Q42667 (PALY_CITLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phenylalanine ammonia-lyase
EC=4.3.1.24

Gene names

Name:

PAL6

Organism

Citrus limon (Lemon) (Citrus limonum)

Taxonomic identifier

2708 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Sapindales › Rutaceae › Citrus

Protein attributes

Sequence length	722 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	This is a key enzyme of plant metabolism catalyzing the first reaction in the biosynthesis from L-phenylalanine of a wide variety of natural products based on the phenylpropane skeleton.
Catalytic activity	L-phenylalanine = trans-cinnamate + ammonia.
Pathway	Phenylpropanoid metabolism; trans-cinnamate biosynthesis; trans-cinnamate from L-phenylalanine: step 1/1.
Subcellular location	Cytoplasm Probable.
Post-translational modification	Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly By similarity.
Sequence similarities	Belongs to the PAL/histidase family.

Ontologies

Keywords
Biological process	Phenylpropanoid metabolism
Cellular component	Cytoplasm
Molecular function	Lyase
Gene Ontology (GO)
Biological process	L-phenylalanine catabolic process Inferred from electronic annotation. Source: InterPro biosynthetic process Inferred from electronic annotation. Source: InterPro phenylpropanoid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ammonia-lyase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 722	722	Phenylalanine ammonia-lyase		PRO_0000215389
Amino acid modifications
	Modified residue	207	1	2,3-didehydroalanine (Ser) By similarity
	Cross-link	206 ↔ 208		5-imidazolinone (Ala-Gly) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q42667 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: C96893196E30D9E5	FASTA	722	78,490
	10 20 30 40 50 60 MELSHETCNG IKNDRNGGTS SLGLCTGTDP LNWTVAADSL KGSHLDEVKR MIDEYRRPVV 70 80 90 100 110 120 KLGGESLTIG QVTAIAAHDS GVKVELAEAA RAGVKASSDW VMDSMMKGTD SYGVTTGFGA 130 140 150 160 170 180 TSHRRTKQGG ALQKELIRFL NSGIFGNGTE SSHTLPHSAT RAAMLVRVNT LLQGYSGIRF 190 200 210 220 230 240 EILETITKFL NHNITPCLPL RGTITASGDL VPLSYIAGLL TGRPNSKAVG SNGQVLNPTE 250 260 270 280 290 300 AFNLAGVTSG FFELQPKEGL ALVNGTAVGS GLAATVLFEA NILAIMSEVL SAIFAEVMNG 310 320 330 340 350 360 KPEFTDHLTH KLKHHPGQIE AAAIMEHILD GSSYVKAAQK LHETDPLQKP KQDRYALRTS 370 380 390 400 410 420 PQWLGPQIEV IRAATKMIER EINSVNDNPL IDVSRNKALH GGNFQGTPIG VSMDNTRLAI 430 440 450 460 470 480 ASIGKLMFAQ FSELVNDFYN NGLPSNLTGG RNPSLDYGFK GAEIAMASYC SELQFLANPV 490 500 510 520 530 540 TNHVQSAEQH NQDVNSLGLN SSRKTAEAVD ILKLMSSTFL VALCQAIDLR HLEENLKNTV 550 560 570 580 590 600 KNTVSQVAKR VLTMGVNGEL HPSRFCEKDL IKVVDREYVF AYIDDPCSAS SPLMQKLRQV 610 620 630 640 650 660 LVDHALDNGD REKNSTTSIF QKIGAFEDEL KTLLPKEVEI ARTELESGNA AIPNRIKECR 670 680 690 700 710 720 SYPLYKIVRE DIGTSLLTGE KVRSPGEEFD KVFTAMCEGK LIDPMLECLK EWNGAPLPIC QN

References

[1]	"A full-length cDNA coding for phenylalanine ammonia-lyase from Citrus limon." Seelenfreund D., Chiong M., Lobos S., Perez L.M. Plant Gene Register PGR96-026 Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	U43338 mRNA. Translation: AAB67733.1.
3D structure databases
ProteinModelPortal	Q42667.
SMR	Q42667. Positions 29-720.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR008948. L-Aspartase-like. IPR024083. L-Aspartase-like_N. IPR001106. Phe/His_NH3-lyase. IPR022313. Phe/His_NH3-lyase_AS. IPR005922. Phe_NH3-lyase. IPR023144. Phe_NH3-lyase_shielding_dom. [Graphical view]
Gene3D	G3DSA:1.10.275.10. G3DSA:1.10.275.10. 1 hit. G3DSA:1.10.274.20. Phe_NH3-lyase_shielding_dom. 1 hit.
Pfam	PF00221. PAL. 1 hit. [Graphical view]
SUPFAM	SSF48557. L-Aspartase-like. 1 hit.
TIGRFAMs	TIGR01226. Phe_am_lyase. 1 hit.
PROSITE	PS00488. PAL_HISTIDASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PALY_CITLI

Accession

Primary (citable) accession number: Q42667

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	November 16, 2011
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program