XDHC_BACSU
ID XDHC_BACSU Reviewed; 277 AA.
AC O32145;
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 C;
DE Short=XDHase subunit C;
DE EC=1.17.1.4;
GN Name=pucC; Synonyms=yurD; OrderedLocusNames=BSU32490;
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=FAD; Xref=ChEBI:CHEBI:57692; Evidence={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.
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DR EMBL; AL009126; CAB15239.1; -; Genomic_DNA.
DR PIR; C70017; C70017.
DR RefSeq; NP_391129.1; NC_000964.3.
DR RefSeq; WP_003228646.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32145; -.
DR SMR; O32145; -.
DR STRING; 224308.BSU32490; -.
DR PaxDb; O32145; -.
DR PRIDE; O32145; -.
DR EnsemblBacteria; CAB15239; CAB15239; BSU_32490.
DR GeneID; 936685; -.
DR KEGG; bsu:BSU32490; -.
DR PATRIC; fig|224308.179.peg.3518; -.
DR eggNOG; COG1319; Bacteria.
DR InParanoid; O32145; -.
DR OMA; KARMNIQ; -.
DR PhylomeDB; O32145; -.
DR BioCyc; BSUB:BSU32490-MON; -.
DR UniPathway; UPA00604; UER00661.
DR UniPathway; UPA00604; UER00662.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004854; F:xanthine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0009114; P:hypoxanthine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR InterPro; IPR017612; Xanthine_dehydrogenase_csu.
DR Pfam; PF00941; FAD_binding_5; 1.
DR SUPFAM; SSF55447; SSF55447; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR TIGRFAMs; TIGR03199; pucC; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; NAD; Oxidoreductase; Purine metabolism;
KW Reference proteome.
FT CHAIN 1..277
FT /note="Probable xanthine dehydrogenase subunit C"
FT /id="PRO_0000166099"
FT DOMAIN 7..176
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ SEQUENCE 277 AA; 30119 MW; 25D8C75D6D237961 CRC64;
MNGQVTKARM NIQLWRPAAL DEAYSLLEKL APDVCAASGS TLLQLQWDKG TLPKQHLVSL
EGIDEMRGIS TSDTHVSIGG LTSLNECRKN PLIKRALSCF SDAASAVAAP GIRSRATIGG
NIASKIGDFI PLLLVLGAEL IVYQKELIRL PLGAWLSEED FRTAIVTRVI IPRAEGERVF
YHKLGRRQAF TGAAAVAAGR FLKDGSIRLA AGHADITPRR LLDSEAKWMA PGWDPHELYK
TLIHELPFSS DVFMSAAYRK KAAANVIMAE LMAEGGE
