Y1664_HAEIN
ID Y1664_HAEIN Reviewed; 251 AA.
AC P45305;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Uncharacterized metal-dependent hydrolase HI_1664 {ECO:0000305};
DE EC=3.1.-.- {ECO:0000305};
GN OrderedLocusNames=HI_1664;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:P0AFQ7};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000250|UniProtKB:P0AFQ7};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC TatD-type hydrolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC23310.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L42023; AAC23310.1; ALT_INIT; Genomic_DNA.
DR PIR; E64174; E64174.
DR RefSeq; NP_439806.2; NC_000907.1.
DR RefSeq; WP_005694391.1; NC_000907.1.
DR AlphaFoldDB; P45305; -.
DR SMR; P45305; -.
DR STRING; 71421.HI_1664; -.
DR EnsemblBacteria; AAC23310; AAC23310; HI_1664.
DR KEGG; hin:HI_1664; -.
DR PATRIC; fig|71421.8.peg.1742; -.
DR eggNOG; COG0084; Bacteria.
DR HOGENOM; CLU_031506_5_2_6; -.
DR PhylomeDB; P45305; -.
DR BioCyc; HINF71421:G1GJ1-1681-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01310; TatD_DNAse; 1.
DR InterPro; IPR018228; DNase_TatD-rel_CS.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR001130; TatD-like.
DR Pfam; PF01026; TatD_DNase; 1.
DR PIRSF; PIRSF005902; DNase_TatD; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR PROSITE; PS01137; TATD_1; 1.
DR PROSITE; PS01091; TATD_3; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..251
FT /note="Uncharacterized metal-dependent hydrolase HI_1664"
FT /id="PRO_0000202005"
FT BINDING 6
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT BINDING 8
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT BINDING 90
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT BINDING 90
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT BINDING 130
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT BINDING 154
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT BINDING 202
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFQ7"
SQ SEQUENCE 251 AA; 29335 MW; F95E9E6967CE9450 CRC64;
MLFDSHLHLD QLSDENIQQT LAHSKIIGML AVSTNLNSAK KLLNLKQTYP KKLYIAAGFH
PEQQLPSLEE QKKLFQWIDE HHSSISAIGE VGLPHYSKRE NPNLDYVPYI ELLERFILIA
KKWDLPLNLH IVHNDVEIAL ELLQKHNIQR AHFHWFKTDE KSFQKFFSTP YFASLTPDIL
WNSKTQYVAQ HLSLNRLMIE TDSPWQHEGF ERAGISEQLL AVLQKLAELK SLPLHSVQKQ
ILLNTQQFYR L
