ID UXUA_HAEIG Reviewed; 394 AA.
AC A5UFM4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Mannonate dehydratase {ECO:0000255|HAMAP-Rule:MF_00106};
DE EC=4.2.1.8 {ECO:0000255|HAMAP-Rule:MF_00106};
DE AltName: Full=D-mannonate hydro-lyase {ECO:0000255|HAMAP-Rule:MF_00106};
GN Name=uxuA {ECO:0000255|HAMAP-Rule:MF_00106};
GN OrderedLocusNames=CGSHiGG_02775;
OS Haemophilus influenzae (strain PittGG).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=374931;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PittGG;
RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA Ehrlich G.D.;
RT "Characterization and modeling of the Haemophilus influenzae core and
RT supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT nontypeable strains.";
RL Genome Biol. 8:R103.1-R103.18(2007).
CC -!- FUNCTION: Catalyzes the dehydration of D-mannonate. {ECO:0000255|HAMAP-
CC Rule:MF_00106}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O;
CC Xref=Rhea:RHEA:20097, ChEBI:CHEBI:15377, ChEBI:CHEBI:17767,
CC ChEBI:CHEBI:57990; EC=4.2.1.8; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00106};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00106};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00106};
CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC interconversion. {ECO:0000255|HAMAP-Rule:MF_00106}.
CC -!- SIMILARITY: Belongs to the mannonate dehydratase family.
CC {ECO:0000255|HAMAP-Rule:MF_00106}.
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; CP000672; ABQ99579.1; -; Genomic_DNA.
DR AlphaFoldDB; A5UFM4; -.
DR SMR; A5UFM4; -.
DR KEGG; hiq:CGSHiGG_02775; -.
DR HOGENOM; CLU_058621_2_0_6; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000001990; Chromosome.
DR GO; GO:0008927; F:mannonate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006064; P:glucuronate catabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 2.
DR HAMAP; MF_00106; UxuA; 1.
DR InterPro; IPR004628; Man_deHydtase.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR NCBIfam; TIGR00695; uxuA; 1.
DR PANTHER; PTHR30387; MANNONATE DEHYDRATASE; 1.
DR PANTHER; PTHR30387:SF2; MANNONATE DEHYDRATASE; 1.
DR Pfam; PF03786; UxuA; 1.
DR PIRSF; PIRSF016049; Man_dehyd; 1.
DR SUPFAM; SSF51658; Xylose isomerase-like; 1.
PE 3: Inferred from homology;
KW Iron; Lyase; Manganese.
FT CHAIN 1..394
FT /note="Mannonate dehydratase"
FT /id="PRO_1000034330"
SQ SEQUENCE 394 AA; 45386 MW; 676F7C5F5B53BFFB CRC64;
MEQAWRWYGP KDPVSLSDIR QAGATGIVTA LHHIPNGEIW RIEEIKKRKT EIENAGLSWS
VVESVPVHEE IKTQTGNYQK WINNYKQTLR NLAQCGIDTV CYNFMPVLDW TRTDLAYELP
DGSKALRFDH IAFAAFELHI LKRPDAEKAY SQEEQVAART YYDKMSEQDI TQLTRNIIAG
LPGAEEGYTL DEFQTQLDRY KDISSEKFRT HLAYFLNEIV PVAQEVGIKM AIHPDDPPRP
ILGLPRIVST IEDMQWFVET QPLPANGFTM CTGSYGVRSD NDLVKMTEQF ADRIYFAHLR
STQREDNPLT FHEAAHLEGD VDMFNMVKAL LNEEYRRLNQ GETRLIPMRP DHGHQMLDDL
RKKTNPGYSA IGRLKGLAEF RGLEMALKKV YFNK
//
