[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-13. STRAIN=ATCC 12633 / DSM 291 / NCIB 9494 / NCTC 10936 / Stanier 90; PubMed=2332400 [NCBI, ExPASy, EBI, Israel, Japan] Consevage M.W., Phillips A.T.; "Sequence analysis of the hutH gene encoding histidine ammonia-lyase in Pseudomonas putida."; J. Bacteriol. 172:2224-2229(1990).
[2]	ACTIVE SITE. DOI=10.1006/abbi.1993.1570; PubMed=8239649 [NCBI, ExPASy, EBI, Israel, Japan] Hernandez D., Stroh J.G., Phillips A.T.; "Identification of Ser143 as the site of modification in the active site of histidine ammonia-lyase."; Arch. Biochem. Biophys. 307:126-132(1993).
[3]	ACTIVE SITE, AND MUTAGENESIS. DOI=10.1006/bbrc.1994.1863; PubMed=8024588 [NCBI, ExPASy, EBI, Israel, Japan] Hernandez D., Phillips A.T.; "Ser-143 is an essential active site residue in histidine ammonia-lyase of Pseudomonas putida."; Biochem. Biophys. Res. Commun. 201:1433-1438(1994).
[4]	ACTIVE SITE, AND MUTAGENESIS. DOI=10.1021/bi00187a011; PubMed=8204579 [NCBI, ExPASy, EBI, Israel, Japan] Langer M., Reck G., Reed J., Retey J.; "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."; Biochemistry 33:6462-6467(1994).
[5]	ACTIVE SITE, AND MUTAGENESIS OF SER-144. DOI=10.1021/bi00251a011; PubMed=7947813 [NCBI, ExPASy, EBI, Israel, Japan] Langer M., Lieber A., Retey J.; "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."; Biochemistry 33:14034-14038(1994).
[6]	X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SEQUENCE REVISION TO 152 AND 439. STRAIN=ATCC 12633 / DSM 291 / NCIB 9494 / NCTC 10936 / Stanier 90; DOI=10.1021/bi982929q; PubMed=10220322 [NCBI, ExPASy, EBI, Israel, Japan] Schwede T.F., Retey J., Schulz G.E.; "Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile."; Biochemistry 38:5355-5361(1999).

Comments

CATALYTIC ACTIVITY: L-histidine = urocanate + NH₃.
PATHWAY: Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3 .
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Cytoplasm (Potential).
INDUCTION: By histidine and urocanate.
PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.
SIMILARITY: Belongs to the PAL/histidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M35140; AAA25840.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A35251; A35251.

3D structure databases

PDB

1B8F; X-ray; 2.10 A; A=1-510.	[ExPASy / RCSB / EBI]
1EB4; X-ray; 2.00 A; A=1-510.	[ExPASy / RCSB / EBI]
1GK2; X-ray; 1.90 A; A/B/C/D=1-510.	[ExPASy / RCSB / EBI]
1GK3; X-ray; 2.25 A; A=1-510.	[ExPASy / RCSB / EBI]
1GKJ; X-ray; 1.70 A; A=1-510.	[ExPASy / RCSB / EBI]
1GKM; X-ray; 1.00 A; A=1-510.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1B8F; -.
1EB4; -.
1GK2; -.
1GK3; -.
1GKJ; -.
1GKM; -.

ModBase

P21310.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-11608; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0016211;	Molecular function: ammonia ligase activity (inferred from electronic annotation from InterPro).
GO:0004397;	Molecular function: histidine ammonia-lyase activity (inferred from electronic annotation from HAMAP).
GO:0009058;	Biological process: biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006548;	Biological process: histidine catabolic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00229; -; 1.
PBIL [Tree]

InterPro

IPR005921; HutH.
IPR001106; Phe/His_NH3-lyase.
Graphical view of domain structure.

Pfam

PF00221; PAL; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01225; hutH; 1.

PROSITE

PS00488; PAL_HISTIDASE; 1.

ProtoNet

P21310.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cytoplasm; Direct protein sequencing; Histidine metabolism; Lyase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 510`	`509`	`Histidine ammonia-lyase.`	`PRO_0000161017`
`MOD_RES`	`144 144`		`2,3-didehydroalanine (Ser).`
`CROSSLNK`	`143 145`		`5-imidazolinone (Ala-Gly).`
`MUTAGEN`	`113 113`		`S->A: No loss of activity.`
`MUTAGEN`	`144 144`		`S->A,T: Complete loss of activity.`
`MUTAGEN`	`144 144`		`S->C: No effect.`
`MUTAGEN`	`394 394`		`S->A: No loss of activity.`
`MUTAGEN`	`419 419`		`S->A: No loss of activity.`
`CONFLICT`	`152 152`		`H -> T (in Ref. 1; AAA25840).`
`CONFLICT`	`439 439`		`L -> P (in Ref. 1; AAA25840).`
`STRAND`	`4 6`	`3`
`HELIX`	`13 21`	`9`
`STRAND`	`26 28`	`3`
`HELIX`	`30 32`	`3`
`HELIX`	`33 48`	`16`
`TURN`	`54 56`	`3`
`HELIX`	`61 63`	`3`
`HELIX`	`70 84`	`15`
`STRAND`	`88 91`	`4`
`HELIX`	`94 109`	`16`
`HELIX`	`117 129`	`13`
`STRAND`	`136 138`	`3`
`HELIX`	`147 155`	`9`
`HELIX`	`156 158`	`3`
`STRAND`	`161 165`	`5`
`STRAND`	`168 171`	`4`
`HELIX`	`172 178`	`7`
`HELIX`	`190 195`	`6`
`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`
`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`

Sequence information

Length: 510 AA [This is the length of the unprocessed precursor]

Molecular weight: 53761 Da [This is the MW of the unprocessed precursor]

CRC64: 7D80C7E64B0C4F57 [This is a checksum on the sequence]

        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

P21310 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools