ID   HUTH_PSEAB              Reviewed;         509 AA.
AC   Q02ER8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=PA14_67320;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA   Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ14481.1; -; Genomic_DNA.
DR   RefSeq; WP_003095952.1; NZ_CP034244.1.
DR   AlphaFoldDB; Q02ER8; -.
DR   SMR; Q02ER8; -.
DR   PRIDE; Q02ER8; -.
DR   EnsemblBacteria; ABJ14481; ABJ14481; PA14_67320.
DR   KEGG; pau:PA14_67320; -.
DR   HOGENOM; CLU_014801_4_0_6; -.
DR   OMA; CAPQVAG; -.
DR   BioCyc; PAER208963:G1G74-5680-MON; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000000653; 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..509
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_1000021565"
FT   MOD_RES         143
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
FT   CROSSLNK        142..144
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
SQ   SEQUENCE   509 AA;  53766 MW;  3D7BEAE86078C80A CRC64;
     MSLHLKPGQL TLADLRQAYL APVRLSLDPS ADAPVAASVA CVENIIAEGR TAYGINTGFG
     LLASTRISPA DLEKLQRSIV LSHAAGVGEA LDDAMVRLVM LLKVNSLARG FSGIRRKVID
     ALIALINAEV YPHIPLKGSV GASGDLAPLA HMSLVLIGES RARHRGEWLP AAEALAVAGL
     EPLTLAAKEG LALLNGTQVS TAYALRGLFE AEDLFAAATV CGGLSVEAML GSRAPFDARI
     HAARGQRGQI DVAAAYRDLL TASSEVARSH EKCDKVQDPY SLRCQPQVMG ACLTQMRQAA
     EVLEIEANAV SDNPLVFAAE GDVISGGNFH AEPVAMAADN LALALAEIGS LSERRISLMM
     DMHMSQLPPF LVANGGVNSG FMIAQVTAAA LASDNKALAH PASVDSLPTS ANQEDHVSMA
     PNAGKRLWAM AENVRGILAV EWLGACQGLD FREGLKSSPK LEQARRLLRD KVPYYQEDRF
     FAPDIEAASQ LLASGCLNAL LPARLLPSL