ID B9NUB3_9RHOB Unreviewed; 805 AA.
AC B9NUB3;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Carbon-monoxide dehydrogenase, large subunit {ECO:0000313|EMBL:EEE39181.1};
DE EC=1.2.7.4 {ECO:0000313|EMBL:EEE39181.1};
GN ORFNames=RKLH11_3028 {ECO:0000313|EMBL:EEE39181.1};
OS Rhodobacteraceae bacterium KLH11.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=467661 {ECO:0000313|EMBL:EEE39181.1, ECO:0000313|Proteomes:UP000005135};
RN [1] {ECO:0000313|Proteomes:UP000005135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLH11 {ECO:0000313|Proteomes:UP000005135};
RX PubMed=21742885; DOI=10.1128/jb.05556-11;
RA Zan J., Fricke W.F., Fuqua C., Ravel J., Hill R.T.;
RT "Genome Sequence of Ruegeria sp. Strain KLH11, an N-Acylhomoserine Lactone-
RT Producing Bacterium Isolated from the Marine Sponge Mycale laxissima.";
RL J. Bacteriol. 193:5011-5012(2011).
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DR EMBL; DS999531; EEE39181.1; -; Genomic_DNA.
DR AlphaFoldDB; B9NUB3; -.
DR STRING; 467661.RKLH11_3028; -.
DR eggNOG; COG1529; Bacteria.
DR HOGENOM; CLU_001681_2_0_5; -.
DR OrthoDB; 9758509at2; -.
DR Proteomes; UP000005135; Unassembled WGS sequence.
DR GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IEA:UniProtKB-EC.
DR GO; GO:0043885; F:carbon-monoxide dehydrogenase (ferredoxin) activity; IEA:UniProtKB-EC.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; 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 InterPro; IPR012780; CO_Mo_DH_lsu.
DR NCBIfam; TIGR02416; CO_dehy_Mo_lg; 1.
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 Oxidoreductase {ECO:0000313|EMBL:EEE39181.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005135}.
FT DOMAIN 32..141
FT /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT hammerhead"
FT /evidence="ECO:0000259|SMART:SM01008"
SQ SEQUENCE 805 AA; 87708 MW; F1D52BEBF3BBC325 CRC64;
MNDQTLTPEE RAANLKGMGC ARKRVEDVRF TQGKGNYVDD IKLDGMLFGD FVRSPYAHAR
VVSVNKEAAL ALPGVIAVLT AEDLSPLGLH WMPTLAGDKQ MVLADGKVLF QGQEVAFVVA
EDRYIAADAV ELVEVEYEEL PVLTDPFEAL KSDVVLREDL EGQTEGAHGP RKHHNHIFTW
EQGDKDATEA VLAEADVVAE EMVYYHRTHP CPLETCGSVA SMDKVTGKLT LYGTFQAPHA
IRTVVSLISG LAEHNIRVIS PDIGGGFGNK VGAYAGYVCS VVASIVTGKP VKWVEDRMEN
LMSTAFARDY WMQGKIAATK EGKITGLWCH TTADHGGFDA CADPTKFPAG FMNICTGSYD
IPTAYLAVDG VYTNKAPGGV AYRCSFRVTE AAYFIERMIE VLAIKLNMDA AELRRINFIK
ANQFPYQSAL GWEYDSGDYH TAWDKALKAV DYDGLRADQA QRIEEFKAGK TRKLLGIGLT
HFTEIVGAGP VKNCDILGLG MFDSCEIRIH PTGSAIARLG TISQGQGHAT TFAQIIASEI
GLPADDITLE EGDTDTAPYG LGTYGSRSTP VAGAATAMAA RKIRAKAQMI AAYLLEVHDN
DVEWDVDRFA VKGAPERFKT MKEIAFAAYN QAIPGLEPGL EAVSYYDPPN MTYPFGAYIC
VMEIDVDTGE WEVRQFYALD DCGTRINPMI IDGQVHGGVT EALAIAMGQE IAYDEMGNVK
TGTLMDFFLP TAWETPNYIT DYTVTPSPHH PIGAKGVGES PNVGGVPAFS NAVHDAFRPF
GLVQSHMPHD HWRIWKIANG LGMHG
//