PHNW_PSEAE
ID PHNW_PSEAE Reviewed; 371 AA.
AC Q9I434;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=2-aminoethylphosphonate--pyruvate transaminase;
DE EC=2.6.1.37;
DE AltName: Full=2-aminoethylphosphonate aminotransferase;
DE AltName: Full=AEP transaminase;
DE Short=AEPT;
GN Name=phnW; OrderedLocusNames=PA1310;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP BIOPHYSICAL CHARACTERIZATION, INDUCTION, ACTIVITY REGULATION, COFACTOR, AND
RP SUBUNIT.
RC STRAIN=A237;
RX PubMed=6406228; DOI=10.1111/j.1432-1033.1983.tb07436.x;
RA Dumora C., Lacoste A.-M., Cassaigne A.;
RT "Purification and properties of 2-aminoethylphosphonate:pyruvate
RT aminotransferase from Pseudomonas aeruginosa.";
RL Eur. J. Biochem. 133:119-125(1983).
RN [3]
RP STEREOSPECIFICITY.
RC STRAIN=A237;
RX PubMed=8394813; DOI=10.1111/j.1432-1033.1993.tb18100.x;
RA Lacoste A.-M., Dumora C., Balas L., Hammerschmidt F., Vercauteren J.;
RT "Stereochemistry of the reaction catalysed by 2-aminoethylphosphonate
RT aminotransferase. A 1H-NMR study.";
RL Eur. J. Biochem. 215:841-844(1993).
CC -!- FUNCTION: Involved in phosphonate degradation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2-aminoethyl)phosphonate + pyruvate = L-alanine +
CC phosphonoacetaldehyde; Xref=Rhea:RHEA:17021, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:57418, ChEBI:CHEBI:57972, ChEBI:CHEBI:58383; EC=2.6.1.37;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:6406228};
CC Note=1 pyridoxal phosphate per subunit. {ECO:0000269|PubMed:6406228};
CC -!- ACTIVITY REGULATION: Inhibited by phosphonic acids and very slightly
CC inhibited by aminophosphonic acids. {ECO:0000269|PubMed:6406228}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.85 mM for 2-aminoethylphosphonate;
CC KM=3.5 mM for pyruvate;
CC pH dependence:
CC Optimum pH is 8.5-9.;
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius. Activity increases from 30
CC to 50 degrees Celsius, the enzyme is inactive at 70 degrees Celsius.;
CC -!- SUBUNIT: Homotetramer; however this is for an enzyme with a molecular
CC weight of 16500, which is in disagreement with the weight of this
CC protein. {ECO:0000269|PubMed:6406228}.
CC -!- INDUCTION: By 2-aminoethylphosphonic acid.
CC {ECO:0000269|PubMed:6406228}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. PhnW subfamily. {ECO:0000305}.
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DR EMBL; AE004091; AAG04699.1; -; Genomic_DNA.
DR PIR; B83482; B83482.
DR RefSeq; NP_250001.1; NC_002516.2.
DR RefSeq; WP_003112368.1; NZ_QZGE01000005.1.
DR PDB; 7E7G; X-ray; 2.35 A; A=1-371.
DR PDBsum; 7E7G; -.
DR AlphaFoldDB; Q9I434; -.
DR SMR; Q9I434; -.
DR STRING; 287.DR97_484; -.
DR PaxDb; Q9I434; -.
DR PRIDE; Q9I434; -.
DR EnsemblBacteria; AAG04699; AAG04699; PA1310.
DR GeneID; 881491; -.
DR KEGG; pae:PA1310; -.
DR PATRIC; fig|208964.12.peg.1361; -.
DR PseudoCAP; PA1310; -.
DR HOGENOM; CLU_027686_3_1_6; -.
DR InParanoid; Q9I434; -.
DR OMA; IRINHMG; -.
DR PhylomeDB; Q9I434; -.
DR BioCyc; MetaCyc:MON-15967; -.
DR BioCyc; PAER208964:G1FZ6-1335-MON; -.
DR BRENDA; 2.6.1.37; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0047304; F:2-aminoethylphosphonate-pyruvate transaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0019700; P:organic phosphonate catabolic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_01376; PhnW_aminotrans_5; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR012703; NH2EtPonate_pyrv_transaminase.
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 TIGRFAMs; TIGR03301; PhnW-AepZ; 1.
DR TIGRFAMs; TIGR02326; transamin_PhnW; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Pyridoxal phosphate; Pyruvate;
KW Reference proteome; Transferase.
FT CHAIN 1..371
FT /note="2-aminoethylphosphonate--pyruvate transaminase"
FT /id="PRO_0000286773"
FT MOD_RES 195
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:7E7G"
FT HELIX 20..24
FT /evidence="ECO:0007829|PDB:7E7G"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:7E7G"
FT HELIX 35..52
FT /evidence="ECO:0007829|PDB:7E7G"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:7E7G"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:7E7G"
FT HELIX 67..78
FT /evidence="ECO:0007829|PDB:7E7G"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:7E7G"
FT HELIX 92..103
FT /evidence="ECO:0007829|PDB:7E7G"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:7E7G"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:7E7G"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:7E7G"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:7E7G"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:7E7G"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:7E7G"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:7E7G"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:7E7G"
FT TURN 171..176
FT /evidence="ECO:0007829|PDB:7E7G"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:7E7G"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:7E7G"
FT STRAND 201..209
FT /evidence="ECO:0007829|PDB:7E7G"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:7E7G"
FT HELIX 227..237
FT /evidence="ECO:0007829|PDB:7E7G"
FT HELIX 246..262
FT /evidence="ECO:0007829|PDB:7E7G"
FT HELIX 264..284
FT /evidence="ECO:0007829|PDB:7E7G"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:7E7G"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:7E7G"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:7E7G"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:7E7G"
FT HELIX 314..323
FT /evidence="ECO:0007829|PDB:7E7G"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:7E7G"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:7E7G"
FT HELIX 349..364
FT /evidence="ECO:0007829|PDB:7E7G"
SQ SEQUENCE 371 AA; 40418 MW; E897ACF4F852D14D CRC64;
MSTAERAPIL LTPGPLTTSY RTRRAMMVDW GSWDSDFNEL TASVCQRLLK IVGGEGSHTC
VPLQGSGTFA VEAAIGTLVP RDGKVLVLIN GAYGKRLAKI CEVLQRPFST LETEENVPTT
AADVERLLAA DPAISHVALI HCETSTGILN PLEAIAKVVE RHGKRLIVDA MSSFGAIGID
ARKVPFDALI AASGKCLEGV PGMGFVFARS AALEASAGNC HSLAMDLQDQ HAYMRKTGQW
RFTPPTHVVA ALHEALSQYE EEGGLPARQR RYASNCETLL GEMARLGFRS FLPAEIQAPI
IVTFHAPRDP RYRFADFYQR VREKGFILYP GKLTQVETFR VGCIGHVDAA EMRQAVAAIG
EALRELEVLE I
