ID   HUTH_PSESM              Reviewed;         515 AA.
AC   Q87UM1;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 106.
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=PSPTO_5275;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA   Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA   Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA   Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA   Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA   Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA   Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(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; AE016853; AAO58701.1; -; Genomic_DNA.
DR   RefSeq; NP_795006.1; NC_004578.1.
DR   RefSeq; WP_011105400.1; NC_004578.1.
DR   AlphaFoldDB; Q87UM1; -.
DR   SMR; Q87UM1; -.
DR   STRING; 223283.PSPTO_5275; -.
DR   EnsemblBacteria; AAO58701; AAO58701; PSPTO_5275.
DR   GeneID; 1186960; -.
DR   KEGG; pst:PSPTO_5275; -.
DR   PATRIC; fig|223283.9.peg.5399; -.
DR   eggNOG; COG2986; Bacteria.
DR   HOGENOM; CLU_014801_4_0_6; -.
DR   OMA; CAPQVAG; -.
DR   OrthoDB; 715502at2; -.
DR   PhylomeDB; Q87UM1; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000002515; 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_0000161019"
FT   MOD_RES         149
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
FT   CROSSLNK        148..150
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
SQ   SEQUENCE   515 AA;  54633 MW;  6D7AAC06413BDC9A CRC64;
     MTTLSAKTLN LIPGQLTLAQ LRAIHQQPVS LTLDSSANQQ IDDSVACVER ILAENRTAYG
     INTGFGLLAS TRIASEDLEN LQRSLVLSHA AGVGQPISDD LVRLIMVLKV NSLSRGFSGI
     RRVVIDALIA LINAEVYPHI PLKGSVGASG DLAPLAHMSL VLLGEGKARH KGEWLNAVDA
     LAVAGLKPLT LAAKEGLALL NGTQVSTAYA LRGLFEGEDL FAAALTCGSL TVEAVLGSRS
     PFDARIHAAR GQRGQIDAAA CYRELLGESS GVSESHRNCD KVQDPYSLRC QPQVMGACLT
     QLRQAAEVLE VESNAVSDNP LVFAAENDVI SGGNFHAEPV AMAADNLALA IAEIGSLSER
     RISLMMDKHM SQLPPFLVAN GGVNSGFMIA QVTAAALASE NKALAHPHSV DSLPTSANQE
     DHVSMAPAAG KRLWEMAENV RGILAVEWLA ACQGLDLREG LKTSAKLEQA RSLLRSKVPF
     YEKDRFFAPD IEAASQLLSS TCLNPLVPAR LLPSL