ID Q2G1L5_STAA8 Unreviewed; 511 AA.
AC Q2G1L5;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=Bifunctional metallophosphatase/5'-nucleotidase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=SAOUHSC_00107 {ECO:0000313|EMBL:ABD29288.1};
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061 {ECO:0000313|EMBL:ABD29288.1, ECO:0000313|Proteomes:UP000008816};
RN [1] {ECO:0000313|Proteomes:UP000008816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47 {ECO:0000313|Proteomes:UP000008816};
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington D.C
RL (2006).
RN [2] {ECO:0007829|PDB:3QFK}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 2-511 IN COMPLEX WITH MANGANESE
RP AND ZINC.
RG Center for Structural Genomics of Infectious Diseases (CSGID);
RA Minasov G., Wawrzak Z., Krishna S.N., Halavaty A., Shuvalova L.,
RA Dubrovska I., Winsor J., Kiryukhina O., Bagnoli F., Falugi F.,
RA Bottomley M., Grandi G., Anderson W.F.;
RT "2.05 Angstrom Crystal Structure of Putative 5'-Nucleotidase from
RT Staphylococcus aureus in complex with alpha-ketoglutarate.";
RL Submitted (JAN-2011) to the PDB data bank.
RN [3] {ECO:0007829|PDB:4Q7F}
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 2-511 IN COMPLEX WITH MAGNESIUM
RP AND MANGANESE.
RG Center for Structural Genomics of Infectious Diseases (CSGID);
RA Minasov G., Nocadello S., Shuvalova L., Dubrovska I., Winsor J.,
RA Bagnoli F., Falugi F., Bottomley M., Grandi G., Anderson W.F.;
RT "1.98 Angstrom Crystal Structure of Putative 5'-Nucleotidase from
RT Staphylococcus aureus in complex with Adenosine.";
RL Submitted (APR-2014) to the PDB data bank.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC {ECO:0000256|RuleBase:RU362119}.
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DR EMBL; CP000253; ABD29288.1; -; Genomic_DNA.
DR RefSeq; WP_000065035.1; NZ_LS483365.1.
DR RefSeq; YP_498707.1; NC_007795.1.
DR PDB; 3QFK; X-ray; 2.05 A; A=2-511.
DR PDB; 4Q7F; X-ray; 1.98 A; A=2-511.
DR PDBsum; 3QFK; -.
DR PDBsum; 4Q7F; -.
DR AlphaFoldDB; Q2G1L5; -.
DR SMR; Q2G1L5; -.
DR STRING; 93061.SAOUHSC_00107; -.
DR PaxDb; 1280-SAXN108_0131; -.
DR GeneID; 3919816; -.
DR KEGG; sao:SAOUHSC_00107; -.
DR PATRIC; fig|93061.5.peg.96; -.
DR eggNOG; COG0737; Bacteria.
DR HOGENOM; CLU_005854_4_4_9; -.
DR OrthoDB; 9775118at2; -.
DR EvolutionaryTrace; Q2G1L5; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008252; F:nucleotidase activity; IEA:UniProt.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006146; 5'-Nucleotdase_CS.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR PANTHER; PTHR11575:SF6; 2',3'-CYCLIC-NUCLEOTIDE 2'-PHOSPHODIESTERASE_3'-NUCLEOTIDASE; 1.
DR PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:3QFK, ECO:0007829|PDB:4Q7F};
KW Hydrolase {ECO:0000256|RuleBase:RU362119};
KW Metal-binding {ECO:0007829|PDB:3QFK, ECO:0007829|PDB:4Q7F};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362119};
KW Reference proteome {ECO:0000313|Proteomes:UP000008816};
KW Zinc {ECO:0007829|PDB:3QFK}.
FT DOMAIN 6..234
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 317..472
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:4Q7F"
FT BINDING 11
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4Q7F"
FT BINDING 11
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:3QFK"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007829|PDB:3QFK"
FT BINDING 13
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4Q7F"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007829|PDB:3QFK"
FT BINDING 56
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:4Q7F"
FT BINDING 56
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:3QFK"
FT BINDING 56
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4Q7F"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007829|PDB:3QFK"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:4Q7F"
FT BINDING 93
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:3QFK"
FT BINDING 94
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0007829|PDB:3QFK"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:4Q7F"
FT BINDING 191
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:3QFK"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:4Q7F"
FT BINDING 231
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:3QFK"
FT BINDING 233
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4Q7F"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007829|PDB:3QFK"
FT BINDING 372
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0007829|PDB:3QFK"
SQ SEQUENCE 511 AA; 58110 MW; E901F488CFA0DD69 CRC64;
MSNIAFYVVS DVHGYIFPTD FTSRNQYQPM GLLLANHVIE QDRRQYDQSF KIDNGDFLQG
SPFCNYLIAH SGSSQPLVDF YNRMAFDFGT LGNHEFNYGL PYLKDTLRRL NYPVLCANIY
ENDSTLTDNG VKYFQVGDQT VGVIGLTTQF IPHWEQPEHI QSLTFHSAFE ILQQYLPEMK
RHADIIVVCY HGGFEKDLES GTPTEVLTGE NEGYAMLEAF SKDIDIFITG HQHRQIAERF
KQTAVIQPGT RGTTVGRVVL STDEYENLSV ESCELLPVID DSTFTIDEDD QHLRKQLEDW
LDYEITTLPY DMTINHAFEA RVAPHPFTNF MNYALLEKSD ADVACTALFD SASGFKQVVT
MRDVINNYPF PNTFKVLAVS GAKLKEAIER SAEYFDVKND EVSVSADFLE PKPQHFNYDI
YGGVSYTIHV GRPKGQRVSN MMIQGHAVDL KQTYTICVNN YRAVGGGQYD MYIDAPVVKD
IQVEGAQLLI DFLSNNNLMR IPQVVDFKVE K
//
