ID A0A101N2P3_9ACTN Unreviewed; 796 AA.
AC A0A101N2P3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Xanthine dehydrogenase subunit D {ECO:0000313|EMBL:KUM85444.1};
GN ORFNames=AQI94_26635 {ECO:0000313|EMBL:KUM85444.1};
OS Streptomyces pseudovenezuelae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=67350 {ECO:0000313|EMBL:KUM85444.1, ECO:0000313|Proteomes:UP000053039};
RN [1] {ECO:0000313|EMBL:KUM85444.1, ECO:0000313|Proteomes:UP000053039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40212 {ECO:0000313|EMBL:KUM85444.1,
RC ECO:0000313|Proteomes:UP000053039};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces pseudovenezuelae DSM 40212, type
RT strain for the species Streptomyces pseudovenezuelae.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUM85444.1}.
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DR EMBL; LMWM01000029; KUM85444.1; -; Genomic_DNA.
DR RefSeq; WP_031050206.1; NZ_KQ948149.1.
DR AlphaFoldDB; A0A101N2P3; -.
DR OrthoDB; 9758509at2; -.
DR Proteomes; UP000053039; 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-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:SF132; ALDEHYDE OXIDASE 1-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;
FT DOMAIN 35..142
FT /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT hammerhead"
FT /evidence="ECO:0000259|SMART:SM01008"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 796 AA; 85141 MW; 355E6FB0A8870288 CRC64;
MSTPNGTPTK ITQGSKTKGG IGESTLRPDG TLKVTGEFAY SSDMWHEDML WGQILRSTVA
HAEIVSIDTS EALALPGVYA VMTYDDLPTE VKNYGLEIQD TPVLAHGKVR HHGEPVAIVA
ADHPETARRA AAKIKVEYRE LPVITDEASA TAPDAILVHE NRDDHHIGHV PHPNIVHRQP
ILRGDARQAA ERADFVVKGE YTFGMQDQAF LGPESGLAVP DEDGGVHLYI ATQWLHSDLR
QIAPVLGLPE RKVRMTLSGV GGAFGGREDL SMQIHACLLA LRTGKPVKIV YNRFESFFGH
VHRHPAKLYY EHGATREGKL THVKCRIVLD GGAYASASPA VVGNASSLSI GPYVVDDVDI
EAIALYTNNP PCGAMRGFGA VQACFAYEAQ MDKLADAVGM DRVEFRQLNA MEQGTIMPTG
QPVDSPAPVA ELLRRVKAMP LPPEQQWLAA GEQADVRQLP GGLSNTTHGE GVVRGIGYAV
GIKNVGFSEG FDDYSTAKVR MEVVGGEPVA TVHTAMAEVG QGGVTVHAQI ARTELGVTQV
TIHPADTQVG SAGSTSASRQ TYVTGGAVKN SCELVREKVL ELGRRKFGSY HPAWATAELL
LEGGKVVTDG GEVLADLADV LEGESVEVEA EWRHRPTEAF DLRTGQGFGH VQYSFAAHRA
VVEVDTELGL VKVIELACAQ DVGKALNPLS VIGQIQGGTT QGLGIAVMEE IIVDPKTAKV
RNPSFTDYLI PTILDTPTIP VDVLELADDH APYGLRGIGE APTLSSTPAV LAAIRNATGL
ELNRTPVRPE HLTGTA
//
