UXAB_YERPE
ID UXAB_YERPE Reviewed; 483 AA.
AC Q8ZIC5; Q0WJ86;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Altronate oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00670};
DE EC=1.1.1.58 {ECO:0000255|HAMAP-Rule:MF_00670};
DE AltName: Full=Tagaturonate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00670};
DE AltName: Full=Tagaturonate reductase {ECO:0000255|HAMAP-Rule:MF_00670};
GN Name=uxaB {ECO:0000255|HAMAP-Rule:MF_00670};
GN OrderedLocusNames=YPO0580, y3599, YP_2900;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-altronate + NAD(+) = H(+) + keto-D-tagaturonate + NADH;
CC Xref=Rhea:RHEA:17813, ChEBI:CHEBI:15378, ChEBI:CHEBI:17360,
CC ChEBI:CHEBI:17886, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.58;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00670};
CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC interconversion. {ECO:0000255|HAMAP-Rule:MF_00670}.
CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family. UxaB
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00670}.
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DR EMBL; AL590842; CAL19260.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM87147.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS63082.1; -; Genomic_DNA.
DR PIR; AB0072; AB0072.
DR RefSeq; WP_002210409.1; NZ_WUCM01000101.1.
DR RefSeq; YP_002345652.1; NC_003143.1.
DR AlphaFoldDB; Q8ZIC5; -.
DR SMR; Q8ZIC5; -.
DR IntAct; Q8ZIC5; 2.
DR STRING; 214092.YPO0580; -.
DR PaxDb; Q8ZIC5; -.
DR DNASU; 1148546; -.
DR EnsemblBacteria; AAM87147; AAM87147; y3599.
DR EnsemblBacteria; AAS63082; AAS63082; YP_2900.
DR GeneID; 57974036; -.
DR KEGG; ype:YPO0580; -.
DR KEGG; ypk:y3599; -.
DR KEGG; ypm:YP_2900; -.
DR PATRIC; fig|214092.21.peg.837; -.
DR eggNOG; COG0246; Bacteria.
DR HOGENOM; CLU_027324_1_0_6; -.
DR OMA; VVIVRPI; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0009026; F:tagaturonate reductase activity; IBA:GO_Central.
DR GO; GO:0019698; P:D-galacturonate catabolic process; IBA:GO_Central.
DR GO; GO:0019592; P:mannitol catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.1040.10; -; 1.
DR HAMAP; MF_00670; Altron_oxidoreduct; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR023668; Altronate_OxRdtase.
DR InterPro; IPR013118; Mannitol_DH_C.
DR InterPro; IPR013131; Mannitol_DH_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01232; Mannitol_dh; 1.
DR Pfam; PF08125; Mannitol_dh_C; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..483
FT /note="Altronate oxidoreductase"
FT /id="PRO_0000170746"
FT BINDING 18..29
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00670"
FT CONFLICT 455
FT /note="A -> S (in Ref. 3; AAS63082)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 54907 MW; BDDB13837F6564B4 CRC64;
MQTLNRRDFP GRSHPDKIIQ FGEGNFLRAF VDWQIDLLNE HTDLNAGIVV IRPIDTDFPP
SLSTQDGLYT AVIRGLNEQG EAVRESRLIR SVNREINIYR QFDDYLALAR DANIRFMFSN
TTEAGIAWNE ADQFSDAPPS SFPAKLTRLL FERFEHFDGA ADKGWVLLPC ELIDYNGEAL
RELVLRYASH WQLPAAFTHW LTENNTFCST LVDRIVTGYP RDEVAALQTE LGYQDSFLDT
AEYFYLFVIQ GPQGLAQELR LDQLDLNVRI VDDIKPYKER KVAILNGAHT ALVPVAYLSG
LDTVGQTMDD AQISRFVEKT ITEEIVPVLD LPEDELLSFS QAVLSRFRNP FIQHQLLSIA
LNGMTKFRTR ILPQLLTYQQ QKGQLPPRLT FALAALIAFY RGEREGQTYP LQDDAHWLER
YSTLWNGVKH GDIALAELVN RVLSDANHWG QDLTAVPQLA NQVTEQLQTI LSRGMRAAVA
AYS
