OAPT_PSEPU
ID OAPT_PSEPU Reviewed; 449 AA.
AC P28269;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Omega-amino acid--pyruvate aminotransferase;
DE Short=Omega-APT;
DE EC=2.6.1.18;
DE AltName: Full=Beta-alanine--pyruvate aminotransferase;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP PROTEIN SEQUENCE, AND SUBUNIT.
RC STRAIN=NBRC 14796 / NCIMB 13499 / F-126;
RX PubMed=1618757; DOI=10.1016/s0021-9258(18)42306-x;
RA Yonaha K., Nishie M., Aibara S.;
RT "The primary structure of omega-amino acid:pyruvate aminotransferase.";
RL J. Biol. Chem. 267:12506-12510(1992).
RN [2]
RP PROTEIN SEQUENCE OF 1-18 AND 285-292, FUNCTION, COFACTOR, AND SUBUNIT.
RC STRAIN=NBRC 14796 / NCIMB 13499 / F-126;
RX PubMed=6822556; DOI=10.1016/s0021-9258(18)32916-8;
RA Yonaha K., Toyama S., Kagamiyama H.;
RT "Properties of the bound coenzyme and subunit structure of omega-amino
RT acid:pyruvate aminotransferase.";
RL J. Biol. Chem. 258:2260-2265(1983).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP COFACTOR, AND SUBUNIT.
RX PubMed=2500426; DOI=10.1093/oxfordjournals.jbchem.a122600;
RA Watanabe N., Sakabe K., Sakabe N., Higashi T., Sasaki K., Aibara S.,
RA Morita Y., Yonaha K., Toyama S., Fukutani H.;
RT "Crystal structure analysis of omega-amino acid:pyruvate aminotransferase
RT with a newly developed Weissenberg camera and an imaging plate using
RT synchrotron radiation.";
RL J. Biochem. 105:1-3(1989).
CC -!- FUNCTION: Catalyzes transamination between a variety of omega-amino
CC acids, mono and diamines, and pyruvate. Plays a pivotal role in the
CC metabolism of the omega amino acids. {ECO:0000269|PubMed:6822556}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxopropanoate + L-alanine = beta-alanine + pyruvate;
CC Xref=Rhea:RHEA:14077, ChEBI:CHEBI:15361, ChEBI:CHEBI:33190,
CC ChEBI:CHEBI:57966, ChEBI:CHEBI:57972; EC=2.6.1.18;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:2500426, ECO:0000269|PubMed:6822556};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:1618757,
CC ECO:0000269|PubMed:2500426, ECO:0000269|PubMed:6822556}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR PIR; A42800; A42800.
DR PDB; 3A8U; X-ray; 1.40 A; X=1-449.
DR PDBsum; 3A8U; -.
DR AlphaFoldDB; P28269; -.
DR SMR; P28269; -.
DR EvolutionaryTrace; P28269; -.
DR GO; GO:0016223; F:beta-alanine-pyruvate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Direct protein sequencing;
KW Pyridoxal phosphate; Transferase.
FT CHAIN 1..449
FT /note="Omega-amino acid--pyruvate aminotransferase"
FT /id="PRO_0000120494"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 119..120
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 327
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 414
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 421
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 288
FT /note="N6-(pyridoxal phosphate)lysine"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:3A8U"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:3A8U"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:3A8U"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:3A8U"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:3A8U"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:3A8U"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:3A8U"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:3A8U"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:3A8U"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:3A8U"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:3A8U"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:3A8U"
FT HELIX 119..136
FT /evidence="ECO:0007829|PDB:3A8U"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:3A8U"
FT HELIX 157..162
FT /evidence="ECO:0007829|PDB:3A8U"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:3A8U"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:3A8U"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:3A8U"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:3A8U"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:3A8U"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:3A8U"
FT HELIX 201..215
FT /evidence="ECO:0007829|PDB:3A8U"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:3A8U"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:3A8U"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:3A8U"
FT TURN 230..233
FT /evidence="ECO:0007829|PDB:3A8U"
FT HELIX 241..252
FT /evidence="ECO:0007829|PDB:3A8U"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:3A8U"
FT TURN 261..268
FT /evidence="ECO:0007829|PDB:3A8U"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:3A8U"
FT HELIX 273..277
FT /evidence="ECO:0007829|PDB:3A8U"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:3A8U"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:3A8U"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:3A8U"
FT HELIX 304..311
FT /evidence="ECO:0007829|PDB:3A8U"
FT TURN 327..330
FT /evidence="ECO:0007829|PDB:3A8U"
FT HELIX 332..347
FT /evidence="ECO:0007829|PDB:3A8U"
FT HELIX 350..366
FT /evidence="ECO:0007829|PDB:3A8U"
FT TURN 367..370
FT /evidence="ECO:0007829|PDB:3A8U"
FT STRAND 374..380
FT /evidence="ECO:0007829|PDB:3A8U"
FT STRAND 383..388
FT /evidence="ECO:0007829|PDB:3A8U"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:3A8U"
FT HELIX 397..409
FT /evidence="ECO:0007829|PDB:3A8U"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:3A8U"
FT STRAND 419..422
FT /evidence="ECO:0007829|PDB:3A8U"
FT HELIX 430..446
FT /evidence="ECO:0007829|PDB:3A8U"
SQ SEQUENCE 449 AA; 48614 MW; EC139EB6B0C1FBD9 CRC64;
NMPEHAGASL ASQLKLDAHW MPYTANRNFL RDPRLIVAAE GSWLVDDKGR KVYDSLSGLW
TCGAGHTRKE IQEAVAKQLS TLDYSPGFQY GHPLSFQLAE KITDLTPGNL NHVFFTDSGS
ECALTAVKMV RAYWRLKGQA TKTKMIGRAR GYHGVNIAGT SLGGVNGNRK LFGQPMQDVD
HLPHTLLASN AYSRGMPKEG GIALADELLK LIELHDASNI AAVFVEPLAG SAGVLVPPEG
YLKRNREICN QHNILLVFDE VITGFGRTGS MFGADSFGVT PDLMCIAKQV TNGAIPMGAV
IASTEIYQTF MNQPTPEYAV EFPHGYTYSA HPVACAAGLA ALCLLQKENL VQSVAEVAPH
FEKALHGIKG AKNVIDIRNF GLAGAIQIAP RDGDAIVRPF EAGMALWKAG FYVRFGGDTL
QFGPTFNSKP QDLDRLFDAV GEVLNKLLD
