ID   HUTH_LEGPA              Reviewed;         506 AA.
AC   Q5X5I5;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=lpp1335;
OS   Legionella pneumophila (strain Paris).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Paris;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
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; CR628336; CAH12486.1; -; Genomic_DNA.
DR   RefSeq; WP_011213676.1; NC_006368.1.
DR   AlphaFoldDB; Q5X5I5; -.
DR   SMR; Q5X5I5; -.
DR   KEGG; lpp:lpp1335; -.
DR   LegioList; lpp1335; -.
DR   HOGENOM; CLU_014801_4_0_6; -.
DR   OMA; CAPQVAG; -.
DR   UniPathway; UPA00379; UER00549.
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.
FT   CHAIN           1..506
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_0000161010"
FT   MOD_RES         145
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
FT   CROSSLNK        144..146
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
SQ   SEQUENCE   506 AA;  54680 MW;  FFA906342D0EB1FE CRC64;
     MSEHFILQPG QLSLVSIKQI LDEELSCVLA EHAFELIRAS HQTVKKVIDE KKTVYGINTG
     FGSLANQTIS SDCLKELQRN IVLSHACGTG KLLPDSVVAL ILLLKINNLS QGYSGVRLEL
     INALIALFNH KVYPCIPSKG SVGASGDLVP LAHLSLPLLG EGEVRHQGQV ISAEEGLKLA
     GLKPLELEAK EGLALLNGLQ VSTALALSAL FISETLFETA IISGSLSVDA ASGSDVPFDD
     RIHQIRGHQA QISAASMYRN LLAGSQIRES HRHCNRVQDP YSLRCQPQIM GAVLHQMQFV
     GQTLQVEANA ISDNPLVFAE QGDILSGGNF HGEIIAMAAD NLALALSEIG GSAERRIALL
     IDKNFSGLPA FLVRESGLNS GFMIAHVTAA SCASDNKALA HPHSVDSLPT SANQEDHVSM
     ATSAARRLHE MIDNTSTILA IELLAACQGL EFHKPLKTSP QLDKIYQSVR SVVKEYDKDR
     YFAPDIEKIK KKILDKEFSL LTLTNE