BHCB_PARDP
ID BHCB_PARDP Reviewed; 315 AA.
AC A1B8Z2;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=beta-hydroxyaspartate dehydratase {ECO:0000303|PubMed:31723261};
DE EC=4.2.1.- {ECO:0000269|PubMed:31723261};
GN Name=bhcB {ECO:0000303|PubMed:31723261};
GN OrderedLocusNames=Pden_3920 {ECO:0000312|EMBL:ABL71986.1};
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, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, AND INDUCTION.
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: Catalyzes the dehydration of (2R,3S)-beta-hydroxyaspartate
CC ((3S)-3-hydroxy-D-aspartate) into iminosuccinate. Is essential for the
CC growth of P.denitrificans in the presence of glycolate and glyoxylate
CC since it functions in glyoxylate assimilation via the beta-
CC hydroxyaspartate cycle (BHAC). {ECO:0000269|PubMed:31723261}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3-hydroxy-D-aspartate = H2O + iminosuccinate;
CC Xref=Rhea:RHEA:62112, ChEBI:CHEBI:15377, ChEBI:CHEBI:60894,
CC ChEBI:CHEBI:77875; Evidence={ECO:0000269|PubMed:31723261};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62113;
CC Evidence={ECO:0000269|PubMed:31723261};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000305|PubMed:31723261};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.20 mM for (3S)-3-hydroxy-D-aspartate
CC {ECO:0000269|PubMed:31723261};
CC Note=kcat is 35 sec(-1). {ECO:0000269|PubMed:31723261};
CC -!- INDUCTION: Induced by glycolate. {ECO:0000269|PubMed:31723261}.
CC -!- DISRUPTION PHENOTYPE: Abolishes growth on glycolate or glyoxylate, but
CC the deletion mutant strain is still able to grow on acetate, succinate
CC or glucose with comparable growth rates as for the wild type.
CC {ECO:0000269|PubMed:31723261}.
CC -!- MISCELLANEOUS: Iminosuccinate is a labile compound that spontaneously
CC decays into free ammonia and oxaloacetate in solution.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000490; ABL71986.1; -; Genomic_DNA.
DR AlphaFoldDB; A1B8Z2; -.
DR SMR; A1B8Z2; -.
DR STRING; 318586.Pden_3920; -.
DR PRIDE; A1B8Z2; -.
DR EnsemblBacteria; ABL71986; ABL71986; Pden_3920.
DR KEGG; pde:Pden_3920; -.
DR eggNOG; COG1171; Bacteria.
DR HOGENOM; CLU_021152_4_2_5; -.
DR OMA; QTQHLGQ; -.
DR Proteomes; UP000000361; Chromosome 2.
DR GO; GO:0016836; F:hydro-lyase activity; IDA:UniProtKB.
DR GO; GO:0046296; P:glycolate catabolic process; IMP:UniProtKB.
DR GO; GO:0009436; P:glyoxylate catabolic process; IMP:UniProtKB.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
PE 1: Evidence at protein level;
KW Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..315
FT /note="beta-hydroxyaspartate dehydratase"
FT /id="PRO_0000449103"
FT BINDING 80
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P04968"
FT BINDING 179..183
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P04968"
FT BINDING 303
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P04968"
FT MOD_RES 53
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P04968"
SQ SEQUENCE 315 AA; 34015 MW; 4ABB7042E239EC66 CRC64;
MYIPTYEDML AAHERIKPHI RRTPIRTSDY LNELTGAQLF FKCENFQEPG AFKVRGATNA
VFGLDDAQAA KGVATHSSGN HASCLSYAAM LRGIPCNVVM PRTAPQAKKD TVRRYGGVIT
ECEPSTSSRE ETFAKVQAET GGDFVHPYND PRVIAGQGTC AKELVEQVDG LDAVVAPIGG
GGMISGTCLT LSTLAPETRV IAAEPEQADD AYRSFKAGYI IADDAPKTVA DGLLVPLKDL
TWHFVKNHVS EIYTASDAEI VDAMKLIWKH LRIVMEPSSA VPLATILKNP EAFAGKRVGV
IVTGGNVDLD KLPWN
