ID A0A0A0EDH1_9RHOB Unreviewed; 262 AA.
AC A0A0A0EDH1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Carbon monoxide dehydrogenase {ECO:0000313|EMBL:KGM48143.1};
GN ORFNames=ATO9_14300 {ECO:0000313|EMBL:KGM48143.1};
OS Pseudooceanicola atlanticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=1461694 {ECO:0000313|EMBL:KGM48143.1, ECO:0000313|Proteomes:UP000030004};
RN [1] {ECO:0000313|EMBL:KGM48143.1, ECO:0000313|Proteomes:UP000030004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-s11g {ECO:0000313|EMBL:KGM48143.1,
RC ECO:0000313|Proteomes:UP000030004};
RX PubMed=25663028; DOI=10.1007/s10482-015-0398-2;
RA Lai Q., Li G., Liu X., Du Y., Sun F., Shao Z.;
RT "Pseudooceanicola atlanticus gen. nov. sp. nov., isolated from surface
RT seawater of the Atlantic Ocean and reclassification of Oceanicola
RT batsensis, Oceanicola marinus, Oceanicola nitratireducens, Oceanicola
RT nanhaiensis, Oceanicola antarcticus and Oceanicola flagellatus, as
RT Pseudooceanicola batsensis comb. nov., Pseudooceanicola marinus comb. nov.,
RT Pseudooceanicola nitratireducens comb. nov., Pseudooceanicola nanhaiensis
RT comb. nov., Pseudooceanicola antarcticus comb. nov., and Pseudooceanicola
RT flagellatus comb. nov.";
RL Antonie Van Leeuwenhoek 107:1065-1074(2015).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGM48143.1}.
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DR EMBL; AQQX01000005; KGM48143.1; -; Genomic_DNA.
DR RefSeq; WP_043750232.1; NZ_CP051248.1.
DR AlphaFoldDB; A0A0A0EDH1; -.
DR STRING; 1461694.ATO9_14300; -.
DR eggNOG; COG1319; Bacteria.
DR OrthoDB; 9793944at2; -.
DR Proteomes; UP000030004; Unassembled WGS sequence.
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; 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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Reference proteome {ECO:0000313|Proteomes:UP000030004}.
FT DOMAIN 1..167
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 262 AA; 27189 MW; F46035B233E5D801 CRC64;
MYAFDIERPT TIADAVAALK SDEAQPLSGG QTLIPTLKSR LAAPSKLVSL SSISEMVGLS
DEGGVLRIGG ATKHDTVAKE AGGSHPGLAG LAGKIGDPAV RHRGTIGGSI ANNDPAACYP
AAALAHGATI VTDRREIAAD DFFTGMFDTA LEEGEIVTAV KFPRPEASNY QKFEQPASRF
AMVGVFVAKF ADGVRVAVTG ASEDGVFRWT EGEEALSANF SPDALDGLSV SAEGMITDLH
GSADYRAHLV KVMTKRAVAA AR
//
