ID A0A085U0I3_9RHOB Unreviewed; 396 AA.
AC A0A085U0I3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=DW2_04189 {ECO:0000313|EMBL:KFE36480.1};
OS Thioclava atlantica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1317124 {ECO:0000313|EMBL:KFE36480.1, ECO:0000313|Proteomes:UP000028607};
RN [1] {ECO:0000313|Proteomes:UP000028607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13D2W-2 {ECO:0000313|Proteomes:UP000028607};
RA Lai Q., Li G., Shao Z.;
RT "Thioclava sp. 13D2W-2 Genome Sequencing.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KFE36480.1, ECO:0000313|Proteomes:UP000028607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13D2W-2 {ECO:0000313|EMBL:KFE36480.1,
RC ECO:0000313|Proteomes:UP000028607};
RX PubMed=25361528; DOI=10.1007/s10482-014-0320-3;
RA Liu Y., Lai Q., Du J., Xu H., Jiang L., Shao Z.;
RT "Thioclava indica sp. nov., isolated from surface seawater of the Indian
RT Ocean.";
RL Antonie Van Leeuwenhoek 107:297-304(2015).
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:KFE36480.1}.
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DR EMBL; AQRC01000002; KFE36480.1; -; Genomic_DNA.
DR RefSeq; WP_038143984.1; NZ_AQRC01000002.1.
DR AlphaFoldDB; A0A085U0I3; -.
DR STRING; 1317124.DW2_04189; -.
DR PATRIC; fig|1317124.6.peg.849; -.
DR eggNOG; COG1312; Bacteria.
DR OrthoDB; 9780250at2; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000028607; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:KFE36480.1};
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}.
SQ SEQUENCE 396 AA; 43438 MW; ABDAA85A3ADD9313 CRC64;
MIESWRWYGP DLDALSLPEI AQTGASGIVT ALHEIAYGEI WPREAVAARR AQLEKAGFHW
KVVESLPIHE RIKRGEGDLG PLFANYRQSM ANLAAEGVTT ICYNFMPVLD WTRTDLAHPL
PRGGSCLRFE AYRMAAFEIH MLGREAAEDA YDAPTRARAA SWFQSASEGE RDALLQAIMA
GLPGAFDRYD IAGLRQQIAL YDGIGPDEIR RNFKRFLDEV IPAAEDLGLR FAVHPDDPPR
DILGLPRVVS DAEDIAWILT AHDSPANGLT LCTGSLGANP ANDLPAIARR FADSIHFAHL
RNVVKDADGS FEEAAHLEGD TDMVAVIAVL LEEEARRRAL GRGDAAIPFR PDHGHVLLDD
VDRAAFPGYP LIGRMRGLAE LRGVIAALRA QGRADV
//
