ID A0A0D5M2C4_9GAMM Unreviewed; 485 AA.
AC A0A0D5M2C4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Xanthine dehydrogenase, small subunit {ECO:0000313|EMBL:AJY50544.1};
DE EC=1.2.3.1 {ECO:0000313|EMBL:AJY50544.1};
GN ORFNames=KO116_02065 {ECO:0000313|EMBL:AJY50544.1};
OS Halomonas sp. KO116.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1504981 {ECO:0000313|EMBL:AJY50544.1, ECO:0000313|Proteomes:UP000028645};
RN [1] {ECO:0000313|EMBL:AJY50544.1, ECO:0000313|Proteomes:UP000028645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KO116 {ECO:0000313|EMBL:AJY50544.1,
RC ECO:0000313|Proteomes:UP000028645};
RX PubMed=25953187;
RA O'Dell K.B., Woo H.L., Utturkar S., Klingeman D., Brown S.D., Hazen T.C.;
RT "Genome Sequence of Halomonas sp. Strain KO116, an Ionic Liquid-Tolerant
RT Marine Bacterium Isolated from a Lignin-Enriched Seawater Microcosm.";
RL Genome Announc. 3:0-0(2015).
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DR EMBL; CP011052; AJY50544.1; -; Genomic_DNA.
DR RefSeq; WP_035555481.1; NZ_CP011052.1.
DR AlphaFoldDB; A0A0D5M2C4; -.
DR STRING; 1504981.KO116_02065; -.
DR KEGG; hak:KO116_02065; -.
DR eggNOG; COG4630; Bacteria.
DR HOGENOM; CLU_001681_9_0_6; -.
DR OrthoDB; 9775084at2; -.
DR Proteomes; UP000028645; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0004031; F:aldehyde oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004854; F:xanthine dehydrogenase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 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; 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; IPR016208; Ald_Oxase/xanthine_DH-like.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
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 InterPro; IPR012175; Xanth_DH_ssu_bac.
DR InterPro; IPR014307; Xanthine_DH_ssu.
DR NCBIfam; TIGR02963; xanthine_xdhA; 1.
DR PANTHER; PTHR45444:SF3; ALDEHYDE OXIDASE_XANTHINE DEHYDROGENASE, MOLYBDOPTERIN BINDING PROTEIN; 1.
DR PANTHER; PTHR45444; XANTHINE DEHYDROGENASE; 1.
DR Pfam; PF03450; CO_deh_flav_C; 1.
DR Pfam; PF00941; FAD_binding_5; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR PIRSF; PIRSF036557; XdhA_RC; 1.
DR SMART; SM01092; CO_deh_flav_C; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AJY50544.1}.
FT DOMAIN 2..86
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 186..365
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 485 AA; 52759 MW; D838EAD04F4D85BA CRC64;
MATIAFLLNG APHQCEVSPN TSTLTLLREH LALTGTKEGC ASGDCGACTV AIGEQNADTH
TFTSANACIT PAHQLQGRHL VTVEGLAKEG RLHPAQEAMI ECHGSQCGFC TPGIVMSLFT
LHNDLTQRPA PLPPERLEAA LGGNLCRCTG YRPIRDAALR MNDMPYERPQ WQDAALSTSE
NDAEITDPTA KTPFFAQPLS LTALTRLRQE APQARLVAGG TDLWLESTQR LASLDQLIDV
SRVAELLTVA ATTFEGQPGW WIGAGVTYTQ LEPLFEEHFP AFAHLLHRLG SQQIRNRGTL
GGNIANASPI GDTPPVLLAL GAQVELASTN GKRCLVLEDF FLDYKKTALA ADEVVSRIFI
PQPVEDSQLR VWKLSKRRED DISALIGAFS YRIEQGTLQD VRIAFGGMAA TPKRAKAAEA
ALEGSTLTAE TFRAAQQALD DDFQPMSDVR GSQHYRQQAA KNLIERLYLS LSVSDHEVML
HAYAH
//
