ID B0VUR7_ACIBS Unreviewed; 794 AA. AC B0VUR7; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 90. DE SubName: Full=Xanthine dehydrogenase, large subunit {ECO:0000313|EMBL:CAP00509.1}; DE EC=1.17.1.4 {ECO:0000313|EMBL:CAP00509.1}; GN Name=xdhB {ECO:0000313|EMBL:CAP00509.1}; GN OrderedLocusNames=ABSDF1159 {ECO:0000313|EMBL:CAP00509.1}; OS Acinetobacter baumannii (strain SDF). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=509170 {ECO:0000313|EMBL:CAP00509.1, ECO:0000313|Proteomes:UP000001741}; RN [1] {ECO:0000313|EMBL:CAP00509.1, ECO:0000313|Proteomes:UP000001741} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SDF {ECO:0000313|EMBL:CAP00509.1, RC ECO:0000313|Proteomes:UP000001741}; RX PubMed=18350144; DOI=10.1371/journal.pone.0001805; RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., RA Weissenbach J., Cruveiller S.; RT "Comparative analysis of Acinetobacters: three genomes for three RT lifestyles."; RL PLoS ONE 3:E1805-E1805(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; CU468230; CAP00509.1; -; Genomic_DNA. DR AlphaFoldDB; B0VUR7; -. DR KEGG; abm:ABSDF1159; -. DR HOGENOM; CLU_001681_4_1_6; -. DR Proteomes; UP000001741; Chromosome. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro. DR GO; GO:0004854; F:xanthine dehydrogenase activity; IEA:UniProtKB-EC. 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 InterPro; IPR014309; Xanthine_DH_Mopterin-bd_su. DR NCBIfam; TIGR02965; xanthine_xdhB; 1. 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; KW Oxidoreductase {ECO:0000313|EMBL:CAP00509.1}. FT DOMAIN 30..140 FT /note="Aldehyde oxidase/xanthine dehydrogenase a/b FT hammerhead" FT /evidence="ECO:0000259|SMART:SM01008" SQ SEQUENCE 794 AA; 87121 MW; D9CDFE92317C064C CRC64; MNQTIDLNIS KKSAKAGDSI PHESAHLHVT GQATYATYID DLPELENTLH LAVGFSNCAK GKISKFDLDA VRQADGVHAV FSAKDIEVEN NWGPIVKDDP IFAEEQVEFY GQALFVVVAE SYQQARQAVR LAKIEYVPET PILTIQDAIK KESWVLPPVE FSHGEVEQAF QNAAHQLSGA IELGGQEHFY LEGQISYAIP QENQSLKVYC STQHPTEMQL LICHALGMNM HQVSVESRRM GGGFGGKESQ SAQWACIASL AAQKTGRPCK LRLDRDDDMS ATGKRHGFAY EWSVAFDDTG ILQGLKVQLA SNCGFSADLS GPVNERAICH IGNAYYLNAV ELRNLRCKTN TVSNTAYRGF GGPQGMFVIE NIIDDIARYL GCDPVEIRQR NFFAEQPGGG RDRMHYGAEV RDNVAPKLVA ELLQSSDYAK RRQTIHAFNQ NNDIIKRGIA LTPLMFGISF NAVHYNQAGA LVYVYMDGTV AITHGGTEMG QGLYTKVRQV AAHELGLPID SVRLIATDTS RVPNTSATAA SSGADLNGKA VQNACIKIRE RLAKLAAEIS QSEADQVQFE DSMVSTANGH SWTFPDLVQR AYMARVQLWD SGFYKTPEIH YDQVNHLGRP FFYYAYGAAV SEVAIDTLTG EMKVLRADIL HDVGQSINPA IDIGQIEGGF VQGMGWLTTE ELYWQPQGPH AGRLFTHAPS TYKIPTSVDI PHIFNVKLFN NQNQADTIYR SKAVGEPPFM LALSVFSAIR QAVQAAIPEN APLVLNAPAT AEEILRAIAI GRGKALAARP QAKM //