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   27-MAR-2024, entry version 116.
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; Bacillota; 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.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 224308-BSU32510; -.
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   OrthoDB; 9773039at2; -.
DR   PhylomeDB; O32147; -.
DR   BioCyc; BSUB:BSU32510-MONOMER; -.
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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR003777; XdhC_CoxI.
DR   InterPro; IPR027051; XdhC_Rossmann_dom.
DR   PANTHER; PTHR30388; ALDEHYDE OXIDOREDUCTASE MOLYBDENUM COFACTOR ASSEMBLY PROTEIN; 1.
DR   PANTHER; PTHR30388:SF6; XANTHINE DEHYDROGENASE SUBUNIT A-RELATED; 1.
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
//