ID Q0S6P2_RHOJR Unreviewed; 905 AA.
AC Q0S6P2;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE SubName: Full=Bifunctional: xanthine dehydrogenase/ 4-hydroxybenzoyl-CoA reductase {ECO:0000313|EMBL:ABG96794.1};
DE EC=1.17.1.4 {ECO:0000313|EMBL:ABG96794.1};
DE EC=1.3.7.9 {ECO:0000313|EMBL:ABG96794.1};
GN OrderedLocusNames=RHA1_ro05013 {ECO:0000313|EMBL:ABG96794.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG96794.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006849}.
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DR EMBL; CP000431; ABG96794.1; -; Genomic_DNA.
DR RefSeq; WP_011597277.1; NC_008268.1.
DR AlphaFoldDB; Q0S6P2; -.
DR KEGG; rha:RHA1_ro05013; -.
DR PATRIC; fig|101510.16.peg.5064; -.
DR eggNOG; COG1529; Bacteria.
DR eggNOG; COG2080; Bacteria.
DR HOGENOM; CLU_001681_2_3_11; -.
DR OrthoDB; 9758509at2; -.
DR Proteomes; UP000008710; 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:0004854; F:xanthine dehydrogenase activity; IEA:UniProtKB-EC.
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 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; 1.
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 ECO:0000313|EMBL:ABG96794.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT DOMAIN 1..74
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 905 AA; 97040 MW; EE4DB8D28716403D CRC64;
MTYIVNGRAF DEEPNPGQCL RTFVRSLGHH GVKKGCDAGD CGACTVWLDG DPVHSCITPA
FRAEGREVTT IEGLGSPDDL HPLQRQFRDA PGFQCGFCTA GMIMTSATFT DAQKEDLPRA
LKGNLCRCTG YRAIEDAVNG VAAVEVAEPG RAVGASVGAP AATDVVTGRA EFTMDTEIEG
MLHLKVLHSP HAHARIVSID TTAALAVPGV HRVYTWEDVP RKRFTTAIHT DHLVDPDDTY
ILDDTVRFAG QRVVAVLADT VGAAEEGCRE VVVEYDVLPA VFDPEEAMAD GAPQLHGSDD
PFVRDPVHNI LLELHGEVGD IEAGFAEADV IHEGTYFTPR VQHAHLETHG SIAWMEDGRL
HVRTSSQSPS IAKVKLAHLF DLRPDQLRVF CKRVGGAFGG KQEVFSEDLV ALATLDTGRP
VCFEFTREEE FTTASPRHPM KLTITLGARS DGTLTAFQVR NVSNTGAYGN HGGETLFAAG
AAISAYRCLN KKFDAYAVYT NSVPSGALRG YGMTQPAFAV ESAMHELAVA LDIDPLELRR
RNIVRPGDSL VAIDDVPDDV GFGEDGLGQC IDLVDDALRR TANGQVLGVD WLVGEGTASS
LHETAPPTEH ISEAWATLGD DCVYELAVGT VEFGEGTSTA HVQIAATHLG TTPARIRLVQ
SDTDRTGFDT GAFASAGLFV AGNAVSNASV ALRDRILAFA AVHTGVDVTE CSMDDDGVLC
GGTRVPLTDL VAAARRRGIR FTEARKAYGS PRSVVSNTHG FRIAVHRVTG EIRILYSVQA
ADVGVVINPV QVRGQIEGGV AQGIGFALTE NFHVDDNGVM INPSLRNYRI PTYADIPRTE
VLLVESNDSV GPMRAKGMAE CCINPVAPAL ANALENATGV RFRELPLTPE RIYHRIGENR
SVPTT
//
