ID B7J6M5_ACIF2 Unreviewed; 782 AA. AC B7J6M5; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAR-2024, entry version 67. DE SubName: Full=Oxidoreductase, molybdopterin binding subunit {ECO:0000313|EMBL:ACK78390.1}; GN OrderedLocusNames=AFE_0809 {ECO:0000313|EMBL:ACK78390.1}; OS Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 OS / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)). OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales; OC Acidithiobacillaceae; Acidithiobacillus. OX NCBI_TaxID=243159 {ECO:0000313|EMBL:ACK78390.1, ECO:0000313|Proteomes:UP000001362}; RN [1] {ECO:0000313|EMBL:ACK78390.1, ECO:0000313|Proteomes:UP000001362} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455 RC {ECO:0000313|Proteomes:UP000001362}; RX PubMed=19077236; DOI=10.1186/1471-2164-9-597; RA Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R.II., RA Eisen J.A., Holmes D.S.; RT "Acidithiobacillus ferrooxidans metabolism: from genome sequence to RT industrial applications."; RL BMC Genomics 9:597-597(2008). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001219; ACK78390.1; -; Genomic_DNA. DR RefSeq; WP_012536374.1; NC_011761.1. DR AlphaFoldDB; B7J6M5; -. DR STRING; 243159.AFE_0809; -. DR PaxDb; 243159-AFE_0809; -. DR GeneID; 66431960; -. DR KEGG; afr:AFE_0809; -. DR eggNOG; COG1529; Bacteria. DR HOGENOM; CLU_001681_2_2_6; -. DR Proteomes; UP000001362; 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: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; KW Reference proteome {ECO:0000313|Proteomes:UP000001362}. FT DOMAIN 59..153 FT /note="Aldehyde oxidase/xanthine dehydrogenase a/b FT hammerhead" FT /evidence="ECO:0000259|SMART:SM01008" SQ SEQUENCE 782 AA; 83712 MW; 1B8B586BBA66368D CRC64; MDDELPRRRE KFPFGLAHLG LDAVEREIPA DEPPPLAPNA ALTQIGKDIR RSDARNKVTG AALYTVDVHP PGMLHAAVLR SPLPHARIRS LDLSPAAALP GVHAVLTVVE PPADGASMVL RYVGQPVAAL AADTPALAEA ALRLIRVEYE PLPFVVDLEG ARQADAPLVY PNGERENIPS AGLPAAAGDL PIAGNIRGPE SKGSRGDIDA GFAAAEIVVD GTYHTQVQTH CCLEPHAIVA AWHEDGLDVW MSTQFTAGVR AQLARHFQLP LSRVRVRAEA VGGGFGSKSQ IGLYGRTAVA LSRLAGAPVR LVHRRDEEHM DTGNRPSSEQ HLRIGARRDG TLTALSLHSY GNAGIAFGAG VGNMITALYR CPHVESLQYD VFTHTGPSCA MRGPGNTQGA FALEQGIDEL AEKLAMDPLA LRDVIDPSPV RREERRMGAE RIGWTQRKPP GADQGPVKRG RGVAQSLWSA NVQTNAACEL RLWRDGRVEV LSSVQDIGTG VGTVLAQVVA EELGLRPEDI HVRIGDTEFP SGPPSYGSRT TASITPPART AAWRIKEALF RSVASAWQVD PQRLTVQDGW IHLRDAPQRR ISWQEAAAAL RTDRISAFAG RSDDYAGFRS RSGDAAMALN DLGGVQFAEV AVDTETGVIR VERVVAVQDC GRPINPLQIE SQVQGGVLMG LSYALLEERI LDIHTGWMLN ANLVDYKLTG AWDTPQIEVI LLENYQGFSA TDAYGIAEPA NIATAAAIAN AVYNAVGVRM RSLPMTPAKV LHALGAAGGG PR //