ID Q8RE68_FUSNN Unreviewed; 275 AA.
AC Q8RE68;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=NagD protein {ECO:0000313|EMBL:AAL95451.1};
GN OrderedLocusNames=FN1255 {ECO:0000313|EMBL:AAL95451.1};
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=190304 {ECO:0000313|EMBL:AAL95451.1, ECO:0000313|Proteomes:UP000002521};
RN [1] {ECO:0000313|EMBL:AAL95451.1, ECO:0000313|Proteomes:UP000002521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 /
RC KCTC 2640 / LMG 13131 / VPI 4355 {ECO:0000313|Proteomes:UP000002521};
RX PubMed=11889109; DOI=10.1128/JB.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N., Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE009951; AAL95451.1; -; Genomic_DNA.
DR RefSeq; NP_604152.1; NC_003454.1.
DR AlphaFoldDB; Q8RE68; -.
DR STRING; 190304.FN1255; -.
DR PaxDb; 190304-FN1255; -.
DR EnsemblBacteria; AAL95451; AAL95451; FN1255.
DR KEGG; fnu:FN1255; -.
DR PATRIC; fig|190304.8.peg.1820; -.
DR eggNOG; COG0647; Bacteria.
DR HOGENOM; CLU_043473_1_2_0; -.
DR InParanoid; Q8RE68; -.
DR BioCyc; FNUC190304:G1FZS-1831-MONOMER; -.
DR Proteomes; UP000002521; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR CDD; cd16422; 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 Magnesium {ECO:0000256|PIRSR:PIRSR000915-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000915-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000002521}.
FT ACT_SITE 24
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT ACT_SITE 26
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT BINDING 24
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 26
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ SEQUENCE 275 AA; 31371 MW; 0384156E1AEFB3B8 CRC64;
MTPFILNLGG LMEKLENIKC YLLDMDGTIY LGNELINGAK EFLEKLKEKK IRYIFLTNNS
SKNKNRYVEK LNKLGIEAHR EDIFSSGEAT TIYLNKKKKG AKIFLLGTKD LEDEFEKAGF
ELVKERNKNI DFVVLGFDTT LTYEKLWIAC EYIANGIEYI ATHPDFNCPL ENGKFMPDAG
AMIAFIKAST EKEPTVIGKP NSHIIDAIIE KYDLKKSELA MVGDRLYTDI RTGIDNGLTS
ILVMSGETDK KMLEKTIYKP NYIFDSVKEL KEKIE
//
