ASDA_COMTE
ID ASDA_COMTE Reviewed; 533 AA.
AC Q93QX0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Bifunctional aspartate aminotransferase and L-aspartate beta-decarboxylase;
DE EC=2.6.1.1 {ECO:0000250|UniProtKB:Q53IZ1};
DE EC=4.1.1.12 {ECO:0000269|PubMed:19368885, ECO:0000269|Ref.1};
DE AltName: Full=Aspartate 4-decarboxylase;
DE Short=ASD;
DE Short=AsdA;
GN Name=asD {ECO:0000303|Ref.1};
OS Comamonas testosteroni (Pseudomonas testosteroni).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=285;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 25094 / DSM 30032 / N;
RX DOI=10.1038/sj.jim.7000043;
RA Chen C.-C., Chou T.-L., Lee C.-Y.;
RT "Cloning, expression and characterization of L-aspartate - decarboxylase
RT gene from Alcaligenes faecalis CCRC 11585.";
RL J. Ind. Microbiol. Biotechnol. 25:132-140(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH PLP, CATALYTIC
RP ACTIVITY, FUNCTION, SUBUNIT, COFACTOR, AND MUTAGENESIS OF TYR-134; LYS-315
RP AND ARG-487.
RC STRAIN=ATCC 25094 / DSM 30032 / N;
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. {ECO:0000269|PubMed:19368885,
CC ECO:0000269|Ref.1}.
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:19368885, ECO:0000269|Ref.1};
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:0000250|UniProtKB:Q53IZ1};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:19368885};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9 mM for L-aspartate {ECO:0000269|Ref.1};
CC pH dependence:
CC Optimum pH is 5. {ECO:0000269|Ref.1};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius. {ECO:0000269|Ref.1};
CC -!- SUBUNIT: Homododecamer. {ECO:0000269|PubMed:19368885}.
CC -!- INTERACTION:
CC Q93QX0; Q93QX0: asD; NbExp=3; IntAct=EBI-15768961, EBI-15768961;
CC -!- BIOTECHNOLOGY: Is highly specific for L-aspartic acid, and so can be
CC used to produce L-alanine and D-aspartic acid from DL-aspartic acid.
CC {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AF168368; AAK58507.1; -; Genomic_DNA.
DR RefSeq; WP_003054930.1; NZ_CP006704.1.
DR PDB; 2ZY3; X-ray; 2.50 A; A/B/C/D/E/F=1-533.
DR PDB; 2ZY4; X-ray; 2.00 A; A/B/C/D/E/F=1-533.
DR PDB; 2ZY5; X-ray; 2.65 A; A/B/C/D/E/F=1-533.
DR PDBsum; 2ZY3; -.
DR PDBsum; 2ZY4; -.
DR PDBsum; 2ZY5; -.
DR AlphaFoldDB; Q93QX0; -.
DR SMR; Q93QX0; -.
DR DIP; DIP-48316N; -.
DR BRENDA; 4.1.1.12; 1590.
DR EvolutionaryTrace; Q93QX0; -.
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..533
FT /note="Bifunctional aspartate aminotransferase and L-
FT aspartate beta-decarboxylase"
FT /id="PRO_0000419123"
FT BINDING 115
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 497
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT MOD_RES 315
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:19368885,
FT ECO:0007744|PDB:2ZY3, ECO:0007744|PDB:2ZY4,
FT ECO:0007744|PDB:2ZY5"
FT MUTAGEN 134
FT /note="Y->F: Slightly reduced activity."
FT /evidence="ECO:0000269|PubMed:19368885"
FT MUTAGEN 315
FT /note="K->A: Slightly reduced activity."
FT /evidence="ECO:0000269|PubMed:19368885"
FT MUTAGEN 487
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19368885"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 27..35
FT /evidence="ECO:0007829|PDB:2ZY4"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 46..63
FT /evidence="ECO:0007829|PDB:2ZY4"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:2ZY4"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 98..112
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 118..130
FT /evidence="ECO:0007829|PDB:2ZY4"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 142..155
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:2ZY4"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 173..187
FT /evidence="ECO:0007829|PDB:2ZY4"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 205..212
FT /evidence="ECO:0007829|PDB:2ZY4"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:2ZY3"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:2ZY4"
FT STRAND 246..254
FT /evidence="ECO:0007829|PDB:2ZY4"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 264..276
FT /evidence="ECO:0007829|PDB:2ZY4"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:2ZY4"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:2ZY3"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:2ZY4"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:2ZY4"
FT TURN 314..318
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:2ZY4"
FT STRAND 324..332
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 334..340
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 344..354
FT /evidence="ECO:0007829|PDB:2ZY4"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 366..373
FT /evidence="ECO:0007829|PDB:2ZY4"
FT TURN 374..379
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 387..402
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 407..424
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:2ZY4"
FT STRAND 440..445
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 446..454
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 456..465
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 468..479
FT /evidence="ECO:0007829|PDB:2ZY4"
FT STRAND 484..487
FT /evidence="ECO:0007829|PDB:2ZY4"
FT STRAND 495..503
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 505..525
FT /evidence="ECO:0007829|PDB:2ZY4"
FT HELIX 529..533
FT /evidence="ECO:0007829|PDB:2ZY4"
SQ SEQUENCE 533 AA; 59584 MW; B6E0042383A51113 CRC64;
MSKDYQSLAK LSPFELKDEL IKIASSDGNR LMLNAGRGNP NFLATTPRRA FFRLGLFAAA
ESELSYSYMT TVGVGGLAKI DGIEGRFERY IAENRDQEGV RFLGKSLSYV RDQLGLDPAA
FLHEMVDGIL GCNYPVPPRM LNISEKIVRQ YIIREMGADA IPSESVNLFA VEGGTAAMAY
IFESLKLNGL LKAGDKVAIG MPVFTPYIEI PELAQYALEE VAINADPSLN WQYPDSELDK
LKDPAIKIFF CVNPSNPPSV KMDQRSLERV RNIVAEHRPD LMILTDDVYG TFADDFQSLF
AICPENTLLV YSFSKYFGAT GWRLGVVAAH QQNVFDLALD KLQESEKVAL DHRYRSLLPD
VRSLKFIDRL VADSRAVALN HTAGLSTPQQ VQMALFSLFA LMDEADEYKH TLKQLIRRRE
TTLYRELGMP PLRDENAVDY YTLIDLQDVT AKLYGEAFSE WAVKQSSTGD MLFRIADETG
IVLLPGRGFG SNRPSGRASL ANLNEYEYAA IGRALRKMAD ELYAEYSGQA QNL
