ID   HUTH_BURA4              Reviewed;         507 AA.
AC   B1YT80;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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};
GN   OrderedLocusNames=BamMC406_2088;
OS   Burkholderia ambifaria (strain MC40-6).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=398577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC40-6;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Ramette A.,
RA   Konstantinidis K., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia ambifaria MC40-6.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001025; ACB64569.1; -; Genomic_DNA.
DR   RefSeq; WP_012364261.1; NC_010551.1.
DR   AlphaFoldDB; B1YT80; -.
DR   SMR; B1YT80; -.
DR   EnsemblBacteria; ACB64569; ACB64569; BamMC406_2088.
DR   KEGG; bac:BamMC406_2088; -.
DR   HOGENOM; CLU_014801_4_0_4; -.
DR   OMA; CAPQVAG; -.
DR   OrthoDB; 715502at2; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000001680; Chromosome 1.
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..507
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_1000100435"
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   507 AA;  53305 MW;  CED17139C79EF3ED CRC64;
     MITLTPGHLT LPQLRKIARE PVQLTLDPAS FAKIDAGAKA VADIAAKGEP AYGINTGFGR
     LASTHIPHDQ LELLQKNLVL SHAVGVGEPM ARSSVRLLMA LKLSSLGRGH SGIRREVMDA
     LITLFNADVL PLIPVKGSVG ASGDLAPLAH MSAVLLGVGE VFIRGERASA LDGLRVAGLA
     PLTLQAKEGL ALLNGTQAST ALALDNMFSI EDLYRTALVA GALSVDAAAG SVKPFDARIH
     ELRGHRGQIE AAAAYRDLLD GSPINQSHRD CDKVQDPYSL RCQPQVMGAC LDQMRHAADV
     LLIEANAVSD NPLIFPDTGE VLSGGNFHAE PVAFAADNLA LAAAEIGALA ERRIALLIDA
     TLSGLPPFLV KDGGVNSGFM IAHVTAAALA SENKTLAHPA SVDSLPTSAN QEDHVSMATF
     AARKLADIAD NTKYILAIEL LAAAQGVDLR APYHTSPKLA PVMETIRSHV AHYELDHYFA
     PDIAVIAKLV GERAFAKAAP FSFASEQ