ID A0A379CE03_9PAST Unreviewed; 459 AA.
AC A0A379CE03;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 9.
DE SubName: Full=Atrazine chlorohydrolase {ECO:0000313|EMBL:SUB59935.1};
DE EC=3.8.1.8 {ECO:0000313|EMBL:SUB59935.1};
GN Name=atzA {ECO:0000313|EMBL:SUB59935.1};
GN ORFNames=NCTC12872_01994 {ECO:0000313|EMBL:SUB59935.1};
OS Phocoenobacter uteri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Phocoenobacter.
OX NCBI_TaxID=146806 {ECO:0000313|EMBL:SUB59935.1, ECO:0000313|Proteomes:UP000255417};
RN [1] {ECO:0000313|EMBL:SUB59935.1, ECO:0000313|Proteomes:UP000255417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12872 {ECO:0000313|EMBL:SUB59935.1,
RC ECO:0000313|Proteomes:UP000255417};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ATZ/TRZ family. {ECO:0000256|ARBA:ARBA00006745}.
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DR EMBL; UGTA01000001; SUB59935.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A379CE03; -.
DR OrthoDB; 9807210at2; -.
DR Proteomes; UP000255417; Unassembled WGS sequence.
DR GO; GO:0018788; F:atrazine chlorohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01298; ATZ_TRZ_like; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43794:SF11; AMIDOHYDRO-REL DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43794; AMINOHYDROLASE SSNA-RELATED; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:SUB59935.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000255417};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..459
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016829558"
FT DOMAIN 80..428
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 459 AA; 50648 MW; 4A82830F8672A93D CRC64;
MKKLLALSSV LALSLFNYTN ASENVDLIVK NGMILTMNQA KEIIDDGVVI VNKNQIIDVG
DKNLLQKYSA KKVIDAEEGI VMPGMINTHS HISMSVFRSL ADDVPNRLQR YIFPLENKMV
SKEMVYTGAV HGAIELAKGG VTTVVDMYLF EDSAAKAVKE VGLRGVMTQN IIKYPTADGK
DGAENIEMAI AFVEKYKNDE LITAGFGPHA PHTVKKADLE RIRDLSQKYN APVSMHVAET
QKEFDKFKAE YNMTPIEYLD SVGLLNERFI AAHCIFVTES DIALMKKRNI GVAHNMVANI
KSAKGVSPAL KMFDEGLNIG LGSDGPMSGN TLDIIGQIGY VAKLHKLMNK DRSVMPPQKV
VEMATMGGAR AIHREKDLGS LEKGKLADIV ILETKSTNMQ PNFDPYSVLV YSANASNVST
TIVNGKIIME KRKLRYNEEK SNKAIKEFSK KVKEIAKTL
//