ID X6MG75_RETFI Unreviewed; 425 AA.
AC X6MG75;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=mannonate dehydratase {ECO:0000256|ARBA:ARBA00012927};
DE EC=4.2.1.8 {ECO:0000256|ARBA:ARBA00012927};
GN ORFNames=RFI_24510 {ECO:0000313|EMBL:ETO12864.1};
OS Reticulomyxa filosa.
OC Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC Reticulomyxidae; Reticulomyxa.
OX NCBI_TaxID=46433 {ECO:0000313|EMBL:ETO12864.1, ECO:0000313|Proteomes:UP000023152};
RN [1] {ECO:0000313|EMBL:ETO12864.1, ECO:0000313|Proteomes:UP000023152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24332546;
RA Glockner G., Hulsmann N., Schleicher M., Noegel A.A., Eichinger L.,
RA Gallinger C., Pawlowski J., Sierra R., Euteneuer U., Pillet L.,
RA Moustafa A., Platzer M., Groth M., Szafranski K., Schliwa M.;
RT "The Genome of the Foraminiferan Reticulomyxa filosa.";
RL Curr. Biol. 0:0-0(2013).
CC -!- FUNCTION: Catalyzes the dehydration of D-mannonate.
CC {ECO:0000256|ARBA:ARBA00002713}.
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};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC interconversion. {ECO:0000256|ARBA:ARBA00004892}.
CC -!- SIMILARITY: Belongs to the mannonate dehydratase family.
CC {ECO:0000256|ARBA:ARBA00007389}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETO12864.1}.
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DR EMBL; ASPP01021012; ETO12864.1; -; Genomic_DNA.
DR AlphaFoldDB; X6MG75; -.
DR EnsemblProtists; ETO12864; ETO12864; RFI_24510.
DR OMA; GFTGYAR; -.
DR OrthoDB; 5482450at2759; -.
DR Proteomes; UP000023152; Unassembled WGS sequence.
DR GO; GO:0008927; F:mannonate dehydratase activity; IEA:InterPro.
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};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Reference proteome {ECO:0000313|Proteomes:UP000023152}.
SQ SEQUENCE 425 AA; 49413 MW; 89197B507304923D CRC64;
MRWFGPNDPV TLDEIRQTGC KGIVTALHDI PVGDIWSKKA IMERKKEIEK NALRWLVVES
VPVHESIKLR KKDNKASVDE CNQLIENYAT SLKNLSECGV HYVAFHFMPL LDWTRTQLEY
KCEDNTYALA FDYIDLCVFE QFILQFDEKE LLKRYSKEEI SAAKQRFEHE MTPKQVEQLK
NAIISGMPGC VNSKYDSSVD MFKKQLSLYV DVSKQQLRDN LLYFLGQIVP VCEKYHVNLA
LHPDDPPFDI LGIPRIVSTA QDLDFILSLF YSVKSKRNGI TLCVGSYASR EDNNVVEITR
KFKDRVNFVH LRNVAKHPSQ RRTFVESNHL SGDVDMFEVM NILLHEMKHR AESKTDDRLD
VCLRPDHGHI MLHDFYMKNV LKVAINPGYT LYGRFKGLCE LRGLQMALQR VLKFKTHQDI
MQCKL
//
