ID C0CTL4_9FIRM Unreviewed; 264 AA.
AC C0CTL4;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=HAD hydrolase, family IA, variant 1 {ECO:0000313|EMBL:EEG57509.1};
GN ORFNames=CLOSTASPAR_00312 {ECO:0000313|EMBL:EEG57509.1};
OS [Clostridium] asparagiforme DSM 15981.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Enterocloster.
OX NCBI_TaxID=518636 {ECO:0000313|EMBL:EEG57509.1, ECO:0000313|Proteomes:UP000004756};
RN [1] {ECO:0000313|EMBL:EEG57509.1, ECO:0000313|Proteomes:UP000004756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG57509.1,
RC ECO:0000313|Proteomes:UP000004756};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG57509.1, ECO:0000313|Proteomes:UP000004756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG57509.1,
RC ECO:0000313|Proteomes:UP000004756};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium asparagiforme (DSM 15981).";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEG57509.1}.
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DR EMBL; ACCJ01000017; EEG57509.1; -; Genomic_DNA.
DR RefSeq; WP_007705746.1; NZ_GG657587.1.
DR AlphaFoldDB; C0CTL4; -.
DR HOGENOM; CLU_045011_8_3_9; -.
DR Proteomes; UP000004756; Unassembled WGS sequence.
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; 1.10.150.520; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR023214; HAD_sf.
DR NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR PANTHER; PTHR46470; N-ACYLNEURAMINATE-9-PHOSPHATASE; 1.
DR PANTHER; PTHR46470:SF2; N-ACYLNEURAMINATE-9-PHOSPHATASE; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:EEG57509.1}.
SQ SEQUENCE 264 AA; 27934 MW; 5F5D7FF388C9D57F CRC64;
MIKTIIFDID NTMYSFRTGN QAGMAALCAY AEEQFGITEG EFLDTFKKGK KLAEDRVGAD
TAAIHNRLIR MQVILELMGK PLFPHALNLY HCYWDALLAS ARPEPGLLEA MEALKAAGLT
LGVGTDMTAY IQYKKLERLG AAPYIDFITT SEEVGAEKPN PRLFLECVRK AGVPAGECLF
IGDSLAKDVR GAMDAGLQAF LYAPGSAREG TGGETALTAG ALALAPAVAA GALAPAPAVP
SGVTALTSFY DLPGLVRDMN AANP
//
