ID   HUTH_GLOVI              Reviewed;         514 AA.
AC   Q7NCB3;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=glr3066;
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(2003).
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; BA000045; BAC91007.1; -; Genomic_DNA.
DR   RefSeq; NP_926012.1; NC_005125.1.
DR   RefSeq; WP_011143059.1; NC_005125.1.
DR   AlphaFoldDB; Q7NCB3; -.
DR   SMR; Q7NCB3; -.
DR   STRING; 251221.35213636; -.
DR   PRIDE; Q7NCB3; -.
DR   EnsemblBacteria; BAC91007; BAC91007; BAC91007.
DR   KEGG; gvi:glr3066; -.
DR   PATRIC; fig|251221.4.peg.3096; -.
DR   eggNOG; COG2986; Bacteria.
DR   HOGENOM; CLU_014801_4_0_3; -.
DR   InParanoid; Q7NCB3; -.
DR   OMA; CAPQVAG; -.
DR   OrthoDB; 715502at2; -.
DR   PhylomeDB; Q7NCB3; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000000557; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016841; F:ammonia-lyase activity; IBA:GO_Central.
DR   GO; GO:0004397; F:histidine ammonia-lyase activity; IBA:GO_Central.
DR   GO; GO:0006548; P:histidine catabolic process; IBA:GO_Central.
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..514
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_0000161007"
FT   MOD_RES         148
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
FT   CROSSLNK        147..149
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
SQ   SEQUENCE   514 AA;  54037 MW;  15CC63A8ED444DA4 CRC64;
     MKLLTDWLVL DGCSLAVDDL VAVARGGVPV RLSPASLELV RRSRAFVEAL LEGDEIVYGI
     TTGFGYFKNR RIPRSAVEQL QQNLLMSSAA GLGEPFGREV VRAMLLLRAN TLAQGYSGVR
     PETLQLLVAM LNRGVHPVVP CRGSVGASGD LAPLAHLALV LTGEGEAEVG GEVLPGAAAL
     ARAGLEPIRL GAKEGLALIN GTQAMSALGA LTVHRAQRLA KLADLACAMT LEATLGSRSA
     FLPHFHRLRP HPGQQSSARN LLVLTEDSAL IASHAGCDRV QDAYSLRCAP QVHGASLDAI
     SYAAGVIAIE INSVTDNPLI FADTGQVVTG GHFHGQPVAM ASDVLAIALA ELADISERRT
     ERLVNADYSN GLPMFLTEAG GLHSGYMVAQ YTAASLVSEN KVLAHPACVD SIPTSAGQED
     HVSMGLTAAR KAVTVCDNCE RVIAIELMCA AQALDLRGKL TPGRGSRVGL EVIRAAVPHL
     ESDRIVSRDI EKVVELMADG HLLEAVEAAC GRLD