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Database: UniProt
Entry: V5XCQ0_MYCNE
LinkDB: V5XCQ0_MYCNE
Original site: V5XCQ0_MYCNE 
ID   V5XCQ0_MYCNE            Unreviewed;       257 AA.
AC   V5XCQ0;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=HAD family hydrolase {ECO:0000313|EMBL:AHC25792.1};
GN   ORFNames=D174_14880 {ECO:0000313|EMBL:AHC25792.1};
OS   Mycolicibacterium neoaurum VKM Ac-1815D.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=700508 {ECO:0000313|EMBL:AHC25792.1, ECO:0000313|Proteomes:UP000018763};
RN   [1] {ECO:0000313|EMBL:AHC25792.1, ECO:0000313|Proteomes:UP000018763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-1815D {ECO:0000313|EMBL:AHC25792.1,
RC   ECO:0000313|Proteomes:UP000018763};
RX   PubMed=24435872;
RA   Shtratnikova V.Y., Bragin E.Y., Dovbnya D.V., Pekov Y.A., Schelkunov M.I.,
RA   Strizhov N., Ivashina T.V., Ashapkin V.V., Donova M.V.;
RT   "Complete Genome Sequence of Sterol-Transforming Mycobacterium neoaurum
RT   Strain VKM Ac-1815D.";
RL   Genome Announc. 2:e01177-13(2014).
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.
CC       {ECO:0000256|PIRNR:PIRNR000915}.
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DR   EMBL; CP006936; AHC25792.1; -; Genomic_DNA.
DR   RefSeq; WP_023985811.1; NC_023036.2.
DR   AlphaFoldDB; V5XCQ0; -.
DR   KEGG; mne:D174_14880; -.
DR   eggNOG; COG0647; Bacteria.
DR   HOGENOM; CLU_043473_1_1_11; -.
DR   Proteomes; UP000018763; 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; IPR023214; HAD_sf.
DR   NCBIfam; TIGR01460; HAD-SF-IIA; 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:AHC25792.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000915-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000915-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018763}.
FT   ACT_SITE        11
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   ACT_SITE        13
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT   BINDING         207
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ   SEQUENCE   257 AA;  27617 MW;  C80D8836621149B3 CRC64;
     MSTTPQCWLT DMDGVLVREE HALPGAAEFL QALSDRQRPF LVLTNNSIFT PRDLAARLAR
     SGLIVPEESI WTSALATAAF LHDQLPGGSA YVIGEAGLTT ALHHVGYTLT DVGPDFVVLG
     ETRTYSFEAI TKAIRLILGG ARFIATNPDV SGPSAEGPLP ATGSVAALIT KATGREPYFV
     GKPNPMMFRS AMNRIDAHSE GTVMIGDRMD TDVVAGIEAG LETILVLTGS TTREEIERYP
     FRPSRVFESI ADVIELV
//
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