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Bifunctional aspartate aminotransferase and L-aspartate beta-decarboxylase (EC 2.6.1.1) (EC 4.1.1.12) (Aspartate 4-decarboxylase) (Asd) (AsdP)

 ASDP_PSESP              Reviewed;         531 AA.
Q53IZ1;
05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
24-MAY-2005, sequence version 1.
23-MAY-2018, entry version 57.
RecName: Full=Bifunctional aspartate aminotransferase and L-aspartate beta-decarboxylase;
EC=2.6.1.1;
EC=4.1.1.12;
AltName: Full=Aspartate 4-decarboxylase;
Short=Asd;
Short=AsdP;
Name=asD;
Pseudomonas sp.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=306;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, FUNCTION,
SUBUNIT, ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=ATCC 19121 / 618;
PubMed=16847601; DOI=10.1007/s00253-006-0475-6;
Wang N.C., Lee C.Y.;
"Molecular cloning of the aspartate 4-decarboxylase gene from
Pseudomonas sp. ATCC 19121 and characterization of the bifunctional
recombinant enzyme.";
Appl. Microbiol. Biotechnol. 73:339-348(2006).
[2]
X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS), CATALYTIC ACTIVITY, FUNCTION,
COFACTOR, SUBUNIT, AND MUTAGENESIS OF 67-SER--MET-69.
STRAIN=ATCC 19121 / 618;
PubMed=19368885; DOI=10.1016/j.str.2009.02.013;
Chen H.J., Ko T.P., Lee C.Y., Wang N.C., Wang A.H.;
"Structure, assembly, and mechanism of a PLP-dependent dodecameric L-
aspartate beta-decarboxylase.";
Structure 17:517-529(2009).
-!- FUNCTION: Bifunctional enzyme that has both L-aspartate
decarboxylase and transaminase activity. Has high activity with L-
aspartate, and much lower activity with D-aspartate, L-lysine and
L-glutamine. {ECO:0000269|PubMed:16847601,
ECO:0000269|PubMed:19368885}.
-!- CATALYTIC ACTIVITY: L-aspartate = L-alanine + CO(2).
-!- CATALYTIC ACTIVITY: L-aspartate + 2-oxoglutarate = oxaloacetate +
L-glutamate.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000269|PubMed:19368885};
-!- ENZYME REGULATION: Inhibited by 10 mM Co(2+), Mn(2+) and Ni(2+),
and by 1 mM Cu(2+) and Hg(2+). {ECO:0000269|PubMed:16847601}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=11 mM for L-aspartate {ECO:0000269|PubMed:16847601};
pH dependence:
Optimum pH is 5. {ECO:0000269|PubMed:16847601};
Temperature dependence:
Optimum temperature is 45 degrees Celsius.
{ECO:0000269|PubMed:16847601};
-!- SUBUNIT: Homododecamer. {ECO:0000269|PubMed:16847601,
ECO:0000269|PubMed:19368885}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-15769000, EBI-15769000;
-!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
aminotransferase family. {ECO:0000305}.
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EMBL; AF506011; AAQ07948.1; -; Genomic_DNA.
PDB; 2ZY2; X-ray; 3.30 A; A=1-531.
PDBsum; 2ZY2; -.
ProteinModelPortal; Q53IZ1; -.
SMR; Q53IZ1; -.
DIP; DIP-48315N; -.
PRIDE; Q53IZ1; -.
BRENDA; 4.1.1.12; 5085.
EvolutionaryTrace; Q53IZ1; -.
GO; GO:0047688; F:aspartate 4-decarboxylase activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0006523; P:alanine biosynthetic process; IDA:UniProtKB.
GO; GO:0006531; P:aspartate metabolic process; IDA:UniProtKB.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 2.
InterPro; IPR004839; Aminotransferase_I/II.
InterPro; IPR022518; Aspartate_4-decarboxylase.
InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
Pfam; PF00155; Aminotran_1_2; 1.
SUPFAM; SSF53383; SSF53383; 2.
TIGRFAMs; TIGR03801; asp_4_decarbox; 1.
PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
1: Evidence at protein level;
3D-structure; Amino-acid biosynthesis; Aminotransferase;
Decarboxylase; Lyase; Pyridoxal phosphate; Transferase.
