ID A0A0P0A1R3_9RHOB Unreviewed; 397 AA.
AC A0A0P0A1R3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Mannonate dehydratase {ECO:0000256|ARBA:ARBA00012927, ECO:0000256|HAMAP-Rule:MF_00106};
DE EC=4.2.1.8 {ECO:0000256|ARBA:ARBA00012927, ECO:0000256|HAMAP-Rule:MF_00106};
DE AltName: Full=D-mannonate hydro-lyase {ECO:0000256|HAMAP-Rule:MF_00106};
GN Name=uxuA {ECO:0000256|HAMAP-Rule:MF_00106};
GN ORFNames=IMCC12053_2759 {ECO:0000313|EMBL:ALI56706.1},
GN SAMN05444421_106144 {ECO:0000313|EMBL:SFK63570.1};
OS Celeribacter marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1397108 {ECO:0000313|EMBL:ALI56706.1, ECO:0000313|Proteomes:UP000064920};
RN [1] {ECO:0000313|EMBL:ALI56706.1, ECO:0000313|Proteomes:UP000064920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC 12053 {ECO:0000313|EMBL:ALI56706.1,
RC ECO:0000313|Proteomes:UP000064920};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SFK63570.1, ECO:0000313|Proteomes:UP000181863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100036 {ECO:0000313|EMBL:SFK63570.1,
RC ECO:0000313|Proteomes:UP000181863};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the dehydration of D-mannonate.
CC {ECO:0000256|ARBA:ARBA00002713, ECO:0000256|HAMAP-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;
CC Evidence={ECO:0000256|ARBA:ARBA00001794, ECO:0000256|HAMAP-
CC Rule:MF_00106};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00106};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00106};
CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC interconversion. {ECO:0000256|ARBA:ARBA00004892, ECO:0000256|HAMAP-
CC Rule:MF_00106}.
CC -!- SIMILARITY: Belongs to the mannonate dehydratase family.
CC {ECO:0000256|ARBA:ARBA00007389, ECO:0000256|HAMAP-Rule:MF_00106}.
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DR EMBL; CP012023; ALI56706.1; -; Genomic_DNA.
DR EMBL; FOSM01000006; SFK63570.1; -; Genomic_DNA.
DR RefSeq; WP_062219877.1; NZ_FOSM01000006.1.
DR AlphaFoldDB; A0A0P0A1R3; -.
DR STRING; 1397108.IMCC12053_2759; -.
DR KEGG; cmar:IMCC12053_2759; -.
DR PATRIC; fig|1397108.4.peg.2821; -.
DR OrthoDB; 9780250at2; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000064920; Chromosome.
DR Proteomes; UP000181863; Unassembled WGS sequence.
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; 1.
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 {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00106};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00106};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00106};
KW Reference proteome {ECO:0000313|Proteomes:UP000064920}.
SQ SEQUENCE 397 AA; 43509 MW; 1F060D74FD093BCB CRC64;
MQESWRWYGP LDKIALSQIA QTGAGGIVTS LHEIPYGEVW TRAAIAARKS LIADARHGQV
WNVVESLPIH ERIKRGEGDL SGLFANYRQS MANLAAEGIT TICYNFMPLI DWTRTALANP
LPNGGTSLRF EQAQIAALEL HMLERDGAEA DFSDDVKARA KVWFDASTAD DREALINAVM
AGLPGAYDRY DVPALKHALT LYSGMGRDDI RANYARFLAE VIPAAQDLGM SFCVHPDDPP
RDIFGLPRVV SNAEDIAWIF DQQDAVENGL TLCAGSLGAN PANDIPAIAR RFAERIHFIH
LRNVRKDADG SFEEAAHLEG DTDMVALIAA LLAEESRRKD IGRSDTNIPW RPDHGHELLS
DIGSGTHPGY PLIGRLRGLA EIRGIIAALS HSQVTFT
//
