ID   HUTH_BRUA2              Reviewed;         511 AA.
AC   Q2YIL6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
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=BAB2_0305;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
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; AM040265; CAJ12471.1; -; Genomic_DNA.
DR   RefSeq; WP_002972121.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YIL6; -.
DR   SMR; Q2YIL6; -.
DR   STRING; 359391.BAB2_0305; -.
DR   EnsemblBacteria; CAJ12471; CAJ12471; BAB2_0305.
DR   GeneID; 3827170; -.
DR   KEGG; bmf:BAB2_0305; -.
DR   PATRIC; fig|359391.11.peg.2259; -.
DR   HOGENOM; CLU_014801_4_0_5; -.
DR   OMA; CAPQVAG; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000002719; 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; Reference proteome.
FT   CHAIN           1..511
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_1000021545"
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;  53254 MW;  8ADEAFB990BB5BEC CRC64;
     MTIILKPGSV PLETLEKIYR EGLPVRIDPA FHAGIEKAAA RIAEIAAGDA PVYGINTGFG
     KLASIRIAAG DVATLQRNLI LSHCCGVGEP 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
     CHGARRLLQM TANLNAIIGI EALTGALGVE LRKPLTTSAE LAKVIAALRA KVATLEEDRY
     MADDLKAAAE LVADGTLSGV ISAGILPDLE A