D89S1_ARCFU
ID D89S1_ARCFU Reviewed; 288 AA.
AC O29161;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Damage-control phosphatase AF_1104 {ECO:0000303|PubMed:27322068};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:O59272};
DE AltName: Full=Nucleotides phosphatase AF_1104 {ECO:0000303|PubMed:27322068};
GN OrderedLocusNames=AF_1104;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP DOMAIN.
RX PubMed=27322068; DOI=10.1038/nchembio.2108;
RA Huang L., Khusnutdinova A., Nocek B., Brown G., Xu X., Cui H., Petit P.,
RA Flick R., Zallot R., Balmant K., Ziemak M.J., Shanklin J.,
RA de Crecy-Lagard V., Fiehn O., Gregory J.F. III, Joachimiak A.,
RA Savchenko A., Yakunin A.F., Hanson A.D.;
RT "A family of metal-dependent phosphatases implicated in metabolite damage-
RT control.";
RL Nat. Chem. Biol. 12:621-627(2016).
RN [3] {ECO:0007744|PDB:2FFJ}
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
RG Joint Center for Structural Genomics (JCSG);
RT "Crystal structure of (2649480) from ARCHAEOGLOBUS FULGIDUS at 2.45 A
RT resolution.";
RL Submitted (DEC-2005) to the PDB data bank.
CC -!- FUNCTION: Metal-dependent phosphatase with probable damage-control
CC functions (By similarity). Could hydrolyze oxidatively damaged purine
CC nucleotides or their biosynthetic intermediates (By similarity).
CC {ECO:0000250|UniProtKB:O59272}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:O59272};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O59272};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000250|UniProtKB:O59272};
CC -!- DOMAIN: Subfamily I proteins are distinguished by three conserved
CC motifs: the CxxC motif localized near the N-terminus, the GNFE motif
CC localized about 40 residues from the C-terminus, and the KC motif
CC localized about 25 residues from the C-terminus (Probable). In the
CC crystal structures of the subfamily I proteins, the side chains of the
CC cysteines in the CxxC and KC motifs face each other across the rim of
CC the putative substrate-binding cleft, and the GNFE motif lies deep in
CC the cleft close to the metal-binding aspartate and asparagine
CC (Probable). the 3 conserved cysteines in motifs CxxC and KC play a key
CC role in the interaction with the Fe-containing chromophore, which is
CC not directly involved in catalysis (Probable).
CC {ECO:0000305|PubMed:27322068}.
CC -!- SIMILARITY: Belongs to the damage-control phosphatase family.
CC Nucleotides phosphatase I subfamily. {ECO:0000305}.
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; AE000782; AAB90134.1; -; Genomic_DNA.
DR PIR; G69387; G69387.
DR RefSeq; WP_010878600.1; NC_000917.1.
DR PDB; 2FFJ; X-ray; 2.45 A; A/B=1-288.
DR PDBsum; 2FFJ; -.
DR AlphaFoldDB; O29161; -.
DR SMR; O29161; -.
DR STRING; 224325.AF_1104; -.
DR DNASU; 1484326; -.
DR EnsemblBacteria; AAB90134; AAB90134; AF_1104.
DR GeneID; 24794709; -.
DR KEGG; afu:AF_1104; -.
DR eggNOG; arCOG04410; Archaea.
DR HOGENOM; CLU_071520_1_0_2; -.
DR OMA; FLLKAKC; -.
DR OrthoDB; 78551at2157; -.
DR PhylomeDB; O29161; -.
DR EvolutionaryTrace; O29161; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR036075; ARMT-1-like_metal-bd_sf.
DR InterPro; IPR002791; ARMT1-like_metal-bd.
DR InterPro; IPR014444; PH1575-like.
DR Pfam; PF01937; ARMT1-like_dom; 1.
DR PIRSF; PIRSF006593; UCP006593; 1.
DR SUPFAM; SSF111321; SSF111321; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Manganese; Metal-binding; Nickel;
KW Reference proteome.
FT CHAIN 1..288
FT /note="Damage-control phosphatase AF_1104"
FT /id="PRO_0000447507"
FT MOTIF 7..10
FT /note="Subfamily I CxxC motif"
FT /evidence="ECO:0000305|PubMed:27322068"
FT MOTIF 247..250
FT /note="Subfamily I GNFE-like motif"
FT /evidence="ECO:0000305|PubMed:27322068"
FT MOTIF 267..268
FT /note="Subfamily I KC motif"
FT /evidence="ECO:0000305|PubMed:27322068"
FT BINDING 160
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 161
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 194
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT HELIX 9..22
FT /evidence="ECO:0007829|PDB:2FFJ"
FT HELIX 26..42
FT /evidence="ECO:0007829|PDB:2FFJ"
FT HELIX 51..65
FT /evidence="ECO:0007829|PDB:2FFJ"
FT HELIX 72..95
FT /evidence="ECO:0007829|PDB:2FFJ"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:2FFJ"
FT HELIX 99..109
FT /evidence="ECO:0007829|PDB:2FFJ"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:2FFJ"
FT HELIX 123..137
FT /evidence="ECO:0007829|PDB:2FFJ"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:2FFJ"
FT HELIX 144..150
FT /evidence="ECO:0007829|PDB:2FFJ"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:2FFJ"
FT HELIX 164..176
FT /evidence="ECO:0007829|PDB:2FFJ"
FT STRAND 180..189
FT /evidence="ECO:0007829|PDB:2FFJ"
FT HELIX 197..202
FT /evidence="ECO:0007829|PDB:2FFJ"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:2FFJ"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:2FFJ"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:2FFJ"
FT HELIX 229..237
FT /evidence="ECO:0007829|PDB:2FFJ"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:2FFJ"
FT HELIX 246..252
FT /evidence="ECO:0007829|PDB:2FFJ"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:2FFJ"
FT HELIX 269..275
FT /evidence="ECO:0007829|PDB:2FFJ"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:2FFJ"
SQ SEQUENCE 288 AA; 31981 MW; B27C997E6ACA28D4 CRC64;
MKISPLCPSC LLGRVYYEAK LVTDDEDLIS QCVDESLKIL AENYSSRPIN AHLATRIHRR
VYEILGVEDP YAEVKARANE VARQVLPLAK EIVEGSDDPF KTAVIVSIVG NNFDYGVQGH
KVVEEEFRDF LKRKVQEGLK INDTERIKEL SSGKVVYLTD NAGEIFFDTL LMKEIKRRCE
KLTAVVRGRP IISDATIEDA RLARVDKIAD ELLTNGKGAI GIIMDELPDE TRKALEEADL
IVAKGMANYE CLSDGSLKPI AFLLTAKCEP VARDIGVNVG DMVAKVVE
