ID K8EPP6_CARML Unreviewed; 254 AA.
AC K8EPP6;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 2.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=HAD-superhydrolase, subIIA family protein {ECO:0000313|EMBL:CCO10481.2};
GN Name=nagD {ECO:0000313|EMBL:CCO10481.2};
GN ORFNames=BN424_1017 {ECO:0000313|EMBL:CCO10481.2};
OS Carnobacterium maltaromaticum LMA28.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1234679 {ECO:0000313|EMBL:CCO10481.2, ECO:0000313|Proteomes:UP000000212};
RN [1] {ECO:0000313|Proteomes:UP000000212}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LMA28 {ECO:0000313|Proteomes:UP000000212};
RX PubMed=23405327; DOI=10.1128/genomeA.00115-12;
RA Cailliez-Grimal C., Chaillou S., Anba-Mondoloni J., Loux V., Afzal M.I.,
RA Rahman A., Kergourlay G., Champomier-Verges M.C., Zagorec M., Dalgaard P.,
RA Leisner J.J., Prevost H., Revol-Junelles A.M., Borges F.;
RT "Complete Chromosome Sequence of Carnobacterium maltaromaticum LMA 28.";
RL Genome Announc. 1:0-0(2013).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000915-3};
CC Note=Divalent metal ions. Mg(2+) is the most effective.
CC {ECO:0000256|PIRSR:PIRSR000915-3};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. NagD family.
CC {ECO:0000256|ARBA:ARBA00006696}.
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DR EMBL; HE999757; CCO10481.2; -; Genomic_DNA.
DR RefSeq; WP_015075873.1; NC_019425.2.
DR AlphaFoldDB; K8EPP6; -.
DR STRING; 1234679.BN424_1017; -.
DR KEGG; cml:BN424_1017; -.
DR eggNOG; COG0647; Bacteria.
DR HOGENOM; CLU_043473_1_1_9; -.
DR OrthoDB; 9810449at2; -.
DR Proteomes; UP000000212; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd07530; HAD_Pase_UmpH-like; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006357; HAD-SF_hydro_IIA.
DR InterPro; IPR006354; HAD-SF_hydro_IIA_hyp1.
DR InterPro; IPR023214; HAD_sf.
DR NCBIfam; TIGR01460; HAD-SF-IIA; 1.
DR NCBIfam; TIGR01457; HAD-SF-IIA-hyp2; 1.
DR PANTHER; PTHR19288; 4-NITROPHENYLPHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR19288:SF46; HALOACID DEHALOGENASE-LIKE HYDROLASE DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF13344; Hydrolase_6; 1.
DR Pfam; PF13242; Hydrolase_like; 1.
DR PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
DR SFLD; SFLDG01139; C2.A:_Pyridoxal_Phosphate_Phos; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CCO10481.2};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000915-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000915-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000000212}.
FT ACT_SITE 9
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT ACT_SITE 11
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT BINDING 206
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ SEQUENCE 254 AA; 27859 MW; 3493E7CF25993EB4 CRC64;
MKYKGYLIDL DGTMYRGSEP IPAATAFIKR LQAEKIPFLF VTNNTTKSQE EVVKNLSTNF
DIHVTEAEVY TGSIATAAYL KSLNKGNKVY AIGEAGLKLA LSEAGFVEEE TNPDYVVVAL
DRNVHYHNFE LATLAIHRGA RFISTNKDTN LPSEKGLIPG AGALTALITA STKKQPTYIG
KPEAIIMEEA LKVIGLDKSD VLMVGDNYET DIMAGIQNEI DSLLVLSGFT SEKDLEKVAK
QPTYVVKSLA EWEF
//
