BHCA_PARDP
ID BHCA_PARDP Reviewed; 396 AA.
AC A1B8Z3;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=L-aspartate--glyoxylate aminotransferase {ECO:0000303|PubMed:31723261};
DE EC=2.6.1.35 {ECO:0000269|PubMed:31723261};
GN Name=bhcA {ECO:0000303|PubMed:31723261};
GN OrderedLocusNames=Pden_3921 {ECO:0000312|EMBL:ABL71987.1};
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 transamination of glyoxylate into glycine using
CC L-aspartate as the preferred amino group donor. 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). Can catalyze the reverse reaction in
CC vitro, and also use L-serine and L-glutamate as amino group donor, but
CC with much less efficiency than L-aspartate.
CC {ECO:0000269|PubMed:31723261}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + oxaloacetate = glyoxylate + L-aspartate;
CC Xref=Rhea:RHEA:17141, ChEBI:CHEBI:16452, ChEBI:CHEBI:29991,
CC ChEBI:CHEBI:36655, ChEBI:CHEBI:57305; EC=2.6.1.35;
CC Evidence={ECO:0000269|PubMed:31723261};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17143;
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=0.43 mM for glyoxylate {ECO:0000269|PubMed:31723261};
CC KM=2.51 mM for L-aspartate {ECO:0000269|PubMed:31723261};
CC KM=9.52 mM for glycine {ECO:0000269|PubMed:31723261};
CC KM=2.90 mM for oxaloacetate {ECO:0000269|PubMed:31723261};
CC KM=2.10 mM for L-serine {ECO:0000269|PubMed:31723261};
CC KM=20.62 mM for L-glutamate {ECO:0000269|PubMed:31723261};
CC Note=kcat is 58 sec(-1) for the transamination of glyoxylate using L-
CC aspartate. kcat is 0.76 sec(-1) for the transamination of glycine
CC using oxaloacetate. kcat is 8.8 sec(-1) for the transamination of
CC glyoxylate using L-serine. kcat is 5.0 sec(-1) for the transamination
CC of glyoxylate using L-glutamate. {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: 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 -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; CP000490; ABL71987.1; -; Genomic_DNA.
DR RefSeq; WP_011750154.1; NC_008687.1.
DR AlphaFoldDB; A1B8Z3; -.
DR SMR; A1B8Z3; -.
DR STRING; 318586.Pden_3921; -.
DR PRIDE; A1B8Z3; -.
DR EnsemblBacteria; ABL71987; ABL71987; Pden_3921.
DR KEGG; pde:Pden_3921; -.
DR eggNOG; COG0075; Bacteria.
DR HOGENOM; CLU_027686_1_0_5; -.
DR OMA; IRINHMG; -.
DR Proteomes; UP000000361; Chromosome 2.
DR GO; GO:0047303; F:glycine-oxaloacetate transaminase 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; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..396
FT /note="L-aspartate--glyoxylate aminotransferase"
FT /id="PRO_0000449102"
FT MOD_RES 196
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q988B8"
SQ SEQUENCE 396 AA; 42507 MW; 5C7CF0E1AB980EFF CRC64;
MTSQNPIFIP GPTNIPEEMR KAVDMPTIDH RSPVFGRMLH PALEGVKKVL KTTQAQVFLF
PSTGTGGWET AITNTLSPGD KVLAARNGMF SHRWIDMCQR HGLDVTFVET PWGEGVPADR
FEEILTADKG HEIRVVLATH NETATGVKSD IAAVRRALDA AKHPALLFVD GVSSIGSMDF
RMDEWGVDIA VTGSQKGFML PPGLAIVGFS PKAMEAVETA RLPRTFFDIR DMATGYARNG
YPYTPPVGLI NGLNASCERI LAEGLENVFA RHHRIASGVR AAVDAWGLKL CAVRPELYSD
SVSAIRVPEG FDANLIVSHA LETYDMAFGT GLGQVAGKVF RIGHLGSLTD AMALSGIATA
EMVMADLGLP IQLGSGVAAA QEHYRQTTAA AQKKAA
