ID S7VQU2_9FLAO Unreviewed; 395 AA.
AC S7VQU2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=ADIWIN_2536 {ECO:0000313|EMBL:EPR72366.1};
OS Winogradskyella psychrotolerans RS-3.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=641526 {ECO:0000313|EMBL:EPR72366.1, ECO:0000313|Proteomes:UP000014962};
RN [1] {ECO:0000313|EMBL:EPR72366.1, ECO:0000313|Proteomes:UP000014962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS-3 {ECO:0000313|EMBL:EPR72366.1,
RC ECO:0000313|Proteomes:UP000014962};
RX PubMed=23950132;
RA Kumar Pinnaka A., Ara S., Singh A., Shivaji S.;
RT "Draft Genome Sequence of Winogradskyella psychrotolerans RS-3T, Isolated
RT from the Marine Transect of Kongsfjorden, Ny-Alesund, Svalbard, Arctic
RT Ocean.";
RL Genome Announc. 1:e00630-e00613(2013).
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}.
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:EPR72366.1}.
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DR EMBL; ATMR01000124; EPR72366.1; -; Genomic_DNA.
DR RefSeq; WP_020897441.1; NZ_ATMR01000124.1.
DR AlphaFoldDB; S7VQU2; -.
DR STRING; 641526.ADIWIN_2536; -.
DR PATRIC; fig|641526.4.peg.2517; -.
DR eggNOG; COG1312; Bacteria.
DR OrthoDB; 9780250at2; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000014962; 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:UP000014962}.
SQ SEQUENCE 395 AA; 44284 MW; 48A43863EE11B454 CRC64;
MRQNLEQTWR WYGPNDPVSL ADIKQAGATG IVSALHHIPN GEVWTVKEIN KRKEVIENIG
LTWSVVESVP IHENIKTKSG DYQLYFDNYK QTLLNLGACG IDTVCYNFMP VLDWTRTNLD
YEVSDGSTAL RFEAAAFAAF ELYLLKRPGA EHDYSDVQKQ TAAEFLKQAS ADEQKTLIRN
IIAGLPGAEE GYTLEEFNAI LATYNNIGPK ELKANLFSFL SEIIPAAEQA GVLMCIHPDD
PPFPILGLPR VVSTEQDIVD LYEAVPSHNN GLTFCTGSFG VRADNDLAGM VERLGERIHF
IHLRATKRDA EGNFHEADHL DGDVDMYAVM KALIKEQQKR IEEGRTDLRM PFRPDHGHKM
LDDLKKKTNP GYSGIGRLRG LAELRGLELG IRRSL
//