UXAC_CAUVC
ID UXAC_CAUVC Reviewed; 487 AA.
AC Q9A874;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=CC_1490;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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; AE005673; AAK23469.1; -; Genomic_DNA.
DR PIR; A87434; A87434.
DR RefSeq; NP_420301.1; NC_002696.2.
DR RefSeq; WP_010919364.1; NC_002696.2.
DR PDB; 2Q01; X-ray; 2.34 A; A/B/C=2-487.
DR PDBsum; 2Q01; -.
DR AlphaFoldDB; Q9A874; -.
DR SMR; Q9A874; -.
DR STRING; 190650.CC_1490; -.
DR EnsemblBacteria; AAK23469; AAK23469; CC_1490.
DR KEGG; ccr:CC_1490; -.
DR PATRIC; fig|190650.5.peg.1517; -.
DR eggNOG; COG1904; Bacteria.
DR HOGENOM; CLU_044465_0_0_5; -.
DR OMA; TDHGHPT; -.
DR BioCyc; CAULO:CC1490-MON; -.
DR UniPathway; UPA00246; -.
DR EvolutionaryTrace; Q9A874; -.
DR Proteomes; UP000001816; 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 1: Evidence at protein level;
KW 3D-structure; Isomerase; Reference proteome.
FT CHAIN 1..487
FT /note="Uronate isomerase"
FT /id="PRO_0000172766"
FT TURN 9..12
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:2Q01"
FT TURN 29..32
FT /evidence="ECO:0007829|PDB:2Q01"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 45..49
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 65..72
FT /evidence="ECO:0007829|PDB:2Q01"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:2Q01"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 112..123
FT /evidence="ECO:0007829|PDB:2Q01"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 136..147
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:2Q01"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:2Q01"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 208..219
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 226..242
FT /evidence="ECO:0007829|PDB:2Q01"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 262..274
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 279..300
FT /evidence="ECO:0007829|PDB:2Q01"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 316..321
FT /evidence="ECO:0007829|PDB:2Q01"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:2Q01"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 341..347
FT /evidence="ECO:0007829|PDB:2Q01"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 369..373
FT /evidence="ECO:0007829|PDB:2Q01"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 391..405
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 423..443
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 449..460
FT /evidence="ECO:0007829|PDB:2Q01"
FT HELIX 462..467
FT /evidence="ECO:0007829|PDB:2Q01"
SQ SEQUENCE 487 AA; 55052 MW; 0FA4C80E085ED4F2 CRC64;
MARPLSFHED RLFPSDPATR SYARGLYALV KDLPIISPHG HTDPSWFATN APFQDATDLL
LAPDHYLFRM LYSQGVSLDA LKVRSKAGVP DTDPREAWRV FASHFYLFRG TPSWVWLNHV
FSQVFGFTEF LEASNADDYF DRITAALATD AFRPRALFDR FNIETLATTE GPHESLQHHA
AIRESGWGGH VITAYRPDAV IDFEDERSPR AFERFAETSG QDVYSWKSYL EAHRLRRQAF
IDAGATSSDH GHPTAATADL SDVEAEALFN SLVKGDVTPE KAELFRAQML TEMAKMSLDD
GLVMQIHPGS HRNHNVGLLN SHGRDKGADI PMRTEYVDAL KPLLTRLGND PRLSIILFTL
DETTYSRELA PLAGHYPVLK LGPSWWFHDS PEGMMRFREQ VTETAGFYNT VGFNDDTRAF
LSIPARHDVA RRVDSAFLAR MVAEHRMDLV EAEELIVDLT YNLPKKAYKL DQRPDWARPA
TLRAAAE
