ID G1XZX5_9PROT Unreviewed; 401 AA.
AC G1XZX5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 03-MAY-2023, entry version 40.
DE RecName: Full=mannonate dehydratase {ECO:0000256|ARBA:ARBA00012927};
DE EC=4.2.1.8 {ECO:0000256|ARBA:ARBA00012927};
GN ORFNames=AZA_88904 {ECO:0000313|EMBL:EGY01182.1};
OS Nitrospirillum amazonense Y2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Nitrospirillum.
OX NCBI_TaxID=1003237 {ECO:0000313|EMBL:EGY01182.1, ECO:0000313|Proteomes:UP000018435};
RN [1] {ECO:0000313|EMBL:EGY01182.1, ECO:0000313|Proteomes:UP000018435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y2 (ATCC 35120) {ECO:0000313|Proteomes:UP000018435};
RX PubMed=21838888; DOI=10.1186/1471-2164-12-409;
RA Sant'anna F.H., Almeida L.G., Cecagno R., Reolon L.A., Siqueira F.M.,
RA Machado M.R., Vasconcelos A.T., Schrank I.S.;
RT "Genomic insights into the versatility of the plant growth-promoting
RT bacterium Azospirillum amazonense.";
RL BMC Genomics 12:409-409(2011).
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:EGY01182.1}.
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DR EMBL; AFBX01000447; EGY01182.1; -; Genomic_DNA.
DR RefSeq; WP_004272919.1; NZ_AFBX01000447.1.
DR AlphaFoldDB; G1XZX5; -.
DR PATRIC; fig|1003237.3.peg.2630; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000018435; 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 CDD; cd03322; RspA; 1.
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.
DR PROSITE; PS00909; MR_MLE_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Reference proteome {ECO:0000313|Proteomes:UP000018435}.
FT DOMAIN 128..256
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
SQ SEQUENCE 401 AA; 44637 MW; 72F0A9ED3F58D4F6 CRC64;
MKITDAYVIV TCPARNFVTL KIRTDEGVYG IGDATLNGRE LAVASYLTDH VIPCLIGRDP
HDIEDIWQYL YKGAYWRRGP VTMSAIAAVD TALWDIKAKV AGLPLYQLLG GKSRNGVMVY
AHANGQTVDD AMNQVQHYVD QGYKAIRIQA GVPGLKGVYG VAKGINYEPA TRGLPAESAW
STEAYLDFAP TLFAAARDRF GWDLHLLHDV HHRLTPIEAA RLGKALEPYR LFWMEDPTPA
ENQESFRLIR QHTTTPLAVG EVFNTIWDAK DLIQNQLIDY IRATVVHAGG ITHLRRIANL
AELYQIRTGS HGATDLSPVC MGAALHFDLW VPNFGIQERM VHEAVTESVF PHAYSFDQGY
MHPGEAPGHG VDIDEAEAAK YPYQPAYLPV ARLTDGTLWN W
//