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HUTH_LEGPH
ID   HUTH_LEGPH              Reviewed;         506 AA.
AC   Q5ZVR0;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   25-MAY-2022, entry version 102.
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=lpg1380;
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS   33152 / DSM 7513).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA   Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA   Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA   Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA   Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA   Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA   Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL   Science 305:1966-1968(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAU27462.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE017354; AAU27462.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_015444533.1; NC_002942.5.
DR   RefSeq; YP_095409.1; NC_002942.5.
DR   AlphaFoldDB; Q5ZVR0; -.
DR   SMR; Q5ZVR0; -.
DR   STRING; 272624.lpg1380; -.
DR   PaxDb; Q5ZVR0; -.
DR   EnsemblBacteria; AAU27462; AAU27462; lpg1380.
DR   GeneID; 66490512; -.
DR   KEGG; lpn:lpg1380; -.
DR   PATRIC; fig|272624.6.peg.1450; -.
DR   eggNOG; COG2986; Bacteria.
DR   HOGENOM; CLU_014801_4_0_6; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000000609; 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..506
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_0000161011"
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;  54720 MW;  323D9D14F66E0527 CRC64;
     MSEQFILQPG QLSLLSIKQI LDEELSCVLA ENSFELIRAS HQTVKKVIDE KKTVYGINTG
     FGSLANQTIS SDCLKELQRN IVLSHACGTG KLLPDDVVAL ILLLKINNLS QGYSGVRLEL
     INALIALFNH KVYPCIPSKG SVGASGDLVP LAHLSLPLLG EGEVRHQGQV ISAEEGLKLA
     GLKPLELEAK EGLALLNGLQ VSTALALSAL FISETLFETA IISGSLSVDA ASGSDVPFDD
     RIHQIRGHQA QISAASMYRN LLAGSQIRES HRHCNRVQDP YSLRCQPQIM GAILHQMQFV
     GQTLQVEANA ISDNPLVFAE QGDILSGGNF HGEIIAMAAD NLALALSEIG GSAERRIALL
     IDKNFSGLPA FLVRESGLNS GFMIAHVTAA SCASDNKALA HPHSVDSLPT SANQEDHVSM
     ATSAARRLHE MIDNTSTILA IELLAACQGL EFHKPLKTSP QLDKIYQSVR SVVKEYDKDR
     YFAPDIEKIK KKILDKEFSL LTLTNE
 
 
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