ID   HUTH_BURMA              Reviewed;         507 AA.
AC   Q62LJ6;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   25-MAY-2022, entry version 96.
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=BMA0645;
OS   Burkholderia mallei (strain ATCC 23344).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=243160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23344;
RX   PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA   Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA   Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA   Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA   Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA   Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA   Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT   "Structural flexibility in the Burkholderia mallei genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAU49673.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000010; AAU49673.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004192520.1; NC_006348.1.
DR   RefSeq; YP_102423.1; NC_006348.1.
DR   AlphaFoldDB; Q62LJ6; -.
DR   SMR; Q62LJ6; -.
DR   STRING; 243160.BMA0645; -.
DR   EnsemblBacteria; AAU49673; AAU49673; BMA0645.
DR   GeneID; 56596250; -.
DR   KEGG; bma:BMA0645; -.
DR   PATRIC; fig|243160.12.peg.666; -.
DR   eggNOG; COG2986; Bacteria.
DR   HOGENOM; CLU_014801_4_0_4; -.
DR   OMA; CAPQVAG; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000006693; 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_0000160997"
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;  53141 MW;  77B4E49060B6D4AE CRC64;
     MITLTPGRLT LPQLRRIARE NVQIALDPAS FAAIDRGAQA VADIAAKGEP AYGINTGFGR
     LASTHIPHDQ LELLQKNLVL SHAVGVGEPM ARPVVRLLMA LKLSSLGRGH SGIRRVVMDA
     LVTLFNADVL PLIPVKGSVG ASGDLAPLAH MSAVLLGIGD VFIRGERASA AEGLRVAGLA
     PLTLEAKEGL ALLNGTQAST ALALDNLFAI EDLYRTALVS GALSVDAAAG SVKPFDARIH
     ELRGHRGQID AAAAYRSLLD GSAINVSHRD CDKVQDPYSL RCQPQVMGAC LDQIRHAAGV
     LLIEANAVSD NPLIFPDTGE VLSGGNFHAE PVAFAADNLA IAAAEIGALA ERRIALLIDA
     TLSGLPPFLV KDGGVNSGFM IAHVTAAALA SENKTLAHPA SVDSLPTSAN QEDHVSMATF
     AARKLTDIAE NVANILAIEL LAAAQGVDLR APHATSPALQ HAMKTIRADV AHYDLDHYFA
     PDIAVVARRV RERAFATLSP LSFESEQ