ID A0A0A8EVP1_9ACTN Unreviewed; 797 AA.
AC A0A0A8EVP1;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Aldehyde oxidase and xanthine dehydrogenase molybdopterin binding protein {ECO:0000313|EMBL:AJC60310.1};
GN ORFNames=GZL_07760 {ECO:0000313|EMBL:AJC60310.1};
OS Streptomyces sp. 769.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1262452 {ECO:0000313|EMBL:AJC60310.1, ECO:0000313|Proteomes:UP000031113};
RN [1] {ECO:0000313|EMBL:AJC60310.1, ECO:0000313|Proteomes:UP000031113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=769 {ECO:0000313|EMBL:AJC60310.1,
RC ECO:0000313|Proteomes:UP000031113};
RA Du Q., Wang Q., Li Q., Wang L., Zhang Z., Ren J., Wang J., Wang M.;
RT "Complete Genome Sequence of Streptomyces gongzhulingensis.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003987; AJC60310.1; -; Genomic_DNA.
DR RefSeq; WP_039638476.1; NZ_CP003987.1.
DR AlphaFoldDB; A0A0A8EVP1; -.
DR KEGG; stre:GZL_07760; -.
DR HOGENOM; CLU_001681_2_0_11; -.
DR Proteomes; UP000031113; Chromosome.
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:SF164; DEHYDROGENASE, MOLYBDENUM BINDING SUBUNIT-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 30..144
FT /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT hammerhead"
FT /evidence="ECO:0000259|SMART:SM01008"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 797 AA; 86070 MW; 052070AEA2F82E39 CRC64;
MTGGQDGARE GEGRLIGRSV PRREDPRLLT GRGRFVDDIA LTGMLHAQFV RSTVAHGEIT
AIDLSAVRAV PGVVAAFTAE DLKAGDIVAR LDRPPQEFVP TAMPVLARDR VRYVGEPVAI
VVARDAYAAE DGVEAARVRY AVRPPVTSEA AALADDAPLV HAEAARNTLV DVELFATDGI
DEVFAAADRV VRVEARTGRQ NALPLETRGA AAHWDDREEQ LVLHTCTQVP HQVRTVASRC
LQLAERAVRV VVPDMGGGFG LKCVVGREEI AAAAAALRLR RPVKWIEDRK DALSASFLAR
EQRYDVRAAF DANGRILALD ADVVCDMGAY SCYPFTAGIE PLMAAAEMPG VYTVPAYRVR
GRAVATNKAP SAPYRGVSRP QYVMVMERLF ERAARELDLD PVEIRRRNLI TSFPYTGVNG
ITYDPGSYRE SLDLCERTLR AEGWYERQRT ARAEGRYLGI GYACFSERTG YGSAAFAQRR
MAVVPGFDLS EARMDPSGAV TVTTGTMSHG QSHETTLAQI VADELGLDID KVRLHQGDTD
RIAYGWGTFA SRSVAIGGSA VRLAAGRLGD KLRALAAARW DVPVDRTALG RGEVFRRDDP
DTAIGYVELA ELAYLRADLL PKGIEPGLTA TASFDVFNDG TFSNATHGTV VELAPDTGRV
EILRYVCVED CGVAINPQVV EGQCRGGIAQ GIAGALFERV TYDAQGEPSA TSFMDYKVPT
AHEIPDVAIH HLETPCAFTE TGAKGAGEGG TIGAPAAVLN AVNDALRPTG VELDDTPITP
ETVHRALHRR HYQESTR
//
