XDHA_BACSU
ID XDHA_BACSU Reviewed; 330 AA.
AC O32147;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Probable xanthine dehydrogenase subunit A;
DE Short=XDHase subunit A;
DE EC=1.17.1.4;
GN Name=pucA; Synonyms=yurF; OrderedLocusNames=BSU32510;
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. PucA subunit
CC could exert a molybdenum cofactor recruiting function.
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 -!- 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; CAB15241.1; -; Genomic_DNA.
DR PIR; E70017; E70017.
DR RefSeq; NP_391131.1; NC_000964.3.
DR RefSeq; WP_003243519.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32147; -.
DR SMR; O32147; -.
DR STRING; 224308.BSU32510; -.
DR PaxDb; O32147; -.
DR EnsemblBacteria; CAB15241; CAB15241; BSU_32510.
DR GeneID; 938865; -.
DR KEGG; bsu:BSU32510; -.
DR PATRIC; fig|224308.179.peg.3520; -.
DR eggNOG; COG1975; Bacteria.
DR InParanoid; O32147; -.
DR OMA; EDDLSWG; -.
DR PhylomeDB; O32147; -.
DR BioCyc; BSUB:BSU32510-MON; -.
DR UniPathway; UPA00604; UER00661.
DR UniPathway; UPA00604; UER00662.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004854; F:xanthine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0009114; P:hypoxanthine catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR003777; XdhC_CoxI.
DR InterPro; IPR027051; XdhC_Rossmann_dom.
DR Pfam; PF13478; XdhC_C; 1.
DR Pfam; PF02625; XdhC_CoxI; 1.
PE 2: Evidence at transcript level;
KW NAD; Oxidoreductase; Purine metabolism; Reference proteome.
FT CHAIN 1..330
FT /note="Probable xanthine dehydrogenase subunit A"
FT /id="PRO_0000166100"
SQ SEQUENCE 330 AA; 36746 MW; E4A70B2155BE1902 CRC64;
MGNFHTMLDA LLEDQEEAVL ATIVQVEGSA YRKAGASMLF KKKGRRIGLL SGGCVEEDVF
QRISALGDQL TSTLIPYDMR SEDDLSWGMG AGCNGIIHVH AERITQEKRR HYEKVRDCLH
SGKAVTSVIK IESSHYLFLT ENGHFGNWPD APLQDIQRTV STLHLPHFDQ TTNMFIQRIE
PKPRLILFGA GPDNVPLANL AADTGFSVIV TDWRPAYCTS SLFPKADQLI TAFPEQMLSE
FQFFPHDAAV VATHHYQHDQ TIINFLFSQN LHYIGLLGSA NRTKRLLSGK HPPSHFYSPV
GLKIGAEGPE EIAVSVVAEI IQTRKRVAVV
