ID   M0M1C3_9EURY            Unreviewed;       811 AA.
AC   M0M1C3;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Aldehyde oxidase {ECO:0000313|EMBL:EMA38190.1};
GN   ORFNames=C447_10695 {ECO:0000313|EMBL:EMA38190.1};
OS   Halococcus hamelinensis 100A6.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halococcaceae; Halococcus.
OX   NCBI_TaxID=1132509 {ECO:0000313|EMBL:EMA38190.1, ECO:0000313|Proteomes:UP000011566};
RN   [1] {ECO:0000313|EMBL:EMA38190.1, ECO:0000313|Proteomes:UP000011566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=100A6 {ECO:0000313|EMBL:EMA38190.1,
RC   ECO:0000313|Proteomes:UP000011566};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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:EMA38190.1}.
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; AOMB01000031; EMA38190.1; -; Genomic_DNA.
DR   RefSeq; WP_007693693.1; NZ_AOMB01000031.1.
DR   AlphaFoldDB; M0M1C3; -.
DR   PATRIC; fig|1132509.6.peg.2416; -.
DR   eggNOG; arCOG01167; Archaea.
DR   OrthoDB; 57164at2157; -.
DR   Proteomes; UP000011566; 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:UP000011566}.
FT   DOMAIN          31..144
FT                   /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT                   hammerhead"
FT                   /evidence="ECO:0000259|SMART:SM01008"
FT   REGION          791..811
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        795..811
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   811 AA;  87167 MW;  F0DBF55FCEE28F13 CRC64;
     MGIDTIESKD IDAEAVLGSA VERREDPALI TGEAEYTDDI QRPNMTHMAV VRSQYGHATI
     EGVDTSAAEE LDGVLAVYTG EDVDVPGMIP TGWQLPSLKN PDRPMLATDR VRHVGEAVAV
     VVAEDRYTAK DGVDLVDVDY DRQDATVDQS DALDDDAPRV HEELDDNVAF DFELGDESAT
     NDAFESAAHT AEVDLENQRV IPNAMEPRAA LAEYKPSSGD LELDLTTQNP HLHRLLLPSV
     LDVPEHKIHV RAPEVGGGFG SKSPLYPDEA LASWCSMQLG RPVKWTATRS ETYQTDAQAR
     AHQTTAEIAM DEDGTIQAVR VNTIANIGAY LSIFAAAIPT VLYAPLLSGQ YEIPSIYCNV
     VGSFTNTVPV DLYRGAGRPE ALYVVERLID LGAREVDMDP AEFRRHNFIG PDEFPYETPV
     AVTYDSGDYE PALDRALEML DYDDLRERQE ELRDEGRYIG VGFSSYIEAC GLAPSKIAGS
     LGAQAGLWEN GLVRMHPGGK VTAFCGTSGH GQGHKTTYAQ IVADELGVPY DDVEIVESDT
     DEVPEGRGTY GSRSAAVGGS ALSTSAGKVV EKARKIAAHQ LEADEADIDF EGGEFSVSGA
     PERSMTIQEV TQQAYLAQDL PEGMEPGLEE TAFYDPENFV FPFGTHAAVV EVDPESGEIE
     FENYVAVDDV GPQINPKIVE GQVHGGIAQG VGQALYEVAE YDDNGSLVTG SMQDYTVPKA
     EHIPHMETDS TETPSPHNPL GVKGVGEAGT IAAPQAVVNA VVDALEPFGV DHIDMPLTNE
     SVWQAVNESA VADGGTTDEA HEDAASDGGE N
//