ID S7WVL2_9BACT Unreviewed; 387 AA.
AC S7WVL2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=mannonate dehydratase {ECO:0000256|ARBA:ARBA00012927};
DE EC=4.2.1.8 {ECO:0000256|ARBA:ARBA00012927};
GN ORFNames=ADICYQ_2833 {ECO:0000313|EMBL:EPR68113.1};
OS Cyclobacterium qasimii M12-11B.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Cyclobacterium.
OX NCBI_TaxID=641524 {ECO:0000313|EMBL:EPR68113.1, ECO:0000313|Proteomes:UP000014974};
RN [1] {ECO:0000313|EMBL:EPR68113.1, ECO:0000313|Proteomes:UP000014974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M12-11B {ECO:0000313|EMBL:EPR68113.1,
RC ECO:0000313|Proteomes:UP000014974};
RX PubMed=23950138;
RA Shivaji S., Ara S., Singh A., Kumar Pinnaka A.;
RT "Draft Genome Sequence of Cyclobacterium qasimii Strain M12-11BT, Isolated
RT from Arctic Marine Sediment.";
RL Genome Announc. 1:e00642-13(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:EPR68113.1}.
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DR EMBL; ATNM01000109; EPR68113.1; -; Genomic_DNA.
DR RefSeq; WP_020890091.1; NZ_ATNM01000109.1.
DR AlphaFoldDB; S7WVL2; -.
DR STRING; 641524.ADICYQ_2833; -.
DR PATRIC; fig|641524.5.peg.2806; -.
DR eggNOG; COG1312; Bacteria.
DR OrthoDB; 9780250at2; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000014974; Unassembled WGS sequence.
DR GO; GO:0008927; F:mannonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0006064; P:glucuronate catabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1.
DR InterPro; IPR004628; Man_deHydtase.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR PANTHER; PTHR30387; MANNONATE DEHYDRATASE; 1.
DR PANTHER; PTHR30387:SF2; MANNONATE DEHYDRATASE; 1.
DR Pfam; PF03786; UxuA; 1.
DR SUPFAM; SSF51658; Xylose isomerase-like; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:EPR68113.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..387
FT /note="mannonate dehydratase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004546371"
SQ SEQUENCE 387 AA; 43466 MW; C9C6E38F38E232C2 CRC64;
MKNILKTLQR RKFMKLFASG TAGALTTASV AMGADRSDSR PSANKLMPAK KLLMKVGCQS
GGTSEENLAF KARHGVYNMD GGMPKFIPGV GWDLEDSLRK RDACEKYGIS LDAYHLPLTS
AGIDRVQVPN IMLGKSPERD KEIEMIQQMI EVSAKSGVKL LNYNTTILPV LRTSRTIDPK
RGNASYSTWN YEEALKREQP MTIAGNVDAD EIFERIAYLL DRIVPVAEEY KVQLGNHIAD
PPVPDQYKGI MRWNSPEVFE GMKRFAKLSD SPYHGFNFCI GSIAEGLRDP KNDIFPIIEY
FGKQKQIFNV HLRNIKGNYN NFQEVYPDNG EMNFFHVIRA LRDVEFDGMI MPDHVPTHEA
EGASSQAFSF AYGHIIGILQ ALKDEEG
//
