ID E3H716_ILYPC Unreviewed; 851 AA.
AC E3H716;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Selenium-dependent molybdenum hydroxylase 1 {ECO:0000313|EMBL:ADO81912.1};
GN OrderedLocusNames=Ilyop_0123 {ECO:0000313|EMBL:ADO81912.1};
OS Ilyobacter polytropus (strain ATCC 51220 / DSM 2926 / LMG 16218 / CuHBu1).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Ilyobacter.
OX NCBI_TaxID=572544 {ECO:0000313|EMBL:ADO81912.1, ECO:0000313|Proteomes:UP000006875};
RN [1] {ECO:0000313|EMBL:ADO81912.1, ECO:0000313|Proteomes:UP000006875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51220 / DSM 2926 / LMG 16218 / CuHBu1
RC {ECO:0000313|Proteomes:UP000006875};
RX PubMed=21304735; DOI=10.4056/sigs.1273360;
RA Sikorski J., Chertkov O., Lapidus A., Nolan M., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Brambilla E., Yasawong M.,
RA Rohde M., Pukall R., Spring S., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Ilyobacter polytropus type strain (CuHbu1).";
RL Stand. Genomic Sci. 3:304-314(2010).
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006849}.
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DR EMBL; CP002281; ADO81912.1; -; Genomic_DNA.
DR RefSeq; WP_013386583.1; NC_014632.1.
DR AlphaFoldDB; E3H716; -.
DR STRING; 572544.Ilyop_0123; -.
DR KEGG; ipo:Ilyop_0123; -.
DR eggNOG; COG1529; Bacteria.
DR eggNOG; COG2080; Bacteria.
DR HOGENOM; CLU_001681_2_3_0; -.
DR OrthoDB; 9759099at2; -.
DR Proteomes; UP000006875; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
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; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
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; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR017697; Xdh.
DR NCBIfam; TIGR03311; Se_dep_XDH; 1.
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; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR Pfam; PF02738; MoCoBD_1; 1.
DR Pfam; PF20256; MoCoBD_2; 2.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006875}.
FT DOMAIN 1..74
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 851 AA; 92006 MW; 35DD2302331B0AD7 CRC64;
MYEIIVNGKL TKTDKVKNLL KYLRDDLDLK AAKNGCEEGA CGTCTVLVDG KAIKACVLKT
DKLKGKKITT LEGLSQRKRD VFAYAFTEVG AVQCGFCIPG MVMSATALFL KTLEPTKDEI
KKSLTGNICR CTGYVKIEEA IELAAEILRT EREIPKRDCK GMVGEHVHRI DGPAKAIGEG
VYAEDIRIEG MYYGGAVRSL YPRARVLSID VSEAEAMEGV LKVLTAEDVP GINNIGHLSF
ISDWDALIPV GKITRYRGDA IALVAAKDKE TLEAAKKAVK IEYEELTPVL SIEGAKDENA
PKIHENGNLL FHQKLSKGNV EKAISDSKYV VTEIYNTPAT EHAYLEPESA TALPTNDGIQ
LYTSSQSIFD EQREVSRLLG VKPSKVRVTS TLVGGGFGGK EDMTVQHHAG LLAYVLQVPV
QVTLSRQESI YVSTKRHSME IEMTTACDEN GILTAMKTTI LSDTGAYSSL GGPVLQRACT
HASGPYNYHN IEIDGKAYYT NNPPGGAFRG FGVTQSTFAS ESNINKLAKL AGISAWEIRS
RNAIRPGQIL PNGQIADAGT GLVETLEAVK DEFYKNKYVG LACAFKNSGI GVGLPDIGRC
RLTVIDGKVH LRTSAACIGQ GVGTVNLQIL CQTTGLDPKN IIIETPDTHV TPDSGTTTAS
RQTVFTGEAV RLAALELKNT LKGKTLKEIE GYDHTEEYSG ITDKIGSFKE NPKSHIAYGY
ATQLVVLNES GKIEKVVAAH DVGKAINPKS VEGQIEGGVV MGLGYALTEI MPFENGMPQV
KFGTLGLLRS TLVPEIKSII IEKNTEELAY GAKGVGEITV IPTAPAVQGA YYNFDGEFRT
ELPLKKTAYK K
//