CHAIN 1 531 Bifunctional aspartate aminotransferase
and L-aspartate beta-decarboxylase.
/FTId=PRO_0000419124.
BINDING 114 114 Aspartate; via amide nitrogen.
{ECO:0000250}.
BINDING 255 255 Aspartate. {ECO:0000250}.
BINDING 496 496 Aspartate. {ECO:0000250}.
MOD_RES 314 314 N6-(pyridoxal phosphate)lysine.
MUTAGEN 67 69 SYM->EEE: Loss of activity. Dissociation
into dimers.
{ECO:0000269|PubMed:19368885}.
TURN 13 15 {ECO:0000244|PDB:2ZY2}.
HELIX 16 21 {ECO:0000244|PDB:2ZY2}.
HELIX 28 35 {ECO:0000244|PDB:2ZY2}.
HELIX 46 63 {ECO:0000244|PDB:2ZY2}.
HELIX 82 91 {ECO:0000244|PDB:2ZY2}.
TURN 92 95 {ECO:0000244|PDB:2ZY2}.
HELIX 97 111 {ECO:0000244|PDB:2ZY2}.
HELIX 117 129 {ECO:0000244|PDB:2ZY2}.
STRAND 135 138 {ECO:0000244|PDB:2ZY2}.
HELIX 141 154 {ECO:0000244|PDB:2ZY2}.
HELIX 162 164 {ECO:0000244|PDB:2ZY2}.
STRAND 169 171 {ECO:0000244|PDB:2ZY2}.
HELIX 172 187 {ECO:0000244|PDB:2ZY2}.
STRAND 195 201 {ECO:0000244|PDB:2ZY2}.
HELIX 204 208 {ECO:0000244|PDB:2ZY2}.
TURN 213 215 {ECO:0000244|PDB:2ZY2}.
HELIX 226 228 {ECO:0000244|PDB:2ZY2}.
HELIX 234 237 {ECO:0000244|PDB:2ZY2}.
HELIX 238 241 {ECO:0000244|PDB:2ZY2}.
STRAND 245 253 {ECO:0000244|PDB:2ZY2}.
TURN 255 257 {ECO:0000244|PDB:2ZY2}.
HELIX 263 275 {ECO:0000244|PDB:2ZY2}.
STRAND 281 285 {ECO:0000244|PDB:2ZY2}.
HELIX 287 289 {ECO:0000244|PDB:2ZY2}.
STRAND 292 294 {ECO:0000244|PDB:2ZY2}.
HELIX 298 301 {ECO:0000244|PDB:2ZY2}.
TURN 303 305 {ECO:0000244|PDB:2ZY2}.
STRAND 306 311 {ECO:0000244|PDB:2ZY2}.
TURN 312 316 {ECO:0000244|PDB:2ZY2}.
HELIX 319 321 {ECO:0000244|PDB:2ZY2}.
STRAND 324 331 {ECO:0000244|PDB:2ZY2}.
HELIX 333 337 {ECO:0000244|PDB:2ZY2}.
HELIX 343 352 {ECO:0000244|PDB:2ZY2}.
TURN 353 356 {ECO:0000244|PDB:2ZY2}.
HELIX 365 373 {ECO:0000244|PDB:2ZY2}.
TURN 374 378 {ECO:0000244|PDB:2ZY2}.
HELIX 379 381 {ECO:0000244|PDB:2ZY2}.
HELIX 386 400 {ECO:0000244|PDB:2ZY2}.
HELIX 406 423 {ECO:0000244|PDB:2ZY2}.
TURN 424 427 {ECO:0000244|PDB:2ZY2}.
STRAND 439 444 {ECO:0000244|PDB:2ZY2}.
HELIX 445 452 {ECO:0000244|PDB:2ZY2}.
HELIX 455 464 {ECO:0000244|PDB:2ZY2}.
HELIX 467 477 {ECO:0000244|PDB:2ZY2}.
STRAND 494 498 {ECO:0000244|PDB:2ZY2}.
HELIX 504 527 {ECO:0000244|PDB:2ZY2}.
TURN 528 531 {ECO:0000244|PDB:2ZY2}.
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


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