UXAC_STRA5
ID UXAC_STRA5 Reviewed; 466 AA.
AC Q8E0M9;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Uronate isomerase {ECO:0000255|HAMAP-Rule:MF_00675};
DE EC=5.3.1.12 {ECO:0000255|HAMAP-Rule:MF_00675};
DE AltName: Full=Glucuronate isomerase {ECO:0000255|HAMAP-Rule:MF_00675};
DE AltName: Full=Uronic isomerase {ECO:0000255|HAMAP-Rule:MF_00675};
GN Name=uxaC {ECO:0000255|HAMAP-Rule:MF_00675}; OrderedLocusNames=SAG0701;
OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=208435;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-611 / 2603 V/R;
RX PubMed=12200547; DOI=10.1073/pnas.182380799;
RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT "Complete genome sequence and comparative genomic analysis of an emerging
RT human pathogen, serotype V Streptococcus agalactiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucuronate = D-fructuronate; Xref=Rhea:RHEA:13049,
CC ChEBI:CHEBI:58720, ChEBI:CHEBI:59863; EC=5.3.1.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00675};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=aldehydo-D-galacturonate = keto-D-tagaturonate;
CC Xref=Rhea:RHEA:27702, ChEBI:CHEBI:12952, ChEBI:CHEBI:17886;
CC EC=5.3.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00675};
CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC interconversion. {ECO:0000255|HAMAP-Rule:MF_00675}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Uronate isomerase family. {ECO:0000255|HAMAP-Rule:MF_00675}.
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DR EMBL; AE009948; AAM99588.1; -; Genomic_DNA.
DR RefSeq; NP_687716.1; NC_004116.1.
DR RefSeq; WP_000885296.1; NC_004116.1.
DR AlphaFoldDB; Q8E0M9; -.
DR SMR; Q8E0M9; -.
DR STRING; 208435.SAG0701; -.
DR EnsemblBacteria; AAM99588; AAM99588; SAG0701.
DR KEGG; sag:SAG0701; -.
DR PATRIC; fig|208435.3.peg.707; -.
DR HOGENOM; CLU_044465_1_0_9; -.
DR OMA; TDHGHPT; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000000821; Chromosome.
DR GO; GO:0008880; F:glucuronate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006064; P:glucuronate catabolic process; IEA:InterPro.
DR HAMAP; MF_00675; UxaC; 1.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR003766; Uronate_isomerase.
DR Pfam; PF02614; UxaC; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome.
FT CHAIN 1..466
FT /note="Uronate isomerase"
FT /id="PRO_0000172788"
SQ SEQUENCE 466 AA; 53804 MW; F248002E2BADFC41 CRC64;
MAFNTETFML KNQAAIQLYE EVKRQPIFDY HCHLDPKDIF EDHIFDNIVD LWLGGDHYKW
RLMRANGISE AEITGPASNL EKFKAFARTL ERAYGNPVYH WSAMELKNVF GVNEILTESN
AEEIYHRLNH FLKEHKISPR RLIADSKVMF IGTTDHPLDT LEWHKKLAAD ESFKTVVAPT
FRPDEAFIEH RHFVDFITKL GDITQKEITD FSTFIAAMEE RIAYFAQNGC RASDISFTEI
VFEQTDELEL NDLFNKVCEG YIPNQSEISK WQTAVFMELC RLYKKYGFVT QVHFGALRNN
HSTIFEKLGA DVGVDSLGDQ VALTVNMNRL LDSLVKKDSL PKMIWYNLNP AYNIAVANTL
ANFQANELGV RSYLQFGAGW WFADTKLGMI SQMNALAEQG MLANFIGMLT DSRSFLSYQR
HDYFRRILCT YLGEWIEEGE VPEDYQALGS MAKDIAYQNA VNYFKN