ID A0A0Q7YWB8_9SPHN Unreviewed; 403 AA.
AC A0A0Q7YWB8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=mannonate dehydratase {ECO:0000256|ARBA:ARBA00012927};
DE EC=4.2.1.8 {ECO:0000256|ARBA:ARBA00012927};
GN ORFNames=ASD67_15835 {ECO:0000313|EMBL:KQZ60776.1};
OS Sphingopyxis sp. Root1497.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1736474 {ECO:0000313|EMBL:KQZ60776.1, ECO:0000313|Proteomes:UP000051141};
RN [1] {ECO:0000313|EMBL:KQZ60776.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1497 {ECO:0000313|EMBL:KQZ60776.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ60776.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1497 {ECO:0000313|EMBL:KQZ60776.1};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the dehydration of D-mannonate. Has no detectable
CC activity with a panel of 70 other acid sugars (in vitro).
CC {ECO:0000256|ARBA:ARBA00023758}.
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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC interconversion. {ECO:0000256|ARBA:ARBA00004892}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. GalD subfamily. {ECO:0000256|ARBA:ARBA00010339}.
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:KQZ60776.1}.
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DR EMBL; LMGF01000005; KQZ60776.1; -; Genomic_DNA.
DR RefSeq; WP_056349299.1; NZ_LMGF01000005.1.
DR AlphaFoldDB; A0A0Q7YWB8; -.
DR STRING; 1736474.ASD67_15835; -.
DR OrthoDB; 9802699at2; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000051141; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0008927; F:mannonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0009063; P:amino acid catabolic process; IEA:InterPro.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1.
DR InterPro; IPR034593; DgoD-like.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR034587; MAND.
DR InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR PANTHER; PTHR48080; D-GALACTONATE DEHYDRATASE-RELATED; 1.
DR PANTHER; PTHR48080:SF6; STARVATION-SENSING PROTEIN RSPA; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SFLD; SFLDS00001; Enolase; 1.
DR SFLD; SFLDF00001; mannonate_dehydratase; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR PROSITE; PS00908; MR_MLE_1; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277}.
FT DOMAIN 129..258
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
SQ SEQUENCE 403 AA; 44394 MW; E327CE6F8141F161 CRC64;
MPKIVSARVI VTSPGRNFVT LKITCDDGTT GVGDATLNGR ELAVASYLAD HVVPCLIGRD
AQQIGDIWNY LYKGAYWRRG PVTMTAIAAV DMALWDIKGK VAGLPVYQLL GGAARSGCMV
YGHANGATIA DTIEAALDYQ RQGYRAIRLQ CGVPGMASTY GVSKDRYFYE PADADLPSGN
IWSTEKYLRV VPELFAAARE ALGWDVHLLH DIHHRLTPIE AARLGKDLEP YRPFWIEDAT
PAEDQEAFRL IRQHTTTPLA VGEIFNSIWD CKALIENRLI DYIRATVLHA GGITHMRQIA
ALAELYQVRT GCHGATDLSP VTMAAALHFG LSIPNFGIQE YMRHTDETDA VFPHAYSLTD
GLMHPGEAPG LGVDIDEARA ETHPYARAYL PVNRLEDGTM WSW
//
