ID   HUTH_RALSO              Reviewed;         515 AA.
AC   Q8XW29;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2002, sequence version 2.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Histidine ammonia-lyase;
DE            Short=Histidase;
DE            EC=4.3.1.3;
GN   Name=hutH; OrderedLocusNames=RSc2646; ORFNames=RS04570;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
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   -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC       glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD16353.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL646052; CAD16353.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q8XW29; -.
DR   SMR; Q8XW29; -.
DR   STRING; 267608.RSc2646; -.
DR   EnsemblBacteria; CAD16353; CAD16353; RSc2646.
DR   KEGG; rso:RSc2646; -.
DR   PATRIC; fig|267608.8.peg.2687; -.
DR   eggNOG; COG2986; Bacteria.
DR   HOGENOM; CLU_014801_4_0_4; -.
DR   OMA; CAPQVAG; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000001436; 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; Reference proteome.
FT   CHAIN           1..515
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_0000161020"
FT   MOD_RES         147
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        146..148
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   515 AA;  53246 MW;  2E14832086A477E3 CRC64;
     MTTPSILTLH PGEMTFADLR RVWLAPTPVT LSGDCAAAIE ASAATVQAIV ARGEPAYGIN
     TGFGKLARTQ IATHELEHLQ RNLILSHAVG TGQDLDDNVA RLVLLMKAAS LARGYSGVRR
     VVIDTLLAML NAGIVPCIPS KGSVGASGDL APLAHMTLAM LGEGDARVNG VRKPAREALA
     AAGIAPIALA AKEGLALING TQVSTALALN GLFLAERLLQ AATVAGALSV DAAKGSDAPF
     DPRVHTVRGQ AGQIATAAVY RGLLAGSAIR RSHLVGDTRV QDPYSLRCQP QVMGACLDLI
     RQAGATLLTE ANAVTDNPLV YADAGEVISG GNFHAEPVAF AADMLALAIA EIGALSERRI
     ALLIDSTLSG LPPFLVEQPG LNSGFMIAHV TAAALASENK SLAHPASVDS LPTSANQEDH
     VSMATFAGRR LAEMAGNTAT IVGIEALAAA QGIDFHRPLA TSDALARAHT CIRSRVAYYG
     EDRLFAPDIE AARRLVLDGD LGDSCRAHLA DLALA