ID   HUTH_PSEFS              Reviewed;         512 AA.
AC   Q8VMR3; C3K809;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   25-MAY-2022, entry version 122.
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}; Synonyms=hutH-1;
GN   OrderedLocusNames=PFLU_0367;
OS   Pseudomonas fluorescens (strain SBW25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=216595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Zhang X.X.;
RT   "Using RIVET to study histidine availability in planta for plant growth-
RT   promoting Pseudomonas fluorescens SBW25.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SBW25;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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; AJ421809; CAD19072.1; -; Genomic_DNA.
DR   EMBL; AM181176; CAY46644.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8VMR3; -.
DR   SMR; Q8VMR3; -.
DR   STRING; 294.SRM1_00418; -.
DR   PRIDE; Q8VMR3; -.
DR   EnsemblBacteria; CAY46644; CAY46644; PFLU_0367.
DR   KEGG; pfs:PFLU_0367; -.
DR   eggNOG; COG2986; Bacteria.
DR   HOGENOM; CLU_014801_4_0_6; -.
DR   OMA; CAPQVAG; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000002332; 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..512
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_0000161016"
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"
FT   CONFLICT        512
FT                   /note="L -> LQPQL (in Ref. 1; CAD19072)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   512 AA;  54243 MW;  CA2098A2E8313361 CRC64;
     MNVTALNLIP GQLSLAQLRA IYQQPVTLRL DDSATAQIEA SVACVEQILA ENRTAYGINT
     GFGLLASTRI ASEDLENLQR SLVLSHAAGV GEPISDALVR LVMVLKVNSL SRGFSGIRRQ
     VIDALIALIN AEVYPHIPLK GSVGASGDLA PLAHMSLVLL GEGKARYKGE WLEATEALKV
     AGLTPLTLAA KEGLALLNGT QVSTAYALRG LFEGEDLFAG ALACGGLTVE AVLGSRSPFD
     ARIHAARGQR GQIDSAAAYR DLLGESSQVS QSHQNCDKVQ DPYSLRCQPQ VMGACLTQFR
     QAAEVLVVEA NAVSDNPLVF AAEGDVISGG NFHAEPVAMA ADNMALAIAE IGSLSERRIS
     LMMDKHMSQL PPFLVGNGGV NSGFMIAQVT AAALASENKA LAHPHSVDSL PTSANQEDHV
     SMAPAAGKRL WEMAENTRGI LAVEWLAACQ GLDLREGLKT SPKLEKARGI LRDKVAFYDK
     DRFFAPDINA ASELLATRCL NELVPANLLP SL