XDHD_ECO57
ID XDHD_ECO57 Reviewed; 956 AA.
AC Q8XD64;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Probable hypoxanthine oxidase XdhD;
DE EC=1.-.-.-;
GN Name=xdhD; OrderedLocusNames=Z4220, ECs3754;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Probably has no xanthine dehydrogenase activity; however
CC deletion results in increased adenine sensitivity, suggesting that this
CC protein contributes to the conversion of adenine to guanine nucleotides
CC during purine salvage. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC Note=Binds 2 [2Fe-2S] centers. {ECO:0000305};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000250};
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AE005174; AAG58010.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37177.1; -; Genomic_DNA.
DR PIR; B91098; B91098.
DR PIR; F85943; F85943.
DR RefSeq; NP_311781.1; NC_002695.1.
DR RefSeq; WP_000583635.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XD64; -.
DR SMR; Q8XD64; -.
DR STRING; 155864.EDL933_4082; -.
DR EnsemblBacteria; AAG58010; AAG58010; Z4220.
DR EnsemblBacteria; BAB37177; BAB37177; ECs_3754.
DR GeneID; 916428; -.
DR KEGG; ece:Z4220; -.
DR KEGG; ecs:ECs_3754; -.
DR PATRIC; fig|386585.9.peg.3916; -.
DR eggNOG; COG1529; Bacteria.
DR eggNOG; COG2080; Bacteria.
DR HOGENOM; CLU_001681_2_3_6; -.
DR OMA; TSYIEWT; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR InterPro; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
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.
DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR InterPro; IPR017699; Mo-bd_YgfN/XdhD.
DR PANTHER; PTHR11908; PTHR11908; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR PIRSF; PIRSF000127; Xanthine_DH; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SUPFAM; SSF47741; SSF47741; 1.
DR SUPFAM; SSF54665; SSF54665; 1.
DR SUPFAM; SSF56003; SSF56003; 1.
DR TIGRFAMs; TIGR03313; Se_sel_red_Mo; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Iron; Iron-sulfur; Metal-binding; Molybdenum; Oxidoreductase;
KW Purine metabolism; Purine salvage; Reference proteome.
FT CHAIN 1..956
FT /note="Probable hypoxanthine oxidase XdhD"
FT /id="PRO_0000166097"
FT BINDING 414
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000255"
FT BINDING 445
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000255"
FT BINDING 727
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000255"
SQ SEQUENCE 956 AA; 103591 MW; BC047DE44B1BAC0C CRC64;
MIIHFTLNGA PQELTVNPGE NVQKLLFNMG MHSVRNSDDG FGFAGSDAII FNGNIVNASL
LIAAQLEKAD IRTAESLGKW NELSLVQQAM VDVGVVQSGY NDPAAALIIT DLLDRIAAPT
REEIDDALSG LFSRDAGWQQ YYQVIELAVA RKNNPQATID IAPTFRDDLE VIGKHYPKTD
AAKMVQAKPC YVEDRVTADA CVIKMLRSPH AHALITHLDV SKAEALPGVV HVITHLNCPD
IYYTPGGQSA PEPSPLDRRM FGKKMRHVGD RVAAVVAESE EIALEALKLI EVEYEVLKPV
MSIDEAMAED APVVHDEPVV YVAGAPDTLE DDNSHAAQRG EHMIINFPIG SRPRKNIAAS
IHGHIGDMDK GFADADVIIE RTYNSTQAQQ CPTETHICFT RMDGDRLVIH ASTQVPWHLR
RQVARLVDMK QHKVHVIKER VGGGFGSKQD ILLEEVCAWA TCVTGRPVLF RYTREEEFIA
NTSRHVAKVT VKLGAKKDGR LTAVKMDFRA NTGPYGNHSL TVPCNGPALS LPLYPCDNVD
FQVTTYYSNI CPNGAYQGYG APKGNFAITM ALAELAEQLQ IDQLEIIERN RVHEGQELKI
LGAIGEGKAP TSVPSAASCA LEEILRQGRE MIQWSSPKPQ NGDWHIGRGV AIIMQKSGIP
DIDQANCMIK LESDGTFIVH SGGADIGTGL DTVVTKLAAE VLHCPPQDVH VISGDTDHAL
FDKGAYASSG TCFSGNAARL AAENLREKIL FHGAQMLGEP VADVQLATPG VVRGKKGEVS
FGDIAHKGET GTGFGSLVGT GSYITPDFAF PYGANFAEVA VNTRTGEIRL DKFYALLDCG
TPVNPELALG QIYGATLRAI GHSMSEEIIY DAEGHPLTRD LRSYGAPKIG DIPRDFRAVL
VPSDDKVGPF GAKSISEIGV NGAAPAIATA IHDACGIWLR EWHFTPEKIL TALEKI
