ID   HUTH_BRUO2              Reviewed;         511 AA.
AC   A5VVJ6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=BOV_A0872;
OS   Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=444178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25840 / 63/290 / NCTC 10512;
RX   PubMed=19436743; DOI=10.1371/journal.pone.0005519;
RA   Tsolis R.M., Seshadri R., Santos R.L., Sangari F.J., Lobo J.M.,
RA   de Jong M.F., Ren Q., Myers G., Brinkac L.M., Nelson W.C., Deboy R.T.,
RA   Angiuoli S., Khouri H., Dimitrov G., Robinson J.R., Mulligan S.,
RA   Walker R.L., Elzer P.E., Hassan K.A., Paulsen I.T.;
RT   "Genome degradation in Brucella ovis corresponds with narrowing of its host
RT   range and tissue tropism.";
RL   PLoS ONE 4:E5519-E5519(2009).
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; CP000709; ABQ62260.1; -; Genomic_DNA.
DR   RefSeq; WP_006155733.1; NC_009504.1.
DR   AlphaFoldDB; A5VVJ6; -.
DR   SMR; A5VVJ6; -.
DR   EnsemblBacteria; ABQ62260; ABQ62260; BOV_A0872.
DR   GeneID; 45126240; -.
DR   KEGG; bov:BOV_A0872; -.
DR   HOGENOM; CLU_014801_4_0_5; -.
DR   OMA; CAPQVAG; -.
DR   PhylomeDB; A5VVJ6; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000006383; Chromosome II.
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..511
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_1000021546"
FT   MOD_RES         143
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
FT   CROSSLNK        142..144
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
SQ   SEQUENCE   511 AA;  53240 MW;  9732523A3DE54F80 CRC64;
     MTIILKPGSV PLETLKKIYR EGLPVRIDPA FHAGIEKAAA RIAEIAAGDA PVYGINTGFG
     KLASIRIAAG DVATLQRNLI LPHCCGVGEP LSENIVRLIM ALKLVSLGRG ASGVRLEVIT
     LIEAMLEKGV IPMIPEKGSV GASGDLAPLA HMTAAMIGEG EAFYRGERLS GAKALGKAGL
     KPVVLAAKEG LALINGTQTS TALALAGLFR AHRAARTALI TGALSTDAAM GSDAPFHEEI
     HQLRGHKGQI DAGRALRTLL EGSAIRRSHL EGDQRVQDPY CIRCQPQVDG ACLDILRQAA
     RTLEIEANAV TDNPLVLSDG RAVSGGNFHA EPVAFAADQI ALAVCEIGAI SQRRIALLVD
     PSLSFGLPAF LARKPGLNSG LMIAEVTSAA LMSENKQMAH PASVDSTPTS ANQEDHVSMA
     CNGARRLLQM TANLNAIIGI EALTGALGVE LRKPLTTSAE LAKVIAALRA KVATLEEDRY
     MADDLKAAAE LVADGTLSGV ISAGILPDLE A