ID   BHCR_PARDP              Reviewed;         279 AA.
AC   A1B8Z4;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=HTH-type transcriptional regulator BhcR {ECO:0000305|PubMed:31723261};
DE   AltName: Full=Bhc regulatory protein {ECO:0000305|PubMed:31723261};
GN   Name=bhcR {ECO:0000303|PubMed:31723261};
GN   OrderedLocusNames=Pden_3922 {ECO:0000312|EMBL:ABL71988.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 2 of Paracoccus denitrificans PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND DNA BINDING.
RC   STRAIN=ATCC 17741 / DSM 413 / NBRC 16712 / NCCB 22021 / NCIMB 11627;
RX   PubMed=31723261; DOI=10.1038/s41586-019-1748-4;
RA   Schada von Borzyskowski L., Severi F., Krueger K., Hermann L., Gilardet A.,
RA   Sippel F., Pommerenke B., Claus P., Cortina N.S., Glatter T., Zauner S.,
RA   Zarzycki J., Fuchs B.M., Bremer E., Maier U.G., Amann R.I., Erb T.J.;
RT   "Marine Proteobacteria metabolize glycolate via the beta-hydroxyaspartate
RT   cycle.";
RL   Nature 575:500-504(2019).
CC   -!- FUNCTION: Transcriptional regulator of the bhc gene cluster involved in
CC       glycolate and glyoxylate assimilation via the beta-hydroxyaspartate
CC       cycle (BHAC). Glyoxylate negatively affects the interaction of BhcR
CC       with the promoter region of the bhc gene cluster.
CC       {ECO:0000269|PubMed:31723261}.
CC   -!- MISCELLANEOUS: The beta-hydroxyaspartate cycle (BHAC) consists of BhcA,
CC       BhcB, BhcC, and BhcD enzyme activities. Overall, it converts two
CC       molecules of glyoxylate (C2) into oxaloacetate (C4) without the loss of
CC       carbon as CO2, under consumption of just one reducing equivalent and
CC       regeneration of the catalytic amino donor, which makes it one of the
CC       most efficient glyoxylate assimilation pathways. This cycle is of
CC       ecological importance in the assimilation of phytoplankton-derived
CC       dissolved organic carbon in marine environments by marine
CC       Proteobacteria, and suggests a trophic interaction between autotrophic
CC       phytoplankton and heterotrophic bacterioplankton. Oxaloacetate formed
CC       in the BHAC can directly enter the tricarboxylic acid cycle or serve as
CC       substrate for anabolic reactions. {ECO:0000305|PubMed:31723261}.
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DR   EMBL; CP000490; ABL71988.1; -; Genomic_DNA.
DR   RefSeq; WP_011750155.1; NC_008687.1.
DR   AlphaFoldDB; A1B8Z4; -.
DR   SMR; A1B8Z4; -.
DR   STRING; 318586.Pden_3922; -.
DR   PRIDE; A1B8Z4; -.
DR   EnsemblBacteria; ABL71988; ABL71988; Pden_3922.
DR   KEGG; pde:Pden_3922; -.
DR   eggNOG; COG1414; Bacteria.
DR   HOGENOM; CLU_062618_5_5_5; -.
DR   OMA; DTTETIH; -.
DR   Proteomes; UP000000361; Chromosome 2.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR014757; Tscrpt_reg_IclR_C.
DR   InterPro; IPR005471; Tscrpt_reg_IclR_N.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF09339; HTH_IclR; 1.
DR   Pfam; PF01614; IclR; 1.
DR   SMART; SM00346; HTH_ICLR; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS51077; HTH_ICLR; 1.
DR   PROSITE; PS51078; ICLR_ED; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..279
FT                   /note="HTH-type transcriptional regulator BhcR"
FT                   /id="PRO_0000449104"
FT   DOMAIN          26..87
FT                   /note="HTH iclR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00393"
FT   DOMAIN          102..271
FT                   /note="IclR-ED"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00394"
FT   DNA_BIND        47..66
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00393"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   279 AA;  30012 MW;  2ABCDDAEDC7AAEE8 CRC64;
     MSVQIRKRGR PRGRAGGLGA EDSGGIRALD RALDILDLIA VSSGLTLTEI AQRLDMAPST
     VHRVLVTLAA RGVAESDSQT QAWHVGPTAF RHGSAFMRRS GLVERARPLL RRLMEVTGET
     ANLGILNGDA VLFLSQAETH ETIRAFFPPG TRSALHASGI GKALLAHARP LDLKRMLREM
     RLERFTDMTL TDPAALVEDL VQIRARGYAL DNEERTPGMR CIAAPIFDLA GEAAAGISVS
     GPTLRMSDAR LSAMSDAVIE AARELSFGMA PRKDAGERA