ID   HUTH_PSEPK              Reviewed;         510 AA.
AC   Q88CZ7;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Histidine ammonia-lyase {ECO:0000255|HAMAP-Rule:MF_00229};
DE            Short=Histidase {ECO:0000255|HAMAP-Rule:MF_00229};
DE            EC=4.3.1.3 {ECO:0000255|HAMAP-Rule:MF_00229};
GN   Name=hutH {ECO:0000255|HAMAP-Rule:MF_00229}; OrderedLocusNames=PP_5032;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidine = NH4(+) + trans-urocanate; Xref=Rhea:RHEA:21232,
CC         ChEBI:CHEBI:17771, ChEBI:CHEBI:28938, ChEBI:CHEBI:57595; EC=4.3.1.3;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00229};
CC   -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC       glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3.
CC       {ECO:0000255|HAMAP-Rule:MF_00229}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00229}.
CC   -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which
CC       is formed autocatalytically by cyclization and dehydration of residues
CC       Ala-Ser-Gly. {ECO:0000255|HAMAP-Rule:MF_00229}.
CC   -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00229}.
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DR   EMBL; AE015451; AAN70597.1; -; Genomic_DNA.
DR   RefSeq; NP_747133.1; NC_002947.4.
DR   RefSeq; WP_010955589.1; NC_002947.4.
DR   AlphaFoldDB; Q88CZ7; -.
DR   SMR; Q88CZ7; -.
DR   STRING; 160488.PP_5032; -.
DR   PRIDE; Q88CZ7; -.
DR   EnsemblBacteria; AAN70597; AAN70597; PP_5032.
DR   KEGG; ppu:PP_5032; -.
DR   PATRIC; fig|160488.4.peg.5373; -.
DR   eggNOG; COG2986; Bacteria.
DR   HOGENOM; CLU_014801_4_0_6; -.
DR   OMA; CAPQVAG; -.
DR   PhylomeDB; Q88CZ7; -.
DR   BioCyc; PPUT160488:G1G01-5377-MON; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000000556; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004397; F:histidine ammonia-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019556; P:histidine catabolic process to glutamate and formamide; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019557; P:histidine catabolic process to glutamate and formate; IEA:UniProtKB-UniPathway.
DR   CDD; cd00332; PAL-HAL; 1.
DR   Gene3D; 1.10.275.10; -; 1.
DR   HAMAP; MF_00229; His_ammonia_lyase; 1.
DR   InterPro; IPR001106; Aromatic_Lyase.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR005921; HutH.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   InterPro; IPR022313; Phe/His_NH3-lyase_AS.
DR   PANTHER; PTHR10362; PTHR10362; 1.
DR   Pfam; PF00221; Lyase_aromatic; 1.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   TIGRFAMs; TIGR01225; hutH; 1.
DR   PROSITE; PS00488; PAL_HISTIDASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Histidine metabolism; Lyase; Reference proteome.
FT   CHAIN           1..510
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_0000161018"
FT   MOD_RES         144
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
FT   CROSSLNK        143..145
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
SQ   SEQUENCE   510 AA;  53748 MW;  50449328B4CCAFBC CRC64;
     MTELTLKPGT LTLAQLRAIH AAPVRLQLDA SAAPAIDASV ACVEQIIAED RTAYGINTGF
     GLLASTRIAS HDLENLQRSL VLSHAAGIGA PLDDDLVRLI MVLKINSLSR GFSGIRRKVI
     DALIALVNAE VYPHIPLKGS VGASGDLAPL AHMSLVLLGE GKARYKGQWL PATEALAIAG
     LEPLTLAAKE GLALLNGTQA STAYALRGLF QAEDLYAAAI ACGGLSVEAA LGSRSPFDAR
     VHEVRGQRGQ IDTAACFRDL LGDSSEVSLS HKNCDKVQDP YSLRCQPQVM GACLTQLRQA
     AEVLGIEANA VSDNPLVFAA EGDVISGGNF HAEPVAMAAD NLALAIAEIG SLSERRISLM
     MDKHMSQLPP FLVENGGVNS GFMIAQVTAA ALASENKALS HPHSVDSLPT SANQEDHVSM
     APAAGKRLWE MAENTRGVLA IEWLGACQGL DLRKGLKTSA KLEQARQALR SEVPHYDRDR
     FFAPDIEKAV DLLAKGSLTG LLPAGVLPSL