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Database: UniProt
Entry: K6DBP0_9BACI
LinkDB: K6DBP0_9BACI
Original site: K6DBP0_9BACI 
ID   K6DBP0_9BACI            Unreviewed;       784 AA.
AC   K6DBP0;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Xanthine dehydrogenase, molybdenum binding subunit {ECO:0000313|EMBL:EKN65739.1};
GN   ORFNames=BABA_19141 {ECO:0000313|EMBL:EKN65739.1};
OS   Neobacillus bataviensis LMG 21833.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX   NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN65739.1, ECO:0000313|Proteomes:UP000006316};
RN   [1] {ECO:0000313|EMBL:EKN65739.1, ECO:0000313|Proteomes:UP000006316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX   PubMed=23087684;
RA   Heylen K., Keltjens J.;
RT   "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT   reduction in Bacillus.";
RL   Front. Microbiol. 3:371-371(2012).
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:EKN65739.1}.
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DR   EMBL; AJLS01000127; EKN65739.1; -; Genomic_DNA.
DR   RefSeq; WP_007086821.1; NZ_AJLS01000127.1.
DR   AlphaFoldDB; K6DBP0; -.
DR   STRING; 1117379.BABA_19141; -.
DR   PATRIC; fig|1117379.3.peg.3964; -.
DR   eggNOG; COG1529; Bacteria.
DR   OrthoDB; 9759099at2; -.
DR   Proteomes; UP000006316; Unassembled WGS sequence.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; 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   InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
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.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006316}.
FT   DOMAIN          628..704
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
SQ   SEQUENCE   784 AA;  86127 MW;  E25CD0B854028F6A CRC64;
     MQEKPWKSVG KSEQRIDAVE KAAGTVRYLG DYSIPGLAHA KLVTSTHAHA KINNIDLTEA
     WKVPGVRAIV TGNMFPYHIG PILADRPPLA FEKVRYYGEP VAIIVADHEH QAKKAAQLVK
     VDYAPLPVVN SVQEAFKTGA PLIHENSGQY MKIISNVYPV QGTNIGSHIK IRKGDFIKTW
     EQCETKIKAS YSFNLSDHTA IEPRCARVEI NPAGKVIIHS TTQSPFTIKK VLNQFFNIDV
     GNIIVHTPLL GGAFGGKGNV QLEPLAYLAS KAVGGKLVKL EYEREDDLIT APCHIGLEAT
     ISLGTNKEGK LIAGQYTFLI DSGAYTDQAA GITRAMAIDC TGPYHIQNVW CDSYCMYTNH
     PFATSFRGYA HPELTFVVER TMDQLAQKLN MEPIELRKIN VIKPGNTSPT QTVLNANNIG
     DVEKCMERAK ELIQWDEGQR IEISKNKIKA KGISTFWKTS TTSTNAQSGA IIKFNADGSV
     FVNCAAIELG QGTKTVLAQI VSERLKMDIK KVHVTMEVNT QYDPHQWRTV ASSTTFLAGR
     AVMAAADDAI SQLKRTASIA MQCSMEDLEV GGGRVYLKPS PEYGIKIEDI ALGYKYPNGH
     AVEGQVVGHG TYIQRHLTPM DKETGFGKPG PWWSVGTQAV EIEYDTNDFT YKILKAVTVL
     DGGTIINPAM ATQQMRGGMY LGLSFASREA FIFDEKGKVL NPQLRTYQIM RFGEQPIEYL
     VDFIESPAAD GPYGARGIGE YGVIGMAGAL ANSLSTAAQV NLNHLPLIPE LIWKTRKEAR
     NDSV
//
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