ID   HUTH_STRP8              Reviewed;         513 AA.
AC   Q8NZ46;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 107.
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=spyM18_2147;
OS   Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=186103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS8232;
RX   PubMed=11917108; DOI=10.1073/pnas.062526099;
RA   Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA   Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D.,
RA   Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A.,
RA   Veasy L.G., Musser J.M.;
RT   "Genome sequence and comparative microarray analysis of serotype M18 group
RT   A Streptococcus strains associated with acute rheumatic fever outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(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; AE009949; AAL98596.1; -; Genomic_DNA.
DR   RefSeq; WP_011018302.1; NC_003485.1.
DR   AlphaFoldDB; Q8NZ46; -.
DR   SMR; Q8NZ46; -.
DR   KEGG; spm:spyM18_2147; -.
DR   HOGENOM; CLU_014801_4_0_9; -.
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..513
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_0000161042"
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   513 AA;  55452 MW;  DFB8FC6182F00ED7 CRC64;
     MTRVINLDGE SLTLEDVIAI ARQGVACRID DSAIEAVNAS RKIVDDIVSE KRVVYGVTTG
     FGSLCNVSIS PEDTVQLQEN LIRTHASGFG DPLPEDAVRA IMLIRINSLV KGYSGIRLST
     IEKLLELLNK GVHPYIPEKG SLGASGDLAP LAHMVLPMLG LGKAYYKGEL LSGQEALDKA
     GIDKISLAAK EGLALINGTT VLTAIGALAT YDAIQLLKLS DLAGALSLEV HNGITSPFEE
     NLHTIRPQSG QLATARNIRN LLEGSQNTTV ATQSRVQDPY TLRCMPQIHG ASKDSIAYVK
     SKVDIEINSV TDNPIICKDG HVISGGNFHG EPMAQSFDFL GIAISEIGNV SERRVERLVN
     SQLSKLPSFL VKYPGLNSGF MITQYACASL ASENKVLAHP ASVDSIPSCE NQEDFVSMGT
     TAARKAFEIL KNSRRIVATE IMAACQALDL KPENHELGKG TKVAYDLFRK EVNFIEHDKH
     IEIYDELNKA SAVIEDPSFL EAVEQAVELS IQF