ID A0A1H3M0T7_9PROT Unreviewed; 559 AA.
AC A0A1H3M0T7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E {ECO:0000313|EMBL:SDY70173.1};
GN ORFNames=SAMN05421754_101831 {ECO:0000313|EMBL:SDY70173.1};
OS Nitrosomonas sp. Nm58.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=200126 {ECO:0000313|EMBL:SDY70173.1, ECO:0000313|Proteomes:UP000199646};
RN [1] {ECO:0000313|Proteomes:UP000199646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm58 {ECO:0000313|Proteomes:UP000199646};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; FNPQ01000018; SDY70173.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3M0T7; -.
DR STRING; 200126.SAMN05421754_101831; -.
DR Proteomes; UP000199646; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0016791; F:phosphatase activity; IEA:UniProt.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 1.20.120.710; Haloacid dehalogenase hydrolase-like domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR048764; PylC_PurT_N.
DR NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR PANTHER; PTHR46470; N-ACYLNEURAMINATE-9-PHOSPHATASE; 1.
DR PANTHER; PTHR46470:SF2; N-ACYLNEURAMINATE-9-PHOSPHATASE; 1.
DR Pfam; PF13419; HAD_2; 1.
DR Pfam; PF21360; PylC-like_N; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000199646}.
FT DOMAIN 120..294
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 559 AA; 62978 MW; DD3A9DB04CC4B5F7 CRC64;
MSLRNILVIS GGGFQGLGLI KALRAVTGTR ILVGDCYAEN VARYFSDAFF LLPLIKEEQA
FLNFVLDLCE RESVNAIFAS TDYELELLAR HRDTFAAQNV TVYVSNIPLL ELANDKLLFY
RWLLREGLPC LPCYTTHQDT NAAFPLIGKP RHGWGSRGLH ILADRETTSA ISIEENEDLV
WQPCLKDFDE YSIDFSINVM GNISPLAFRR RIRSLGGFAI LCEPYAPENI QSIARLTIEH
LIPLGARGPM NLQILRAYDD TCWVSDLNPR AGTSMPLSLA IGLNPLAFLL TDGAVDSNFS
NHSSVQGSRA RTLRYLEERS IPDLQLNEVR GIVFDLDDTL LDQKAWMISK LELTWHEERA
VLPERAVFLS MALQIIEEGN RAYLFDALCL QLGLDDTIRL RLIETYRKAR PEDIPLYSDV
PSTLYQLRKL GYRIAILSDN PPVSQRQKLD VCGLLPLIDT LVLTAELGTQ KPDPHAFIEC
TRLLELPPDQ IVMVGDNLFR DMRGSFDAGY RHSFHVQRAG AFFNFNPNLA LRVSSVMLTC
TTITNLNELF WHLTGVATP
//