ID Q5LT95_RUEPO Unreviewed; 788 AA.
AC Q5LT95;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Carbon monoxide dehydrogenase, large subunit {ECO:0000313|EMBL:AAV94806.1};
DE EC=1.2.99.2 {ECO:0000313|EMBL:AAV94806.1};
GN Name=coxL-1 {ECO:0000313|EMBL:AAV94806.1};
GN OrderedLocusNames=SPO1519 {ECO:0000313|EMBL:AAV94806.1};
OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS pomeroyi).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV94806.1, ECO:0000313|Proteomes:UP000001023};
RN [1] {ECO:0000313|EMBL:AAV94806.1, ECO:0000313|Proteomes:UP000001023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC {ECO:0000313|Proteomes:UP000001023};
RX PubMed=15602564; DOI=10.1038/nature03170;
RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA Daugherty S.C., Deboy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT environment.";
RL Nature 432:910-913(2004).
RN [2] {ECO:0000313|EMBL:AAV94806.1, ECO:0000313|Proteomes:UP000001023}
RP GENOME REANNOTATION.
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC {ECO:0000313|Proteomes:UP000001023};
RX PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA Rivers A.R., Smith C.B., Moran M.A.;
RT "An updated genome annotation for the model marine bacterium Ruegeria
RT pomeroyi DSS-3.";
RL Stand. Genomic Sci. 9:11-11(2014).
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DR EMBL; CP000031; AAV94806.1; -; Genomic_DNA.
DR RefSeq; WP_011047256.1; NC_003911.12.
DR AlphaFoldDB; Q5LT95; -.
DR STRING; 246200.SPO1519; -.
DR PaxDb; 246200-SPO1519; -.
DR KEGG; sil:SPO1519; -.
DR eggNOG; COG1529; Bacteria.
DR HOGENOM; CLU_001681_2_0_5; -.
DR OrthoDB; 9758509at2; -.
DR Proteomes; UP000001023; Chromosome.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 Oxidoreductase {ECO:0000313|EMBL:AAV94806.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001023}.
FT DOMAIN 21..139
FT /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT hammerhead"
FT /evidence="ECO:0000259|SMART:SM01008"
SQ SEQUENCE 788 AA; 83768 MW; 3091EB1B6AEE33E0 CRC64;
MPKDSGIGAS SKRREDVRFL TGAGNYTDDI NLHGQAYVHF LRSDMAHGRI VSLDTAAAAA
MPGVVRIFTG ADFEGVGGLP CGWQVTDKHG EPMQEPGHPV LAQGKVRHVG DPIAAVVAET
PDQARDAAEA IGVEIEELPA VIDMKAALAE GAAKVHDDLS SNLCYDWGFV EENKGAVDAA
FAEAAHVTTL ELVNNRLVAN PMEPRVAIGD YARATGDSTL YTTSQNPHVI RLLMGAFVLG
IPEHKLRVVA PDVGGGFGSK IFHYAEEAFC TFAAKALARP VKWTSSRSEA FMSDAHGRDH
VTRIELALDA QNNFTALRTE TLANMGAYLS TFAPSVPTWL HGTLMAGNYK TPLIYVNVKA
VFTNTVPVDA YRGAGRPEAT YQLERVIDKA ARELGVDPIA LRRQNFVTEF PYQTPVAVVY
DTGDYNATMD KLEEIADLSG FAARRAESEA RGKLRGLGIN CYIEACGIAP SNLVGQLGAR
AGLYDAATVR VNATGSISVM VGAHSHGQGH ETAFPQVVAE MLGIDESMIE IVHGDSSKIP
FGMGTYGSRS LAVCGSAMVR ATEKIINKAK KIAAHLMEAS EADIELKDGQ FSVAGTDKSV
AWGDVTLAAY VPHNYPLEDI EPGLEETAFY DPSNFTYPAG AYACEVEVDP DTGKVTVERF
SAADDFGNIV NPMIVSGQVH GGLGQGIGQA LLENCAYDPE TGQLLSASYM DYAMPRADDV
PFYAVDHSCA TPCTHNPLGV KGCGEAGAIG SPPAVVNAVI DALQSGGKTV THIDMPMSPS
RVWSAMQG
//
