ID   PCD_PSEOX               Reviewed;         493 AA.
AC   Q01470;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Phenmedipham hydrolase;
DE            EC=3.1.1.-;
DE   AltName: Full=Phenylcarbamate hydrolase;
GN   Name=pcd;
OS   Pseudarthrobacter oxydans (Arthrobacter oxydans).
OG   Plasmid pHP52.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Pseudarthrobacter.
OX   NCBI_TaxID=1671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 264-270; 272-281
RP   AND 410-427.
RC   STRAIN=P52;
RX   PubMed=1400211; DOI=10.1128/jb.174.20.6600-6607.1992;
RA   Pohlenz H.-D., Boidol W., Schuettke I., Streber W.R.;
RT   "Purification and properties of an Arthrobacter oxydans P52 carbamate
RT   hydrolase specific for the herbicide phenmedipham and nucleotide sequence
RT   of the corresponding gene.";
RL   J. Bacteriol. 174:6600-6607(1992).
CC   -!- FUNCTION: May degrade the phenylcarbamate herbicides phenmedipham and
CC       desmedipham cometabolically by hydrolyzing their central carbamate
CC       linkages. Conveys resistance to the herbicide phenmedipham.
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; M94965; AAA22078.1; -; Genomic_DNA.
DR   PIR; A45737; A45737.
DR   AlphaFoldDB; Q01470; -.
DR   SMR; Q01470; -.
DR   ESTHER; artox-phhyd; Carb_B_Bacteria.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Herbicide resistance; Hydrolase; Plasmid;
KW   Serine esterase.
FT   CHAIN           1..493
FT                   /note="Phenmedipham hydrolase"
FT                   /id="PRO_0000070295"
FT   ACT_SITE        188
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        307
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        402
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   493 AA;  53728 MW;  83CECE7F3194BB6E CRC64;
     MITRPIAHTT AGDLGGCLED GLYVFRGVPY AEPPVGDLRW RAARPHAGWT GVRDASAYGP
     SAPQPVEPGG SPILGTHGDP PFDEDCLTLN LWTPNLDGGS RPVLVWIHGG GLLTGSGNLP
     NYATDTFARD GDLVGISINY RLGPLGFLAG MGDENVWLTD QVEALRWIAD NVAAFGGDPN
     RITLVGQSGG AYSIAALAQH PVARQLFHRA ILQSPPFGMQ PHTVEESTAR TKALARHLGH
     DDIEALRHEP WERLIQGTIG VLMEHTKFGE WPLAFYPVFD EATIPRHPIE SIIDSDIEII
     IGWTRDEGTF PFAFDPQVSQ ADRDQVESWL QKRFGDHAAS AYEAHAGDGT SPWTVIANVV
     GDELFHSAGY RVADERATRR PVRAYQFDVV SPLSDGALGA VHCIEMPFTF ANLDRWTGKP
     FVDGLDPDVV ARVTNVLHQA WIAFVRTGDP THDQLPVWPT FRADDPAVLV VGDEGAEVAR
     DLARPDHVSV RTL