XDHD_BACSU
ID XDHD_BACSU Reviewed; 745 AA.
AC O32144;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable xanthine dehydrogenase subunit D;
DE Short=XDHase subunit D;
DE EC=1.17.1.4;
GN Name=pucD; Synonyms=yurC; OrderedLocusNames=BSU32480;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION.
RC STRAIN=168;
RX PubMed=11344136; DOI=10.1128/jb.183.11.3293-3302.2001;
RA Schultz A.C., Nygaard P., Saxild H.H.;
RT "Functional analysis of 14 genes that constitute the purine catabolic
RT pathway in Bacillus subtilis and evidence for a novel regulon controlled by
RT the PucR transcription activator.";
RL J. Bacteriol. 183:3293-3302(2001).
CC -!- FUNCTION: Oxidizes hypoxanthine and xanthine to uric acid.
CC {ECO:0000269|PubMed:11344136}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + xanthine = H(+) + NADH + urate;
CC Xref=Rhea:RHEA:16669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17712, ChEBI:CHEBI:17775, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.17.1.4;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hypoxanthine + NAD(+) = H(+) + NADH + xanthine;
CC Xref=Rhea:RHEA:24670, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17368, ChEBI:CHEBI:17712, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.17.1.4;
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 -!- PATHWAY: Purine metabolism; hypoxanthine degradation; urate from
CC hypoxanthine: step 1/2.
CC -!- PATHWAY: Purine metabolism; hypoxanthine degradation; urate from
CC hypoxanthine: step 2/2.
CC -!- SUBUNIT: Could be composed of four subunits: PucA, PucC, PucD and PucE.
CC -!- INDUCTION: Expression is very low in excess nitrogen (glutamate plus
CC ammonia) and is induced during limiting-nitrogen conditions
CC (glutamate). Expression decreases when allantoin is added during
CC limiting-nitrogen conditions.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AL009126; CAB15238.1; -; Genomic_DNA.
DR PIR; B70017; B70017.
DR RefSeq; NP_391128.1; NC_000964.3.
DR RefSeq; WP_003243174.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32144; -.
DR SMR; O32144; -.
DR STRING; 224308.BSU32480; -.
DR PaxDb; O32144; -.
DR PRIDE; O32144; -.
DR EnsemblBacteria; CAB15238; CAB15238; BSU_32480.
DR GeneID; 936686; -.
DR KEGG; bsu:BSU32480; -.
DR PATRIC; fig|224308.179.peg.3517; -.
DR eggNOG; COG1529; Bacteria.
DR InParanoid; O32144; -.
DR OMA; MFTFGYR; -.
DR PhylomeDB; O32144; -.
DR BioCyc; BSUB:BSU32480-MON; -.
DR UniPathway; UPA00604; UER00661.
DR UniPathway; UPA00604; UER00662.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0004854; F:xanthine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0009114; P:hypoxanthine catabolic process; IEA:UniProtKB-UniPathway.
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; IPR017609; Xanthine_dehydrogenase_dsu.
DR PANTHER; PTHR11908; PTHR11908; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SUPFAM; SSF54665; SSF54665; 1.
DR SUPFAM; SSF56003; SSF56003; 1.
DR TIGRFAMs; TIGR03196; pucD; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Molybdenum; NAD; Oxidoreductase; Purine metabolism;
KW Reference proteome.
FT CHAIN 1..745
FT /note="Probable xanthine dehydrogenase subunit D"
FT /id="PRO_0000166098"
FT BINDING 204
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 235
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 508
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 745 AA; 80434 MW; C4A3EC5F0094EF8D CRC64;
MIINKPSRVR PDGRGKVTGE LKYMTDLSFP GMLYGKVLRS AYPHAEIVSV CTIKAEKMEG
VQAVVTHKDV PGLNRFGIVI PDQPVLCEDR VRYVGDAIAA VAAETEEIAE AALELIQVEY
KELEVMDSPE KALRPNAQRL HEDGNILHRA FFSNGDVEEG FQASDTVFEE TYELPRQMHT
YMETEGGVAV PEDDGGFTMY AGTQHGYKDR FQLARIFDIP EEKIRIVSSP MGGSFGGKDE
LNIQPYAALL ALKSGRPVKI HQTRKESVRS GIKRHPMKIT IKTGADHSGN LLAHDVKIVA
DTGAYATLGP AVLDFSVEHA AGPYRIPNIR TEGISVFTNN GVAGEFRGFG GNQITFALET
HLDRLSGMLG IDPLELRRKN IRKPHDLGPL EHRIAPTDGA AQVLNAISKS PILKKTSRNC
GYLQRGTGAA ITMHGGGLGF GRMDAAGGRL SLSSEGKITA SFGFEECGQG ILAAIEQIVM
EELGCAAEDI SIVIGDTAKV PKSGSSTASR GTSMVWHAIQ RLKKPFLAQL KKRAAEWSGC
SAENLIPGAA GLRDKNTKAL VVTYKELAEK GPLAEETAFD FPTTPDPVVG GHFLYSFGAA
AVEVEVDLLT GDVKLIDCEH AIAAGPVVSP QGYRGQIEGG AAMALGYTLM EEAKMTDGRY
AAENLDHYLI PGIKDVPDMK LIAIEDLMKG DVYGPRGVGE IGTIAITPAI VKAVHDAVGC
WINKLPISRE ELLEAIDRKG LKQWT
