ASDP_PSESP
ID ASDP_PSESP Reviewed; 531 AA.
AC Q53IZ1;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Bifunctional aspartate aminotransferase and L-aspartate beta-decarboxylase;
DE EC=2.6.1.1 {ECO:0000269|PubMed:16847601};
DE EC=4.1.1.12 {ECO:0000269|PubMed:16847601, ECO:0000269|PubMed:19368885};
DE AltName: Full=Aspartate 4-decarboxylase;
DE Short=Asd;
DE Short=AsdP;
GN Name=asD {ECO:0000303|PubMed:16847601};
OS Pseudomonas sp.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=306;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, FUNCTION, SUBUNIT,
RP ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 19121 / 618;
RX PubMed=16847601; DOI=10.1007/s00253-006-0475-6;
RA Wang N.C., Lee C.Y.;
RT "Molecular cloning of the aspartate 4-decarboxylase gene from Pseudomonas
RT sp. ATCC 19121 and characterization of the bifunctional recombinant
RT enzyme.";
RL Appl. Microbiol. Biotechnol. 73:339-348(2006).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) IN COMPLEX WITH PLP, CATALYTIC
RP ACTIVITY, FUNCTION, COFACTOR, SUBUNIT, AND MUTAGENESIS OF 67-SER--MET-69.
RC STRAIN=ATCC 19121 / 618;
RX PubMed=19368885; DOI=10.1016/j.str.2009.02.013;
RA Chen H.J., Ko T.P., Lee C.Y., Wang N.C., Wang A.H.;
RT "Structure, assembly, and mechanism of a PLP-dependent dodecameric L-
RT aspartate beta-decarboxylase.";
RL Structure 17:517-529(2009).
CC -!- FUNCTION: Bifunctional enzyme that has both L-aspartate decarboxylase
CC and transaminase activity. Has high activity with L-aspartate, and much
CC lower activity with D-aspartate, L-lysine and L-glutamine.
CC {ECO:0000269|PubMed:16847601, ECO:0000269|PubMed:19368885}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-aspartate = CO2 + L-alanine; Xref=Rhea:RHEA:12621,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29991,
CC ChEBI:CHEBI:57972; EC=4.1.1.12;
CC Evidence={ECO:0000269|PubMed:16847601, ECO:0000269|PubMed:19368885};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC Evidence={ECO:0000269|PubMed:16847601};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:19368885};
CC -!- ACTIVITY REGULATION: Inhibited by 10 mM Co(2+), Mn(2+) and Ni(2+), and
CC by 1 mM Cu(2+) and Hg(2+). {ECO:0000269|PubMed:16847601}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11 mM for L-aspartate {ECO:0000269|PubMed:16847601};
CC pH dependence:
CC Optimum pH is 5. {ECO:0000269|PubMed:16847601};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:16847601};
CC -!- SUBUNIT: Homododecamer. {ECO:0000269|PubMed:16847601,
CC ECO:0000269|PubMed:19368885}.
CC -!- INTERACTION:
CC Q53IZ1; Q53IZ1: asD; NbExp=2; IntAct=EBI-15769000, EBI-15769000;
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AF506011; AAQ07948.1; -; Genomic_DNA.
DR PDB; 2ZY2; X-ray; 3.30 A; A=1-531.
DR PDBsum; 2ZY2; -.
DR AlphaFoldDB; Q53IZ1; -.
DR SMR; Q53IZ1; -.
DR DIP; DIP-48315N; -.
DR BRENDA; 4.1.1.12; 5085.
DR EvolutionaryTrace; Q53IZ1; -.
DR GO; GO:0047688; F:aspartate 4-decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006523; P:alanine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006531; P:aspartate metabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR022518; Aspartate_4-decarboxylase.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR03801; asp_4_decarbox; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aminotransferase; Decarboxylase;
KW Lyase; Pyridoxal phosphate; Transferase.
FT CHAIN 1..531
FT /note="Bifunctional aspartate aminotransferase and L-
FT aspartate beta-decarboxylase"
FT /id="PRO_0000419124"
FT BINDING 114
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 496
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT MOD_RES 314
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:19368885,
FT ECO:0007744|PDB:2ZY2"
FT MUTAGEN 67..69
FT /note="SYM->EEE: Loss of activity. Dissociation into
FT dimers."
FT /evidence="ECO:0000269|PubMed:19368885"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 16..21
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 28..35
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 46..63
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:2ZY2"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 97..111
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:2ZY2"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 141..154
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:2ZY2"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 172..187
FT /evidence="ECO:0007829|PDB:2ZY2"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:2ZY2"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:2ZY2"
FT STRAND 245..253
FT /evidence="ECO:0007829|PDB:2ZY2"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 263..275
FT /evidence="ECO:0007829|PDB:2ZY2"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:2ZY2"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:2ZY2"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:2ZY2"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:2ZY2"
FT TURN 312..316
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:2ZY2"
FT STRAND 324..331
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 333..337
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 343..352
FT /evidence="ECO:0007829|PDB:2ZY2"
FT TURN 353..356
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 365..373
FT /evidence="ECO:0007829|PDB:2ZY2"
FT TURN 374..378
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 386..400
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 406..423
FT /evidence="ECO:0007829|PDB:2ZY2"
FT TURN 424..427
FT /evidence="ECO:0007829|PDB:2ZY2"
FT STRAND 439..444
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 445..452
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 455..464
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 467..477
FT /evidence="ECO:0007829|PDB:2ZY2"
FT STRAND 494..498
FT /evidence="ECO:0007829|PDB:2ZY2"
FT HELIX 504..527
FT /evidence="ECO:0007829|PDB:2ZY2"
FT TURN 528..531
FT /evidence="ECO:0007829|PDB:2ZY2"
SQ SEQUENCE 531 AA; 59246 MW; C2EE19A83CC7B00D CRC64;
MSKDYRSLAN LSPFELKDEL IKVASGKANR LMLNAGRGNP NFLATTPRRA FFRLGLFAAA
ESELSYSYMT VGVGGLAKLD GIEGRFERFI AEHRDQEGVK FLGKSLSYVR DQLGLDPAAF
LHEMVDGILG CNYPVPPRML TVSEQIVRQY IVREMAGGAV PPESVDLFAV EGGTAAMAYI
FESLRISGLL KAGDKVAIGM PVFTPYIEIP ELAQYDLKEV PIHADPDNGW QYSDAELDKL
KDPDVKIFFC VNPSNPPSVK MDQRSLDRVR AIVAEQRPDL LILTDDVYGT FADEFQSLFS
VCPRNTLLVY SFSKYFGATG WRLGVIAAHK DNVFDHALSQ LPESAKKALD HRYRSLLPDV
RSLKFIDRLV ADSRVVALNH TAGLSTPQQV QMVLFSLFAL MDEADAYKQA LKQLIRRREA
TLYRELGMPP LENPNSVNYY TLIDLQNVTC RLYGEAFSQW AVQQSSTGDM LFRVADETGI
VLLPGRGFGS DRPSGRASLA NLNEYEYAAI GRALRRLADE LYEQYKALGK E
