ID A0A0C1TWZ4_9CLOT Unreviewed; 241 AA.
AC A0A0C1TWZ4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=HAD hydrolase, IA, variant 1 family protein {ECO:0000313|EMBL:KIE45209.1};
GN ORFNames=U732_727 {ECO:0000313|EMBL:KIE45209.1};
OS Clostridium argentinense CDC 2741.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1418104 {ECO:0000313|EMBL:KIE45209.1, ECO:0000313|Proteomes:UP000031366};
RN [1] {ECO:0000313|EMBL:KIE45209.1, ECO:0000313|Proteomes:UP000031366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 2741 {ECO:0000313|EMBL:KIE45209.1,
RC ECO:0000313|Proteomes:UP000031366};
RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA Karavis M.A., Smith L.A.;
RT "Genomic sequences of six botulinum neurotoxin-producing strains
RT representing three clostridial species illustrate the mobility and
RT diversity of botulinum neurotoxin genes.";
RL Infect. Genet. Evol. 30:102-113(2014).
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:KIE45209.1}.
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DR EMBL; AYSO01000020; KIE45209.1; -; Genomic_DNA.
DR RefSeq; WP_039636773.1; NZ_AYSO01000020.1.
DR AlphaFoldDB; A0A0C1TWZ4; -.
DR STRING; 29341.RSJ17_06435; -.
DR OrthoDB; 9802350at2; -.
DR Proteomes; UP000031366; 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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 1.20.120.710; Haloacid dehalogenase hydrolase-like domain; 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 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 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:KIE45209.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031366}.
SQ SEQUENCE 241 AA; 28706 MW; 134282295F695AA3 CRC64;
MFNNIKVIYF DMGNTLLHFH YGDSDKEKDM VGLYKLTQYL KKFHSKISFE EVKIGFYNKW
MNIMNLRKET LIEYPIEEFL NEFLKNYDVY LTINQCIEAI HIFYSEYKKQ LFFEKDLHKT
LNKIKAKGYK IGVISNTCYY DEVMIDCFKV SGLYDLIDNF TFSYSLKLCK PREEIFKKAL
EKMNVCGKEC LMVGDNLKCD IKPALDLDMK TIWLNKNQVK NPTEIKPNII ISNLHEINNY
I
//
