ID D5ZP48_STRV1 Unreviewed; 807 AA.
AC D5ZP48;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Xanthine dehydrogenase {ECO:0000313|EMBL:EFE66281.2};
GN ORFNames=SSFG_01531 {ECO:0000313|EMBL:EFE66281.2};
OS Streptomyces viridosporus (strain ATCC 14672 / DSM 40746 / JCM 4963 / KCTC
OS 9882 / NRRL B-12104 / FH 1290) (Streptomyces ghanaensis).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=566461 {ECO:0000313|EMBL:EFE66281.2, ECO:0000313|Proteomes:UP000003824};
RN [1] {ECO:0000313|Proteomes:UP000003824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14672 / DSM 40746 / JCM 4963 / KCTC 9882 / NRRL B-12104 /
RC FH 1290 {ECO:0000313|Proteomes:UP000003824};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Ward D., Young S., Kodira C.D., Zeng Q., Koehrsen M.,
RA Godfrey P., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland B.L.C., Ilzarbe M.,
RA Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces ghanaensis ATCC 14672.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DS999641; EFE66281.2; -; Genomic_DNA.
DR RefSeq; WP_004981673.1; NZ_DS999641.1.
DR AlphaFoldDB; D5ZP48; -.
DR eggNOG; COG1529; Bacteria.
DR OMA; THYYQTV; -.
DR Proteomes; UP000003824; Unassembled WGS sequence.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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.
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; IPR017609; Xanthine_dehydrogenase_dsu.
DR NCBIfam; TIGR03196; pucD; 1.
DR PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR PANTHER; PTHR11908:SF157; XANTHINE DEHYDROGENASE SUBUNIT D-RELATED; 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;
FT DOMAIN 47..154
FT /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT hammerhead"
FT /evidence="ECO:0000259|SMART:SM01008"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 807 AA; 85993 MW; 94E660458F845D42 CRC64;
MRSSEPSAAS GQGGAPLGVP TKITQGSGTR GGIGESTLRP DGVLKVTGEF AYASDLWHED
MLWGQILRSP VAHAEIVSID TGEALAVPGV YAVMTYDDLP ADVKHYGLEI QDTPVLAHGR
VRHHGEPVAI VAADHPETAR RAAAKIEVDY RELPVVTDEA SALAPDAVLV HEDRTDHHSR
HVPHPNIVHR QPIVRGDVAG ARRRADVIVE GEYTFGMQDQ AFLGPESGLA VPEEDGGVHL
YIATQWLHSD LRQIAPVLGL PEDKVRMTLA GVGGAFGGRE DLSMQIHACL LALRTGRPVK
IVYNRFESFF GHVHRHPAKL RYEHGATRDG RLTHVKCRIV LDGGAYASAS PAVVGNASSL
GIGPYVVDDV DIEAVALYTN NPPCGAMRGF GAVQACFAYE AQMDKLAKEL GLDPVEFRQL
NAMEQGAVMP TGQRVDSPAP VAELLRRVKA MPMPPERQWE SSEGADVRQL PGGLSNTTHG
EGVVRGVGYA VGIKNVGFSE GFDDYSTARV RMEVAGGEPV VTVHTAMAEV GQGGVTVHAQ
IARTELGVTR VTIHPADTRV GSAGSTSASR QTYVTGGAVR HACALVREKV LELGRRRFGS
YHPAWASAEL LLEGGKVVTD GGETLADLVD VLGDEAVEAE EEWRHRPTEP FDLRTGQGNG
HVQYSFAAHR AVVEVDTELG LVKVIELACA QDVGKALNPL SVVGQIQGGT AQGLGMAVME
EILVDPRTAK VRNPSFTDYL IPTILDTPTI PVDVLELADG HAPYGLRGVG EAPTLSSTPA
VLAAIRDATG LELNRTPVRP EHLTGTA
//