ID   HUTH_STRSV              Reviewed;         513 AA.
AC   A3CL24;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 95.
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=SSA_0429;
OS   Streptococcus sanguinis (strain SK36).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=388919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK36;
RX   PubMed=17277061; DOI=10.1128/jb.01808-06;
RA   Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA   Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA   Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT   "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL   J. Bacteriol. 189:3166-3175(2007).
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=ABN43879.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000387; ABN43879.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_032916282.1; NC_009009.1.
DR   RefSeq; YP_001034429.1; NC_009009.1.
DR   AlphaFoldDB; A3CL24; -.
DR   SMR; A3CL24; -.
DR   STRING; 388919.SSA_0429; -.
DR   PRIDE; A3CL24; -.
DR   EnsemblBacteria; ABN43879; ABN43879; SSA_0429.
DR   KEGG; ssa:SSA_0429; -.
DR   PATRIC; fig|388919.9.peg.415; -.
DR   eggNOG; COG2986; Bacteria.
DR   HOGENOM; CLU_014801_4_0_9; -.
DR   OrthoDB; 715502at2; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000002148; 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..513
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_0000336590"
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;  55643 MW;  B5C2E9392B164339 CRC64;
     MTHVINLDGE HLTLEDVIAV ARHGATCEID QEAKKAVEAS RKIVDDIVRE KRVVYGVTTG
     FGSLCNVSIS PEDTTQLQEN LIRTHSSGYG DPLPEDAVRA IMLIRINSLV KGYSGIRLST
     VEKLLELLNK GVVPYIPEKG SLGASGDLAP LAHMVLPMLG LGRAYYQGQL LSGQEALDKA
     GIEKIALAAK EGLALINGTT VLTGIGALAT YDAIQLLKLS DVAGALSMEV HNGITSPFEE
     DLHTIRPQSG QLATARNIRN LLEGSGNTTV ATQQRVQDPY TLRCIPQIHG ASKDSIAYVK
     TKVEIEINSV TDNPIITKEG HVISGGNFHG EPMAQPFDFL GIAISEIGNV SERRVERLVN
     SQLSKLPSFL VKHPGLNSGF MITQYACASL ASENKVLSHP ASVDSIPSCE NQEDFVSMGT
     TAARKAAEIL KNSRRIVATE IMAACQALDL KPENHELGKG TKPAYDLFRQ HVRFIEFDKD
     IEIYEELNKA SELIENEEFL AAVEKAVDLS IQF