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Database: UniProt
Entry: A4A376_9GAMM
LinkDB: A4A376_9GAMM
Original site: A4A376_9GAMM 
ID   A4A376_9GAMM            Unreviewed;       786 AA.
AC   A4A376;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Xanthine dehydrogenase, molybdenum binding protein subunit apoprotein {ECO:0000313|EMBL:EAQ99149.1};
DE            EC=1.17.1.4 {ECO:0000313|EMBL:EAQ99149.1};
GN   ORFNames=KT71_15806 {ECO:0000313|EMBL:EAQ99149.1};
OS   Congregibacter litoralis KT71.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC   Congregibacter.
OX   NCBI_TaxID=314285 {ECO:0000313|EMBL:EAQ99149.1, ECO:0000313|Proteomes:UP000019205};
RN   [1] {ECO:0000313|EMBL:EAQ99149.1, ECO:0000313|Proteomes:UP000019205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT71 {ECO:0000313|EMBL:EAQ99149.1,
RC   ECO:0000313|Proteomes:UP000019205};
RX   PubMed=17299055; DOI=10.1073/pnas.0608046104;
RA   Fuchs B.M., Spring S., Teeling H., Quast C., Wulf J., Schattenhofer M.,
RA   Yan S., Ferriera S., Johnson J., Glockner F.O., Amann R.;
RT   "Characterization of a marine gammaproteobacterium capable of aerobic
RT   anoxygenic photosynthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2891-2896(2007).
RN   [2] {ECO:0000313|EMBL:EAQ99149.1, ECO:0000313|Proteomes:UP000019205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT71 {ECO:0000313|EMBL:EAQ99149.1,
RC   ECO:0000313|Proteomes:UP000019205};
RX   PubMed=19287491; DOI=10.1371/journal.pone.0004866;
RA   Spring S., Lunsdorf H., Fuchs B.M., Tindall B.J.;
RT   "The photosynthetic apparatus and its regulation in the aerobic
RT   gammaproteobacterium Congregibacter litoralis gen. nov., sp. nov.";
RL   PLoS ONE 4:E4866-E4866(2009).
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:EAQ99149.1}.
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DR   EMBL; AAOA02000001; EAQ99149.1; -; Genomic_DNA.
DR   RefSeq; WP_008295595.1; NZ_CM002299.1.
DR   AlphaFoldDB; A4A376; -.
DR   STRING; 314285.KT71_15806; -.
DR   eggNOG; COG4631; Bacteria.
DR   HOGENOM; CLU_001681_4_1_6; -.
DR   OrthoDB; 9758509at2; -.
DR   Proteomes; UP000019205; 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:EAQ99149.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019205}.
FT   DOMAIN          33..142
FT                   /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT                   hammerhead"
FT                   /evidence="ECO:0000259|SMART:SM01008"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   786 AA;  84603 MW;  5B2AC19B0AA8DC24 CRC64;
     MTDSSAATGR NHAGPRGSAG QGVAHESAAK HVSGEAIYID DMMAPKGTLH AYVGLSTIAH
     GVVNEMSLAA VKNAPGVVDV ITRDDIPGIT DIGPVFPGDP LMVGLGDTVE FHGQVLFAVA
     ATSYAAARKA AQLAKIEYSP LPACLSIEDG LAAKSFVRPA HFQRRGDAER GLENAAHRMQ
     GELQIGGQEQ MYLEGQASLC VPEEDGGMLV YSSTQNPTEG QKLVAEVLGV DFHQVTVDTR
     RMGGAFGGKE THANQWACLA AILARRTGRA VKLRLARADD MRATGKRHHF LSRYDVGFDD
     EGQIQALDLM LAGGCGMSPD LSDAIVDRAM FHCDNAYYLP DVAVAGHRVK THTVSNTAFR
     GFGGPQGMVA IEDIIDAIAR KTGMDPLDVR KKNLYTSAGG RDVTHYGQTI EQHVLPQIIE
     RLEQTSDYHA RREAIRAFNA DSTVIKKGLA LTPVKFGISF TAKHLNQAGA LIHVYTDGSI
     QLNHGGTEMG QGLYTKVAQV VARELQVDIA CIRCTATRTD KVPNTSPTAA SSGSDINGMA
     ALNAARKIRY RLTKFACEHF DVSEDAVVFA PNEVQVGAQS FTFAELVNLA YHQRISLSAT
     GFYRTPKIHY DRATATGRPF YYYANGACVS EVQVDTLTGE YRVERVDICH DVGNSLNPAI
     DIGQIEGGFI QGMGWLTNEE LAWDDAGRLS TTGPATYKIP AIGDTPAIFN VELLPDSPNA
     EATIFRSKAV GEPPLMLAIS VWSAIRDAVA SLGNYRVHPK LDTPATPERV LLACESLRKS
     ARERIE
//
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