Y1775_ARCFU
ID Y1775_ARCFU Reviewed; 330 AA.
AC O28499;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Putative aminohydrolase AF_1775;
DE EC=3.-.-.-;
GN OrderedLocusNames=AF_1775;
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).
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ATZ/TRZ family. {ECO:0000305}.
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DR EMBL; AE000782; AAB89475.1; -; Genomic_DNA.
DR PIR; F69471; F69471.
DR AlphaFoldDB; O28499; -.
DR SMR; O28499; -.
DR STRING; 224325.AF_1775; -.
DR DNASU; 1484998; -.
DR EnsemblBacteria; AAB89475; AAB89475; AF_1775.
DR KEGG; afu:AF_1775; -.
DR eggNOG; arCOG00692; Archaea.
DR HOGENOM; CLU_012358_1_0_2; -.
DR OMA; AVCPRAN; -.
DR PhylomeDB; O28499; -.
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; IPR006680; Amidohydro-rel.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..330
FT /note="Putative aminohydrolase AF_1775"
FT /id="PRO_0000122310"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
SQ SEQUENCE 330 AA; 37069 MW; 525AD9F7F35A6FB1 CRC64;
MGEYLTLPME VYSGILVTHE GVFHGDLIVE EMAFEESRVE KDDFVISPTF FNAHTHLGDA
ALREAPRLDL VSIVGPGGYK HRMLSQIDSK TLRQEVELEV RISRDAGTSH FLDFREGGKA
GLEIVKGIDG VLPLARPTSV EEAEEVEAFG FAYSSARDHD LKLMEEVREI ARRRKMLFAI
HAGEKDCADV DAALALEPDF VVHMNSCPEK IREFVEAEIP IVSCIRSNAF FGLLNKKSYE
LLSEYEKWML GTDNAMISTA SMLDEMHFAA YLIGKEKAIL RAATASYAVF GFRHGYVVFN
RNCSFRRTSD PLLTLVRRAG VKDIERVLIL