Reviewed, UniProtKB/Swiss-Prot P21310 (HUTH_PSEPU)

Names and origin

Protein names

Recommended name:
    Histidine ammonia-lyase
      Short name=Histidase
    EC=4.3.1.3

Gene names

Name:

hutH

Organism

Pseudomonas putida

Taxonomic identifier

303 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	510 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	L-histidine = urocanate + NH3. HAMAP MF_00229
Pathway	Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3. HAMAP MF_00229
Subunit structure	Homotetramer. HAMAP MF_00229
Subcellular location	Cytoplasm Potential.
Induction	By histidine and urocanate. HAMAP MF_00229
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. HAMAP MF_00229
Sequence similarities	Belongs to the PAL/histidase family.

Ontologies

Keywords
Biological process	Histidine metabolism
Cellular component	Cytoplasm
Molecular function	Lyase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	biosynthetic process Inferred from electronic annotation. Source: InterPro histidine catabolic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ammonia ligase activity Inferred from electronic annotation. Source: InterPro histidine ammonia-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

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 510

509

Histidine ammonia-lyase HAMAP MF_00229

PRO_0000161017

Amino acid modifications

Modified residue

144

1

2,3-didehydroalanine (Ser) HAMAP MF_00229

Cross-link

143 ↔ 145

5-imidazolinone (Ala-Gly) HAMAP MF_00229

Experimental info

Mutagenesis

113

1

S → A: No loss of activity. HAMAP MF_00229

Mutagenesis

144

1

S → A or T: Complete loss of activity. Ref.5

Mutagenesis

144

1

S → C: No effect. Ref.5

Mutagenesis

394

1

S → A: No loss of activity. HAMAP MF_00229

Mutagenesis

419

1

S → A: No loss of activity. HAMAP MF_00229

Sequence conflict

152

1

H → T in AAA25840. Ref.1

Sequence conflict

439

1

L → P in AAA25840. Ref.1

Secondary structure

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510

Helix Strand Turn

Details...

