ID   HUTH_CERS4              Reviewed;         507 AA.
AC   Q3J289;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=RHOS4_15270;
GN   ORFNames=RSP_2935;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) 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; CP000143; ABA79095.1; -; Genomic_DNA.
DR   RefSeq; WP_011337859.1; NZ_CP030271.1.
DR   RefSeq; YP_352996.1; NC_007493.2.
DR   AlphaFoldDB; Q3J289; -.
DR   SMR; Q3J289; -.
DR   STRING; 272943.RSP_2935; -.
DR   EnsemblBacteria; ABA79095; ABA79095; RSP_2935.
DR   KEGG; rsp:RSP_2935; -.
DR   PATRIC; fig|272943.9.peg.1871; -.
DR   eggNOG; COG2986; Bacteria.
DR   OMA; CAPQVAG; -.
DR   PhylomeDB; Q3J289; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000002703; 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; Reference proteome.
FT   CHAIN           1..507
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_0000336586"
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;  51873 MW;  A52D7AC004846E3B CRC64;
     MEILVPGQAT LAQLEAIWRE GRRARLAPEA RPAVEAAAAR VAEAAAGTAP VYGVNTGFGK
     LASLKIAPAD TAQLQRNLIL SHCCGVGEPM PPSTARLMIA LKLLSLGRGA SGVRWEIVAL
     LEGMLAAGVT PVIPAQGSVG ASGDLAPLAH MAAVMIGEGE AEVGGRRLPG AAALAEAGLA
     PVALGPKEGL ALINGTQFST AYALAGLFEG WRAAQAALVI SALSTDAIMG STAPLRPEIH
     ALRGHAGQIE AAATMRALLE GSAIRESHRE GDQRVQDPYC IRCQPQVTGA AMDVLRMAAG
     TLATEANAAT DNPLVLSDGR IVSGGNFHAE PVGFAADMIA LALSEIGAIA QRRVALMVDP
     TLSFDLPPFL TPEPGLNSGL MIAEVTTAAL MSENKHMAAP TVTDSTPTSA NQEDHVSMAA
     HGARRLGRMV ENLAVILGTE AICAAQGVEF RAPLATSAPL GAVLARLRAE VPRIAADRIL
     APDLAAAARL VRTGALARAA GLPFPAL