ID   HUTH_GEOKA              Reviewed;         504 AA.
AC   Q5L310;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=GK0385;
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426;
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(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}.
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DR   EMBL; BA000043; BAD74670.1; -; Genomic_DNA.
DR   RefSeq; WP_011229889.1; NC_006510.1.
DR   AlphaFoldDB; Q5L310; -.
DR   SMR; Q5L310; -.
DR   STRING; 235909.GK0385; -.
DR   PRIDE; Q5L310; -.
DR   EnsemblBacteria; BAD74670; BAD74670; GK0385.
DR   KEGG; gka:GK0385; -.
DR   eggNOG; COG2986; Bacteria.
DR   HOGENOM; CLU_014801_4_0_9; -.
DR   OMA; CAPQVAG; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000001172; 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..504
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_0000161006"
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   504 AA;  54670 MW;  D68B92DB2D4CD94A CRC64;
     MIVLTGHTLT IDEVRRVVYE RERVAADEES MRAVEKSRAA VEQAISNGRT IYGVNTGFGK
     LADVRIEGSD LEQLQINLLR SHACAVGEPF AEDVVRAMLL LRANALLKGY SGVRPAVIEQ
     LLAFLNTGIH PIVPQQGSLG ASGDLAPLAH LALAFAGEGE AMYQGRRMPA AQALSQAGIS
     PLSLQEKEGL ALINGTQVMT AVGALAYLEA EQLAYDSEWI AALTIEALYG IVDAFDARIH
     AARGFQEQVE VAERLRRYLA GSQLTTRQGE RRVQDAYSIR CLPQVHGASL RALRYVKETL
     EIEMNAATDN PLIFADGTAL SGGNFHGQPV AIAMDLLKIA VAELANISER RIERLVNPQL
     SEGLPPFLSP QPGLQSGAMI MQYVAASLVS ENKTLAHPAS VDSIPSSANQ EDHVSMGTTA
     ARHAYMIVQN ARKVLAIELI CALQAVEARG IERMAPSTRQ FYHKARRIVS SITADRVFSD
     DIEAVAAWLS ERANHHFLRD EAKA