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Database: UniProt
Entry: N0E2E2_9MICO
LinkDB: N0E2E2_9MICO
Original site: N0E2E2_9MICO 
ID   N0E2E2_9MICO            Unreviewed;       824 AA.
AC   N0E2E2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Nicotine dehydrogenase chain C {ECO:0000313|EMBL:CCH69951.1};
GN   ORFNames=BN10_460052 {ECO:0000313|EMBL:CCH69951.1};
OS   Phycicoccus elongatus Lp2.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Phycicoccus.
OX   NCBI_TaxID=1193181 {ECO:0000313|EMBL:CCH69951.1, ECO:0000313|Proteomes:UP000013167};
RN   [1] {ECO:0000313|EMBL:CCH69951.1, ECO:0000313|Proteomes:UP000013167}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lp2 {ECO:0000313|EMBL:CCH69951.1,
RC   ECO:0000313|Proteomes:UP000013167};
RX   PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA   Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA   Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA   Nielsen K.L., Nielsen P.H.;
RT   "A metabolic model for members of the genus Tetrasphaera involved in
RT   enhanced biological phosphorus removal.";
RL   ISME J. 7:543-554(2013).
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:CCH69951.1}.
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DR   EMBL; CAIZ01000115; CCH69951.1; -; Genomic_DNA.
DR   RefSeq; WP_010849827.1; NZ_HF570956.1.
DR   AlphaFoldDB; N0E2E2; -.
DR   STRING; 1193181.BN10_460052; -.
DR   eggNOG; COG1529; Bacteria.
DR   HOGENOM; CLU_001681_2_0_11; -.
DR   OrthoDB; 9758509at2; -.
DR   Proteomes; UP000013167; 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: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   Reference proteome {ECO:0000313|Proteomes:UP000013167}.
FT   DOMAIN          28..143
FT                   /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT                   hammerhead"
FT                   /evidence="ECO:0000259|SMART:SM01008"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   824 AA;  88000 MW;  536194B09E14C392 CRC64;
     MTAVDERPAE SAEIGKARRR KEDQRLITGR TKWTDNIVLP GMLHLAMVRS PFAHAKVTSI
     DTEAAKGATN VVAVYTAADF PDGMGACANA WPITPEQVTP DHLPMVTEHV ACAGEIVAVV
     VARSAAAARD AAELVDVDYE ELPAVLDAKE ALKDEVLAHP DKGTNKSAFW RLDSAEAGTG
     GSVDEAIAKA REDGIVIERE YRQQRLVPAF MEPRSTVVDP TGEQVTMWTS TQVPHILRFL
     IAATTGMPES KIRVIAPDVG GGFGGKLQTT PEEFITLAVA RKLGKPAKYT ETRSESLLSA
     HHGRDQYQML TLAATKDGTV TGLKVDLLAN LGAYVAIVGG GVPVLGAWMF HAIYKFPAYQ
     FNCQTVLTNT TWVDAYRGAG RPEATFAIER LMDELAAEVG VDPLEIREKN WIKHEEFPFV
     SVSGMTYDSG NYEAATARAK ELFGYDELRA EQKQRRQSGD PVQLGIGVST FTEMCGLAPS
     RVLGQLSYGA GGWESAAIRM LPTGKVEVIT GTSPHGQGHE TAWSQIVADR LGVPFDDVEV
     LHGDTAIAYK GLDTYGSRSL VVGGEAVVRA ADKVIEKAKP FAAHLLEASV DDLEFKDGRY
     AVKGTDKGVG ITEVALATFA SHNYPDHLEP GIDADATYDP VDFSFPHGTH LCAMEVDTET
     GASTIRKYVC VDDIGQVINP LIVEGQVHGG LVQGIAQALW EEAVYDDNGT LVTGSFVDYT
     LPTTADTINF VTDNTTSLAT TNTLGTKGVG EAGTIASTPA VVNAIVDAVR DRGIHDIQMP
     CTPARVWAAL QSAGSAEVAQ AQPHFHEEAA NNADPGTTGE GSGS
//
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