Beta strand

4 – 6

3

Helix

13 – 21

9

Beta strand

26 – 28

3

Helix

30 – 32

3

Helix

33 – 48

16

Turn

54 – 56

3

Helix

61 – 63

3

Helix

70 – 84

15

Beta strand

88 – 91

4

Helix

94 – 109

16

Helix

117 – 129

13

Beta strand

136 – 138

3

Helix

147 – 155

9

Helix

156 – 158

3

Beta strand

161 – 165

5

Beta strand

168 – 171

4

Helix

172 – 178

7

Helix

190 – 195

6

Beta strand

196 – 198

3

Helix

199 – 229

31

Helix

235 – 237

3

Helix

239 – 245

7

Helix

248 – 261

14

Helix

266 – 269

4

Helix

281 – 284

4

Helix

286 – 308

23

Beta strand

314 – 317

4

Turn

319 – 321

3

Helix

333 – 361

29

Helix

363 – 366

4

Helix

370 – 372

3

Turn

374 – 378

5

Helix

383 – 399

17

Helix

411 – 413

3

Helix

421 – 452

32

Helix

460 – 470

11

Helix

483 – 494

12

Turn

495 – 498

4

Helix

499 – 501

3

Sequences

	Sequence		Length	Mass (Da)
	P21310-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 7D80C7E64B0C4F57	FASTA	510	53,761
	10 20 30 40 50 60 MTELTLKPGT LTLAQLRAIH AAPVRLQLDA SAAPAIDASV ACVEQIIAED RTAYGINTGF 70 80 90 100 110 120 GLLASTRIAS HDLENLQRSL VLSHAAGIGA PLDDDLVRLI MVLKINSLSR GFSGIRRKVI 130 140 150 160 170 180 DALIALVNAE VYPHIPLKGS VGASGDLAPL AHMSLVLLGE GKARYKGQWL SATEALAVAG 190 200 210 220 230 240 LEPLTLAAKE GLALLNGTQA STAYALRGLF YAEDLYAAAI ACGGLSVEAV LGSRSPFDAR 250 260 270 280 290 300 IHEARGQRGQ IDTAACFRDL LGDSSEVSLS HKNCDKVQDP YSLRCQPQVM GACLTQLRQA 310 320 330 340 350 360 AEVLGIEANA VSDNPLVFAA EGDVISGGNF HAEPVAMAAD NLALAIAEIG SLSERRISLM 370 380 390 400 410 420 MDKHMSQLPP FLVENGGVNS GFMIAQVTAA ALASENKALS HPHSVDSLPT SANQEDHVSM 430 440 450 460 470 480 APAAGKRLWE MAENTRGVLA IEWLGACQGL DLRKGLKTSA KLEKARQALR SEVAHYDRDR 490 500 510 FFAPDIEKAV ELLAKGSLTG LLPAGVLPSL

References

[1]	"Sequence analysis of the hutH gene encoding histidine ammonia-lyase in Pseudomonas putida." Consevage M.W., Phillips A.T. J. Bacteriol. 172:2224-2229(1990) [PubMed: 2332400] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13. Strain: ATCC 12633 / DSM 291 / NCIB 9494 / NCTC 10936 / Stanier 90.
[2]	"Identification of Ser143 as the site of modification in the active site of histidine ammonia-lyase." Hernandez D., Stroh J.G., Phillips A.T. Arch. Biochem. Biophys. 307:126-132(1993) [PubMed: 8239649] [Abstract] Cited for: ACTIVE SITE.
[3]	"Ser-143 is an essential active site residue in histidine ammonia-lyase of Pseudomonas putida." Hernandez D., Phillips A.T. Biochem. Biophys. Res. Commun. 201:1433-1438(1994) [PubMed: 8024588] [Abstract] Cited for: ACTIVE SITE, MUTAGENESIS.
[4]	"Identification of serine-143 as the most likely precursor of dehydroalanine in the active site of histidine ammonia-lyase. A study of the overexpressed enzyme by site-directed mutagenesis." Langer M., Reck G., Reed J., Retey J. Biochemistry 33:6462-6467(1994) [PubMed: 8204579] [Abstract] Cited for: ACTIVE SITE, MUTAGENESIS.
[5]	"Histidine ammonia-lyase mutant S143C is posttranslationally converted into fully active wild-type enzyme. Evidence for serine 143 to be the precursor of active site dehydroalanine." Langer M., Lieber A., Retey J. Biochemistry 33:14034-14038(1994) [PubMed: 7947813] [Abstract] Cited for: ACTIVE SITE, MUTAGENESIS OF SER-144.
[6]	"Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile." Schwede T.F., Retey J., Schulz G.E. Biochemistry 38:5355-5361(1999) [PubMed: 10220322] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SEQUENCE REVISION TO 152 AND 439. Strain: ATCC 12633 / DSM 291 / NCIB 9494 / NCTC 10936 / Stanier 90.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M35140 Genomic DNA. Translation: AAA25840.1.

PIR

A35251.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B8F	X-ray	2.10	A	2-510	[»]
1EB4	X-ray	2.00	A	2-509	[»]
1GK2	X-ray	1.90	A/B/C/D	2-509	[»]
1GK3	X-ray	2.25	A	2-509	[»]
1GKJ	X-ray	1.70	A	2-509	[»]
1GKM	X-ray	1.00	A	2-509	[»]

ModBase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MON-11608.

BRENDA

4.3.1.3. 403.

Family and domain databases

HAMAP

MF_00229.
[Tree]

InterPro

IPR005921. HutH.
IPR001106. Phe/His_NH3-lyase.
[Graphical view]

Pfam

PF00221. PAL. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01225. hutH. 1 hit.

PROSITE

PS00488. PAL_HISTIDASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

HUTH_PSEPU

Accession

Primary (citable) accession number: P21310

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 78 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)