ID   HUTH_HALS3              Reviewed;         525 AA.
AC   B0R544;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Probable 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=OE_2739F;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM774415; CAP13859.1; -; Genomic_DNA.
DR   RefSeq; WP_012289292.1; NC_010364.1.
DR   AlphaFoldDB; B0R544; -.
DR   SMR; B0R544; -.
DR   PRIDE; B0R544; -.
DR   EnsemblBacteria; CAP13859; CAP13859; OE_2739F.
DR   GeneID; 5953911; -.
DR   KEGG; hsl:OE_2739F; -.
DR   HOGENOM; CLU_014801_4_0_2; -.
DR   OMA; CAPQVAG; -.
DR   PhylomeDB; B0R544; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000001321; Chromosome.
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..525
FT                   /note="Probable histidine ammonia-lyase"
FT                   /id="PRO_1000100440"
FT   MOD_RES         146
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
FT   CROSSLNK        145..147
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
SQ   SEQUENCE   525 AA;  54073 MW;  D020924892D9D520 CRC64;
     MTTEGVVIDG ESLTPAAVDA VARHDAPVSI AAGAREAVRE SRARIADVLG GDEAVYGVNT
     GFGSMSDTRI DAADREALQA NLVRSHAAGA GSELDTAAVR ALLVTRLNAL AKGYSGIRER
     VLDVLVGLLN EGVHPVVPSR GSLGASGDLA PLAHMSRVLI GEGQADVAGE RMPAAEALAA
     ADLEPVTLQA KEGLALINGT QLTTGVAALA LVDAERVLRS ADTAGALTTE VTMSTTASCA
     PAIHEVRPHD GQAVSARHIR NLTAGSEVLD HHRDCDRVQD AYSIRCLPQV HGAVRDALDH
     LRAAVATELN SATDNPLVFA GDRVGPRASG TDRAAVVSGG NFHGEVLALR LGYAASALAE
     LAAISERRTD RLLNPETQEP HLEPFLAPDS GLHSGLMIPQ YTAASLVNDL RSLGQPTLDN
     ASVSGAQEDH VSMSAGAAYN FREAVEKAAT VVGVELLCGA QGREFLDPDL ALGAGTAAAY
     DLVREVSEPV AGDRALADDM AAVGDLVRAG LVEDAVARAL DAPLA