PAL_NOSP7
ID PAL_NOSP7 Reviewed; 569 AA.
AC B2J528;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Phenylalanine ammonia-lyase {ECO:0000303|PubMed:17240984};
DE EC=4.3.1.24 {ECO:0000269|PubMed:17240984};
GN OrderedLocusNames=Npun_R2068;
OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=63737;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29133 / PCC 73102;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, PTM, AND DEHYDRATION AT SER-168.
RX PubMed=17240984; DOI=10.1021/bi061774g;
RA Moffitt M.C., Louie G.V., Bowman M.E., Pence J., Noel J.P., Moore B.S.;
RT "Discovery of two cyanobacterial phenylalanine ammonia lyases: kinetic and
RT structural characterization.";
RL Biochemistry 46:1004-1012(2007).
CC -!- FUNCTION: Catalyzes the non-oxidative deamination of L-phenylalanine to
CC form trans-cinnamic acid, the first step in the phenylpropanoid
CC pathway. {ECO:0000269|PubMed:17240984}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-phenylalanine = (E)-cinnamate + NH4(+);
CC Xref=Rhea:RHEA:21384, ChEBI:CHEBI:15669, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58095; EC=4.3.1.24;
CC Evidence={ECO:0000269|PubMed:17240984};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.045 mM for phenylalanine {ECO:0000269|PubMed:17240984};
CC Note=kcat is 1.96 sec(-1) for phenylalanine.;
CC pH dependence:
CC Optimum pH is 7.7-8.5 (PubMed:17240984 and PubMed:18556022).
CC {ECO:0000269|PubMed:17240984};
CC -!- PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis;
CC trans-cinnamate from L-phenylalanine: step 1/1.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17240984}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which
CC is formed autocatalytically by cyclization and dehydration of residues
CC Ala-Ser-Gly. {ECO:0000269|PubMed:17240984}.
CC -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000305}.
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DR EMBL; CP001037; ACC80688.1; -; Genomic_DNA.
DR RefSeq; WP_012408693.1; NC_010628.1.
DR PDB; 2NYF; X-ray; 2.50 A; A=1-569.
DR PDBsum; 2NYF; -.
DR AlphaFoldDB; B2J528; -.
DR SMR; B2J528; -.
DR STRING; 63737.Npun_R2068; -.
DR EnsemblBacteria; ACC80688; ACC80688; Npun_R2068.
DR KEGG; npu:Npun_R2068; -.
DR eggNOG; COG2986; Bacteria.
DR HOGENOM; CLU_014801_3_2_3; -.
DR OMA; CAPQVAG; -.
DR OrthoDB; 715502at2; -.
DR PhylomeDB; B2J528; -.
DR BRENDA; 4.3.1.24; 4370.
DR SABIO-RK; B2J528; -.
DR UniPathway; UPA00713; UER00725.
DR Proteomes; UP000001191; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045548; F:phenylalanine ammonia-lyase activity; IDA:UniProtKB.
DR GO; GO:0009072; P:aromatic amino acid family metabolic process; IDA:UniProtKB.
DR GO; GO:0009800; P:cinnamic acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009699; P:phenylpropanoid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR CDD; cd00332; PAL-HAL; 1.
DR Gene3D; 1.10.275.10; -; 1.
DR InterPro; IPR001106; Aromatic_Lyase.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR InterPro; IPR022313; Phe/His_NH3-lyase_AS.
DR PANTHER; PTHR10362; PTHR10362; 1.
DR Pfam; PF00221; Lyase_aromatic; 1.
DR SUPFAM; SSF48557; SSF48557; 1.
DR PROSITE; PS00488; PAL_HISTIDASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lyase; Phenylalanine catabolism;
KW Phenylpropanoid metabolism; Reference proteome.
FT CHAIN 1..569
FT /note="Phenylalanine ammonia-lyase"
FT /id="PRO_0000429967"
FT ACT_SITE 78
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 451
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT MOD_RES 168
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000269|PubMed:17240984"
FT CROSSLNK 167..169
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000269|PubMed:17240984"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:2NYF"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 54..73
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 94..107
FT /evidence="ECO:0007829|PDB:2NYF"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 118..132
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 141..153
FT /evidence="ECO:0007829|PDB:2NYF"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:2NYF"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:2NYF"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:2NYF"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 199..205
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:2NYF"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 226..256
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 275..287
FT /evidence="ECO:0007829|PDB:2NYF"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:2NYF"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 319..341
FT /evidence="ECO:0007829|PDB:2NYF"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:2NYF"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 366..394
FT /evidence="ECO:0007829|PDB:2NYF"
FT TURN 396..400
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:2NYF"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 419..435
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:2NYF"
FT TURN 445..452
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 458..495
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 506..519
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 533..535
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 538..551
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 554..557
FT /evidence="ECO:0007829|PDB:2NYF"
FT HELIX 560..563
FT /evidence="ECO:0007829|PDB:2NYF"
SQ SEQUENCE 569 AA; 62244 MW; F4EA2BF170FF0063 CRC64;
MNITSLQQNI TRSWQIPFTN SSDSIVTVGD RNLTIDEVVN VARHGTQVRL TDNADVIRGV
QASCDYINNA VETAQPIYGV TSGFGGMADV VISREQAAEL QTNLIWFLKS GAGNKLSLAD
VRAAMLLRAN SHLYGASGIR LELIQRIETF LNAGVTPHVY EFGSIGASGD LVPLSYITGA
LIGLDPSFTV DFDGKEMDAV TALSRLGLPK LQLQPKEGLA MMNGTSVMTG IAANCVYDAK
VLLALTMGVH ALAIQGLYGT NQSFHPFIHQ CKPHPGQLWT ADQMFSLLKD SSLVREELDG
KHEYRGKDLI QDRYSLRCLA QFIGPIVDGV SEITKQIEVE MNSVTDNPLI DVENQVSYHG
GNFLGQYVGV TMDRLRYYIG LLAKHIDVQI ALLVSPEFSN GLPPSLVGNS DRKVNMGLKG
LQISGNSIMP LLSFYGNSLA DRFPTHAEQF NQNINSQGYI SANLTRRSVD IFQNYMAIAL
MFGVQAVDLR TYKMKGHYDA RTCLSPNTVQ LYTAVCEVVG KPLTSVRPYI WNDNEQCLDE
HIARISADIA GGGLIVQAVE HIFSSLKST
