IMAND_CATAD
ID IMAND_CATAD Reviewed; 429 AA.
AC C7PW26;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=D-galactonate dehydratase family member Caci_4410;
GN OrderedLocusNames=Caci_4410;
OS Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS B-24433 / ID139908).
OC Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC Catenulispora.
OX NCBI_TaxID=479433;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908;
RX PubMed=21304647; DOI=10.4056/sigs.17259;
RA Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT 139908).";
RL Stand. Genomic Sci. 1:119-125(2009).
RN [2]
RP FUNCTION, AND LACK OF D-MANNONATE DEHYDRATASE ACTIVITY.
RC STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908;
RX PubMed=24697546; DOI=10.1021/bi500264p;
RA Wichelecki D.J., Balthazor B.M., Chau A.C., Vetting M.W., Fedorov A.A.,
RA Fedorov E.V., Lukk T., Patskovsky Y.V., Stead M.B., Hillerich B.S.,
RA Seidel R.D., Almo S.C., Gerlt J.A.;
RT "Discovery of function in the enolase superfamily: D-mannonate and D-
RT gluconate dehydratases in the D-mannonate dehydratase subgroup.";
RL Biochemistry 53:2722-2731(2014).
CC -!- FUNCTION: Has no detectable activity with D-mannonate and with a panel
CC of 70 other acid sugars (in vitro), in spite of the conservation of the
CC residues that are expected to be important for catalytic activity and
CC cofactor binding. May have evolved a divergent function.
CC {ECO:0000269|PubMed:24697546}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. GalD subfamily. {ECO:0000305}.
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DR EMBL; CP001700; ACU73274.1; -; Genomic_DNA.
DR AlphaFoldDB; C7PW26; -.
DR SMR; C7PW26; -.
DR STRING; 479433.Caci_4410; -.
DR EnsemblBacteria; ACU73274; ACU73274; Caci_4410.
DR KEGG; cai:Caci_4410; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_6_1_11; -.
DR OMA; IRCHVST; -.
DR OrthoDB; 1825548at2; -.
DR Proteomes; UP000000851; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0009063; P:cellular amino acid catabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR InterPro; IPR034589; D-mannonate_dehydratase-like.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR034593; Mandelate_racemase_DgoD-like.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR PANTHER; PTHR48080; PTHR48080; 1.
DR PANTHER; PTHR48080:SF6; PTHR48080:SF6; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR PROSITE; PS00908; MR_MLE_1; 1.
PE 3: Inferred from homology;
KW Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..429
FT /note="D-galactonate dehydratase family member Caci_4410"
FT /id="PRO_0000429902"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="D-arabinonate"
FT /ligand_id="ChEBI:CHEBI:16157"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="D-arabinonate"
FT /ligand_id="ChEBI:CHEBI:16157"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="D-arabinonate"
FT /ligand_id="ChEBI:CHEBI:16157"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="D-arabinonate"
FT /ligand_id="ChEBI:CHEBI:16157"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="D-arabinonate"
FT /ligand_id="ChEBI:CHEBI:16157"
FT /evidence="ECO:0000250"
SQ SEQUENCE 429 AA; 46181 MW; 347E1B082FB905BC CRC64;
MTDANHLLDP SGALPQTRPP WTSRDSLRIT RVRAIVTAPE GQPLVVVRVD TSDDGLYGLG
CATFTQRYAA VAAAVDEHVG PLAVGRHPAD IEDITRLIHY SSYWRSGPVL NNALSGLDQA
LWDIAGKRAG MPVYELLGGR SRSAVEVYSH AAGGTIEATL DQAEELLAEG YRNVRLQLGG
PGLGTYGAPG TLGGYPRSPH PDGWAVEQYL RDAPRLFAAA RERLGDSVNL MHDVHSRLTP
KQAVVLARAL EPYRLSFLED VIAPELYDRL PEVRAASPVP IAVGEQIGSV PDAVRLVRDG
GVDLLRLHTS AVGGLTPTRK IVALCELLGV RTAFHSPADV SPVGVAANLA VDISTPAFGY
QESHTYNDAT HEVFPGTRVV REGHLYPAEE PGWGIEIDER AAAKFPPVKF LHERWSSGVR
RPDGGLEAP
