BSDC_CHLPN
ID BSDC_CHLPN Reviewed; 584 AA.
AC Q9Z8L0; Q9JQJ5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=4-hydroxybenzoate decarboxylase subunit C;
DE Short=4-hydroxybenzoate DC;
DE Short=HBDC;
DE EC=4.1.1.61;
GN OrderedLocusNames=CPn_0328, CP_0429, CPj0328, CpB0338;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=17211544; DOI=10.1007/s00284-006-0153-z;
RA Liu J., Zhang X., Zhou S., Tao P., Liu J.;
RT "Purification and characterization of a 4-hydroxybenzoate decarboxylase
RT from Chlamydophila pneumoniae AR39.";
RL Curr. Microbiol. 54:102-107(2007).
CC -!- FUNCTION: Catalyzes the reversible decarboxylation of 4-
CC hydroxybenzoate. {ECO:0000269|PubMed:17211544}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoate + H(+) = CO2 + phenol; Xref=Rhea:RHEA:10876,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15882, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17879; EC=4.1.1.61;
CC Evidence={ECO:0000269|PubMed:17211544};
CC -!- ACTIVITY REGULATION: The enzyme activity is enhanced by Mg(2+), Fe(2+),
CC Mn(2+) and Ca(2+). No stimulation is observed with Cu(2+) and Zn(2+).
CC {ECO:0000269|PubMed:17211544}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.21 mM for 4-hydroxybenzoate (at pH 7.5 and at 30 degrees
CC Celsius) {ECO:0000269|PubMed:17211544};
CC Vmax=11.9 nmol/min/mg enzyme (at pH 7.5 and at 30 degrees Celsius)
CC {ECO:0000269|PubMed:17211544};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:17211544};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius. It loses above 50%
CC decarboxylase activity at 40 degrees Celsius for 5 minutes, and above
CC 25% enzyme activity remains after incubation at 50 degrees Celsius
CC for 5 minutes. {ECO:0000269|PubMed:17211544};
CC -!- SUBUNIT: Component of the decarboxylase complex composed of the
CC subunits B and C (Potential). The subunit D usually found in other
CC organisms seems to be absent. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the UbiD family. {ECO:0000305}.
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DR EMBL; AE001363; AAD18477.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38271.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98538.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98271.1; -; Genomic_DNA.
DR PIR; A72092; A72092.
DR PIR; H86531; H86531.
DR RefSeq; NP_224533.1; NC_000922.1.
DR RefSeq; WP_010882976.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z8L0; -.
DR SMR; Q9Z8L0; -.
DR STRING; 115711.CP_0429; -.
DR EnsemblBacteria; AAD18477; AAD18477; CPn_0328.
DR EnsemblBacteria; AAF38271; AAF38271; CP_0429.
DR GeneID; 45050377; -.
DR KEGG; cpa:CP_0429; -.
DR KEGG; cpj:CPj0328; -.
DR KEGG; cpn:CPn_0328; -.
DR KEGG; cpt:CpB0338; -.
DR PATRIC; fig|115713.3.peg.364; -.
DR eggNOG; COG0043; Bacteria.
DR HOGENOM; CLU_023348_4_1_0; -.
DR OrthoDB; 1012819at2; -.
DR SABIO-RK; Q9Z8L0; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; Chromosome.
DR GO; GO:0018799; F:4-hydroxybenzoate decarboxylase activity; IEA:UniProtKB-EC.
DR InterPro; IPR022390; HBDC.
DR InterPro; IPR002830; UbiD.
DR PANTHER; PTHR30108; PTHR30108; 1.
DR Pfam; PF01977; UbiD; 1.
DR TIGRFAMs; TIGR03701; mena_SCO4490; 1.
DR TIGRFAMs; TIGR00148; TIGR00148; 1.
PE 1: Evidence at protein level;
KW Decarboxylase; Lyase.
FT CHAIN 1..584
FT /note="4-hydroxybenzoate decarboxylase subunit C"
FT /id="PRO_0000157372"
SQ SEQUENCE 584 AA; 66507 MW; 87F394EEE47748F5 CRC64;
MSFLRRHISL FRSQKQLIDV FAPVSPNLEL AEIHRRVIED QGPALLFHNV IGSSFPVLTN
LFGTKHRVDQ LFSQAPDNLI ARVAHLISST PKLSSLWKSR DLLKRISSLG LKKARFRRFP
FVSMSSVNLD HLPLLTSWPE DGGAFLTLPL VYTESPTLTT PNLGMYRVQR FNQNTMGLHF
QIQKGGGMHL YEAEQKKQNL PVSVFLSGNP FLTLSAIAPL PENVSELLFA TFLQGAKLLY
KKTNDHPHPL LYDAEFILVG ESPAGKRRPE GPFGDHFGYY SLQHDFPEFH CHKIYHRKDA
IYPATVVGKP YQEDFYIGNK LQEYLSPLFP LVMPGVRRLK SYGESGFHAL TAAVVKERYW
RESLTTALRI LGEGQLSLTK FLMVTDQEVP LDRFSVVLET ILERLQPDRD LIIFSETAND
TLDYTGPSLN KGSKGIFMGI GKAIRDLPHG YQGGKIHGVQ DIAPFCRGCL VLETSLEDRC
IKSLLHHPDL KSWPLIILAD NLRETIQSEK DFLWRTFTRC APANDLHALH SHFATHRPNY
NFPFVIDALM KPSYPKEVEV DPSTKQKVSE RWHAYFPNKE TFYI
