ID HUTH_PSEPF Reviewed; 510 AA. AC Q3KJE6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 16-JUN-2009, entry version 33. DE RecName: Full=Histidine ammonia-lyase; DE Short=Histidase; DE EC=4.3.1.3; GN Name=hutH; OrderedLocusNames=Pfl01_0366; OS Pseudomonas fluorescens (strain Pf0-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=205922; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., RA Larimer F., Land M., Kyripides N., Anderson I., Richardson P.; RT "Complete sequence of Pseudomonas fluorescens PfO-1."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: L-histidine = urocanate + NH(3). CC -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L- CC glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), CC which is formed autocatalytically by cyclization and dehydration CC of residues Ala-Ser-Gly (By similarity). CC -!- SIMILARITY: Belongs to the PAL/histidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000094; ABA72110.1; -; Genomic_DNA. DR RefSeq; YP_346099.1; -. DR SMR; Q3KJE6; 2-510. DR GeneID; 3713414; -. DR GenomeReviews; CP000094_GR; Pfl01_0366. DR KEGG; pfo:Pfl01_0366; -. DR HOGENOM; Q3KJE6; -. DR OMA; Q3KJE6; FAPDIEA. DR BioCyc; PFLU205922:PFL_0366-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016211; F:ammonia ligase activity; IEA:InterPro. DR GO; GO:0004397; F:histidine ammonia-lyase activity; IEA:HAMAP. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR GO; GO:0006548; P:histidine catabolic process; IEA:HAMAP. DR HAMAP; MF_00229; -; 1. DR InterPro; IPR005921; HutH. DR InterPro; IPR001106; Phe/His_NH3-lyase. DR Pfam; PF00221; PAL; 1. DR TIGRFAMs; TIGR01225; hutH; 1. DR PROSITE; PS00488; PAL_HISTIDASE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Histidine metabolism; Lyase. FT CHAIN 1 510 Histidine ammonia-lyase. FT /FTId=PRO_1000021566. FT MOD_RES 144 144 2,3-didehydroalanine (Ser) (By FT similarity). FT CROSSLNK 143 145 5-imidazolinone (Ala-Gly) (By FT similarity). SQ SEQUENCE 510 AA; 54108 MW; 8646F690D1E5D65A CRC64; MTALNLIPGQ LSLAQLRDVY QNPVKLTLDN SASAQIEASV ACVEQILAEN RTAYGINTGF GLLASTRIAS EDLENLQRSL VLSHAAGVGQ PISDELVRLI MVLKVNSLSR GFSGIRRVVI DALIALINAE VYPHIPLKGS VGASGDLAPL AHMSLVLLGE GKARHKGEWM DATEALKVAG LTPLTLAAKE GLALLNGTQV STAFALRGLF EGEDLFAGAL ALGGLTVEAV LGSRSPFDAR IHAARGQKGQ IDAAAAYRDL LGERSEVSDS HQNCEKVQDP YSLRCQPQVM GACLTQFRQA AEVLAIEANA VSDNPLVFAA EGDVISGGNF HAEPVAMAAD NMALAIAEIG SLSERRISLM MDKHMSQLPP FLVANGGVNS GFMIAQVTAA ALASENKALS HPHSVDSLPT SANQEDHVSM APAAGKRLWE MAENTRGILA VEWLAAVQGL DLRNGLKTSA KLEQARGILR REVPFYEKDR FFAPDINAAT ELLASRILTE LVPAKLLPSL //