYLLP TSTEVPDIRA VATGDYPSPH NPYGFKGAGE
GGIVAVAAAV GNAIARAIGP AGDAICQTPF HPEKILTLLH AAKKGKQ
//