ID A0A1N6HR93_9BURK Unreviewed; 392 AA.
AC A0A1N6HR93;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=L-rhamnonate dehydratase {ECO:0000256|HAMAP-Rule:MF_01288};
DE Short=RhamD {ECO:0000256|HAMAP-Rule:MF_01288};
DE EC=4.2.1.90 {ECO:0000256|HAMAP-Rule:MF_01288};
GN Name=rhmD {ECO:0000256|HAMAP-Rule:MF_01288};
GN ORFNames=SAMN05444165_1532 {ECO:0000313|EMBL:SIO22292.1};
OS Paraburkholderia phenazinium.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=60549 {ECO:0000313|EMBL:SIO22292.1, ECO:0000313|Proteomes:UP000185151};
RN [1] {ECO:0000313|EMBL:SIO22292.1, ECO:0000313|Proteomes:UP000185151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAS95 {ECO:0000313|EMBL:SIO22292.1,
RC ECO:0000313|Proteomes:UP000185151};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy-
CC L-rhamnonate (KDR). {ECO:0000256|HAMAP-Rule:MF_01288}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-rhamnonate = 2-dehydro-3-deoxy-L-rhamnonate + H2O;
CC Xref=Rhea:RHEA:23080, ChEBI:CHEBI:15377, ChEBI:CHEBI:58118,
CC ChEBI:CHEBI:58371; EC=4.2.1.90; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01288};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01288};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01288};
CC -!- SUBUNIT: Homooctamer; tetramer of dimers. {ECO:0000256|HAMAP-
CC Rule:MF_01288}.
CC -!- MISCELLANEOUS: Reaction proceeds via a syn dehydration.
CC {ECO:0000256|HAMAP-Rule:MF_01288}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. RhamD subfamily. {ECO:0000256|HAMAP-Rule:MF_01288}.
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DR EMBL; FSRU01000001; SIO22292.1; -; Genomic_DNA.
DR RefSeq; WP_074295103.1; NZ_FSRU01000001.1.
DR AlphaFoldDB; A0A1N6HR93; -.
DR OrthoDB; 103536at2; -.
DR Proteomes; UP000185151; Unassembled WGS sequence.
DR GO; GO:0050032; F:L-rhamnonate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009063; P:amino acid catabolic process; IEA:InterPro.
DR CDD; cd03327; MR_like_2; 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 HAMAP; MF_01288; Rhamnon_dehydrat; 1.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR023444; L-Rhamnon_dehydrat.
DR InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR InterPro; IPR046945; RHMD-like.
DR PANTHER; PTHR13794; ENOLASE SUPERFAMILY, MANDELATE RACEMASE; 1.
DR PANTHER; PTHR13794:SF58; MITOCHONDRIAL ENOLASE SUPERFAMILY MEMBER 1; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SFLD; SFLDS00001; Enolase; 1.
DR SFLD; SFLDF00006; rhamnonate_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 Lyase {ECO:0000256|HAMAP-Rule:MF_01288};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01288};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01288}; Reference proteome {ECO:0000313|Proteomes:UP000185151}.
FT DOMAIN 155..261
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 318
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01288"
FT BINDING 22
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01288"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01288"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01288"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01288"
FT BINDING 268
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01288"
FT BINDING 338
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01288"
FT SITE 291
FT /note="Increases basicity of active site His"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01288"
FT SITE 338
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01288"
SQ SEQUENCE 392 AA; 43980 MW; B5A31D54C762FCBE CRC64;
MAMPTIKHVR AFIVRGGGAD YHDQPDGHWI DDHISTPMAR YPEYRQSRQS FGINVLGTLV
VEIEASDGTV GFAVTTGGEI GAFIVEKHLA RFLEGQLVTD IEKMWDQMYF STLYYGRKGV
VLNTISGVDL ALWDLLAKVR KEPVYQLLGG PVRDELVFYA TGARPDLARE MGFIGGKLPL
QHGPAEGEAG LKKNLERLAE MRSRVGDDFW LMYDCWMSLD VPYATRLAQA AHEYGLKWIE
EALPPDDYWG YAELRRNVPR GMMVSTGEHE ATRWGFRMLL EMNCCDLIQP DVGWCGGITE
LIKISALADA HNVMVVPHGS SVYSYHFVVT RHNSPFAEFL MMAPKADEVV PMFTPLLLDE
PVPVNGRMKV PDTPGFGVRL NPECALVRPY PR
//
