P31013 (TPL_CITFR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine phenol-lyase
EC=4.1.99.2

Alternative name(s):
Beta-tyrosinase

Gene names

Name:

tpl

Organism

Citrobacter freundii

Taxonomic identifier

546 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Citrobacter

Protein attributes

Sequence length	456 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	L-tyrosine + H2O = phenol + pyruvate + NH3. HAMAP-Rule MF_00543
Cofactor	Pyridoxal phosphate.
Subunit structure	Homotetramer.
Sequence similarities	Belongs to the beta-eliminating lyase family.

Ontologies

Keywords
Ligand	Pyridoxal phosphate
Molecular function	Lyase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	tyrosine metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro tyrosine phenol-lyase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 456

456

Tyrosine phenol-lyase HAMAP-Rule MF_00543

PRO_0000195631

Amino acid modifications

Modified residue

257

1

N6-(pyridoxal phosphate)lysine HAMAP-Rule MF_00543

Experimental info

Sequence conflict

205

1

E → A in AAA23098. Ref.2

Secondary structure

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456

Helix Strand Turn

Details...

Beta strand

7 – 15

9

Helix

21 – 30

10

Turn

31 – 33

3

Helix

35 – 37

3

Helix

40 – 42

3

Beta strand

44 – 46

3

Beta strand

50 – 52

3

Helix

58 – 64

7

Beta strand

71 – 73

3

Helix

75 – 88

14

Beta strand

91 – 98

8

Helix

99 – 110

12

Beta strand

116 – 121

6

Helix

124 – 132

9

Beta strand

136 – 139

4

Helix

143 – 146

4

Turn

153 – 156

4

Helix

160 – 170

11

Helix

172 – 174

3

Beta strand

175 – 184

10

Turn

185 – 188

4

Helix

194 – 206

13

Beta strand

211 – 214

4

Helix

218 – 228

11

Helix

237 – 245

9

Beta strand

249 – 254

6

Turn

255 – 259

5

Beta strand

265 – 270

6

Helix

272 – 285

14

Turn

289 – 293

5

Helix

296 – 309

14

Helix

312 – 331

20

Beta strand

342 – 348

7

Helix

349 – 352

4

Turn

353 – 355

3

Helix

358 – 360

3

Helix

362 – 374

13

Beta strand

375 – 377

3

Beta strand

379 – 382

4

Helix

383 – 386

4

Turn

390 – 392

3

Beta strand

402 – 406

5

Turn

409 – 411

3

Helix

414 – 429

16

Helix

430 – 433

4

Beta strand

437 – 441

5

Beta strand

444 – 446

3

Helix

447 – 449

3

Beta strand

452 – 455

4

Sequences

	Sequence		Length	Mass (Da)
	P31013 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: B77AB58233C22474	FASTA	456	51,500
	10 20 30 40 50 60 MNYPAEPFRI KSVETVSMIP RDERLKKMQE AGYNTFLLNS KDIYIDLLTD SGTNAMSDKQ 70 80 90 100 110 120 WAGMMMGDEA YAGSENFYHL ERTVQELFGF KHIVPTHQGR GAENLLSQLA IKPGQYVAGN 130 140 150 160 170 180 MYFTTTRYHQ EKNGAVFVDI VRDEAHDAGL NIAFKGDIDL KKLQKLIDEK GAENIAYICL 190 200 210 220 230 240 AVTVNLAGGQ PVSMANMRAV RELTEAHGIK VFYDATRCVE NAYFIKEQEQ GFENKSIAEI 250 260 270 280 290 300 VHEMFSYADG CTMSGKKDCL VNIGGFLCMN DDEMFSSAKE LVVVYEGMPS YGGLAGRDME 310 320 330 340 350 360 AMAIGLREAM QYEYIEHRVK QVRYLGDKLK AAGVPIVEPV GGHAVFLDAR RFCEHLTQDE 370 380 390 400 410 420 FPAQSLAASI YVETGVRSME RGIISAGRNN VTGEHHRPKL ETVRLTIPRR VYTYAHMDVV 430 440 450 ADGIIKLYQH KEDIRGLKFI YEPKQLRFFT ARFDYI

References

[1]	"Structure of tyrosine phenol-lyase genes from Citrobacter freundii and structural comparison with tryptophanase from Escherichia coli." Iwamori S., Yoshino S., Ishiwata K., Makiguchi N. J. Ferment. Bioeng. 72:147-151(1991) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 8090 / DSM 30039 / JCM 1657 / LMG 3246 / NCTC 9750.
[2]	"Three-dimensional structure of tyrosine phenol-lyase." Antson A.A., Demidkina T.V., Gollnick P., Dauter Z., Vontersch R., Long J., Berezhnoy S.N., Phillips R.S., Harutyunyan D., Wilson K.S. Biochemistry 32:4195-4206(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 254-269; 275-299 AND 303-310, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), PYRIDOXAL PHOSPHATE AT LYS-257.
[3]	"The polypeptide chain fold in tyrosine phenol-lyase, a pyridoxal-5'-phosphate-dependent enzyme." Antson A.A., Strokopytov B.V., Murshudov G.N., Isupov M.N., Harutyunyan E.H., Demidkina T.V., Vassylyev D.G., Dauter Z., Terry H., Wilson K.S. FEBS Lett. 302:256-260(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[4]	"The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity." Sundararaju B., Antson A.A., Phillips R.S., Demidkina T.V., Barbolina M.V., Gollnick P., Dodson G.G., Wilson K.S. Biochemistry 36:6502-6510(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X66978 Genomic DNA. Translation: CAA47388.1.
L10821 Genomic DNA. Translation: AAA23098.1.

PIR

A49493.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TPL	X-ray	2.30	A/B	1-456	[»]
2EZ1	X-ray	1.90	A/B	1-456	[»]
2EZ2	X-ray	1.85	A/B	1-456	[»]
2TPL	X-ray	2.50	A/B	1-456	[»]
2VLF	X-ray	1.89	A/B	1-456	[»]
2VLH	X-ray	1.95	A/B	1-456	[»]
2YCN	X-ray	2.04	A/B	1-456	[»]
2YCP	X-ray	2.00	A/B/C/D	1-456	[»]
2YCT	X-ray	2.25	A/B	1-456	[»]
2YHK	X-ray	1.91	A/B	1-456	[»]

ProteinModelPortal

P31013.

SMR

P31013. Positions 1-456.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.

HAMAP

MF_00543. Tyr_phenol_lyase.

InterPro

IPR001597. ArAA_b-elim_lyase/Thr_aldolase.
IPR011166. Beta-eliminating_lyase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR018176. Tryptophanase_CS.
IPR013441. Tyr_phenol_ly.
[Graphical view]

Pfam

PF01212. Beta_elim_lyase. 1 hit.
[Graphical view]

PIRSF

PIRSF001386. Trpase. 1 hit.

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

TIGRFAMs

TIGR02618. tyr_phenol_ly. 1 hit.

PROSITE

PS00853. BETA_ELIM_LYASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P31013.

Entry information

Entry name

TPL_CITFR

Accession

Primary (citable) accession number: P31013

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	April 3, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program