ID   HUTH_THEAC              Reviewed;         496 AA.
AC   Q9HLI6;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Probable 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=Ta0242;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
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; AL445063; CAC11387.1; -; Genomic_DNA.
DR   RefSeq; WP_010900671.1; NC_002578.1.
DR   PDB; 7TQR; X-ray; 2.10 A; A=1-496.
DR   PDBsum; 7TQR; -.
DR   AlphaFoldDB; Q9HLI6; -.
DR   SMR; Q9HLI6; -.
DR   STRING; 273075.Ta0242; -.
DR   EnsemblBacteria; CAC11387; CAC11387; CAC11387.
DR   GeneID; 1455875; -.
DR   KEGG; tac:Ta0242; -.
DR   eggNOG; arCOG04671; Archaea.
DR   HOGENOM; CLU_014801_4_0_2; -.
DR   OMA; CAPQVAG; -.
DR   OrthoDB; 30804at2157; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000001024; 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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Histidine metabolism; Lyase; Reference proteome.
FT   CHAIN           1..496
FT                   /note="Probable histidine ammonia-lyase"
FT                   /id="PRO_0000161056"
FT   MOD_RES         142
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
FT   CROSSLNK        141..143
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
SQ   SEQUENCE   496 AA;  54149 MW;  D5F0BF275477CA23 CRC64;
     MIEIDGRSLR VEDVYAVAVE YDRVSISDDT LKAVEEKHEA FLKLINSGKT VYGVNTGFGS
     LLNVHIERDQ EIELQKNLIR SHSSGVGDYL ENRYVRAIMA VRLNSLAAGY SAVSADLLNM
     MVEMLNRDVI PAVPKYGSVG ASGDLAPLAH IGLAMMGEGK AFFEGRLMDS ARALEKAGLK
     PYQFKEKEGV ALINGTSFMS GILSIAVMDA HDILENAIRS ALLSFEALGG TSKAFTPWIL
     GARPHLGQVA IGNRFREYLT GSDIVKRADS VKVQDAYTLR CIPQVYGSVA DVIDYVENVL
     SVEINSATDN PLFNGEEVVS GGNFHGEPVA LAADFLAIAL TDLGNMVERR IARLVDTNLS
     GLPPFLTPDS GLNSGYMIPQ YTAAALCNRN KVLAYPSSAD TIPTSANQED HVSMGATGSL
     KLLEIIDNVR YIIAIEYLLG SQALEFTDKG MSPSTRKIYE KIREKVEKLD HDRPPSFDIE
     TIRKMMDKKE FISALP