ID   HUTH_STIAU              Reviewed;         510 AA.
AC   Q93TX3;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 74.
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};
OS   Stigmatella aurantiaca.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Archangiaceae; Stigmatella.
OX   NCBI_TaxID=41;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11182319; DOI=10.1016/s1074-5521(00)00056-9;
RA   Silakowski B., Nordsiek G., Kunze B., Blocker H., Muller R.;
RT   "Novel features in a combined polyketide synthase/non-ribosomal peptide
RT   synthetase: the myxalamid biosynthetic gene cluster of the myxobacterium
RT   Stigmatella aurantiaca Sga15.";
RL   Chem. Biol. 8:59-69(2001).
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; AF319998; AAK57183.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q93TX3; -.
DR   SMR; Q93TX3; -.
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..510
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_0000161035"
FT   MOD_RES         146
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
FT   CROSSLNK        145..147
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
SQ   SEQUENCE   510 AA;  54201 MW;  DE78439DB4FBF3A6 CRC64;
     MSRPRLNIDG DTLKLEEILQ VARHTVTVEL APAAAARVKA ARDLVDRVAA GDTPSYGINT
     GFGTLAEVRI DKKDLRELQR NLILSHAAGV GSPLPLPEAR VLLLLRCNVL AKGYSGIRPE
     TLALALEMLN RDVVPVVPER GSVGASGDLA PLAHLALVFI GEGEAFYKGE RLPAAQALER
     AGLKPVVLEA KEGLALVNGT QAMCAVGTLL QLRAEMLADL ADLAGAMTLE GLLGSHKPFI
     PEIQDVRAHE GQKACAAHLR ELLADSALVE SHVNCSKVQD PYSLRCMPQV HGAAREGLSF
     ARRILEVEIN SATDNPLVFV ETERIVSGGN FHGQPVSLAL DVAAMALTQL SAISERRVEQ
     LVNPALSGLP PFLAKNSGLN SGFMIAQVTS AALVAESRVL SHPASVDSIP SSAGREDHVS
     MGMTAALKGR QVADFTRSCL AIELLVAAQA LDYRQPTRAG KGPQAAYELI RSKIPTMEKD
     RELHRDIAAV SALIDSGELL NAVRTATRGQ