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UXAA_BACSU
ID   UXAA_BACSU              Reviewed;         497 AA.
AC   O34673;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Altronate dehydratase;
DE            EC=4.2.1.7;
DE   AltName: Full=D-altronate hydro-lyase;
GN   Name=uxaA; Synonyms=yjmJ; OrderedLocusNames=BSU12390;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROBABLE OPERON STRUCTURE.
RC   STRAIN=168;
RX   PubMed=9579062; DOI=10.1099/00221287-144-4-877;
RA   Rivolta C., Soldo B., Lazarevic V., Joris B., Mauel C., Karamata D.;
RT   "A 35.7 kb DNA fragment from the Bacillus subtilis chromosome containing a
RT   putative 12.3 kb operon involved in hexuronate catabolism and a perfectly
RT   symmetrical hypothetical catabolite-responsive element.";
RL   Microbiology 144:877-884(1998).
RN   [2]
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   [3]
RP   SEQUENCE REVISION TO 19.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [4]
RP   PROBABLE OPERON STRUCTURE, AND INDUCTION.
RC   STRAIN=168 / MB24;
RX   PubMed=9882655; DOI=10.1128/jb.181.2.426-433.1999;
RA   Mekjian K.R., Bryan E.M., Beall B.W., Moran C.P. Jr.;
RT   "Regulation of hexuronate utilization in Bacillus subtilis.";
RL   J. Bacteriol. 181:426-433(1999).
CC   -!- FUNCTION: Catalyzes the dehydration of D-altronate. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-altronate = 2-dehydro-3-deoxy-D-gluconate + H2O;
CC         Xref=Rhea:RHEA:15957, ChEBI:CHEBI:15377, ChEBI:CHEBI:17360,
CC         ChEBI:CHEBI:57990; EC=4.2.1.7;
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC       interconversion.
CC   -!- INDUCTION: Induced by galacturonate, repressed by glucose.
CC       {ECO:0000305|PubMed:9882655}.
CC   -!- MISCELLANEOUS: Last gene in the exu locus which is required for
CC       galacturonate utilization.
CC   -!- SIMILARITY: Belongs to the UxaA family. {ECO:0000305}.
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DR   EMBL; AF015825; AAC46335.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13096.2; -; Genomic_DNA.
DR   PIR; D69853; D69853.
DR   RefSeq; NP_389121.2; NC_000964.3.
DR   RefSeq; WP_003245409.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O34673; -.
DR   SMR; O34673; -.
DR   STRING; 224308.BSU12390; -.
DR   PaxDb; O34673; -.
DR   EnsemblBacteria; CAB13096; CAB13096; BSU_12390.
DR   GeneID; 939837; -.
DR   KEGG; bsu:BSU12390; -.
DR   PATRIC; fig|224308.179.peg.1340; -.
DR   eggNOG; COG2721; Bacteria.
DR   InParanoid; O34673; -.
DR   OMA; MRHDKRE; -.
DR   PhylomeDB; O34673; -.
DR   BioCyc; BSUB:BSU12390-MON; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0008789; F:altronate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019698; P:D-galacturonate catabolic process; IBA:GO_Central.
DR   CDD; cd11613; SAF_AH_GD; 1.
DR   InterPro; IPR007392; Gal/Altron_deHydtase_C.
DR   InterPro; IPR013974; SAF.
DR   InterPro; IPR044144; UxaA/GarD_SAF.
DR   Pfam; PF04295; GD_AH_C; 1.
DR   Pfam; PF08666; SAF; 1.
DR   SMART; SM00858; SAF; 1.
PE   2: Evidence at transcript level;
KW   Iron; Lyase; Manganese; Reference proteome.
FT   CHAIN           1..497
FT                   /note="Altronate dehydratase"
FT                   /id="PRO_0000172282"
FT   CONFLICT        19
FT                   /note="D -> Y (in Ref. 1; AAC46335)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   497 AA;  54872 MW;  5B58AD93B572C3E9 CRC64;
     MKSFIKIHKQ DNVLLALRDI QKGERLHAYG VSIEVKDDIK RGHKIALQSI KENDSIVKYG
     FPIGHASQDI SIGEHIHVHN TKTNLSDIQL YSYTPRFDEN PYSNENRTFK GFRRENGDAG
     VRNELWIVPT VGCVNGIAEK MLQRFVRETG DIAPFDNVLV LKHQYGCSQL GDDHENTKQI
     LLNAIRHPNA GGVLVLGLGC ENNELARMKE ALQDVNLKRV KFLESQSVTD EMEAGVALLK
     EIHEAAKGDK REDIPLSELK IGLKCGGSDG FSGITANPLL GRFSDYLIAQ GGSTVLTEVP
     EMFGAETILM QRAANEEVFH KIVDLINDFK QYFIKHDQPV YENPSPGNKA GGISTLEDKS
     LGCTQKAGIS PVTDVLKYGE VLKTKGLTLL SAPGNDLIAS SALAAAGCQI VLFTTGRGTP
     FGTFVPTVKV ATNTELYEAK PHWIDFNAGL LAEDDVHEEY VLREFIHYMI EVASGQLVNH
     EKNDFKELAI FKSGVTL
 
 
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