ID   HUTH_GLUOX              Reviewed;         515 AA.
AC   Q5FRR8;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=GOX1167;
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H;
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
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; CP000009; AAW60928.1; -; Genomic_DNA.
DR   RefSeq; WP_011252720.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FRR8; -.
DR   SMR; Q5FRR8; -.
DR   STRING; 290633.GOX1167; -.
DR   EnsemblBacteria; AAW60928; AAW60928; GOX1167.
DR   KEGG; gox:GOX1167; -.
DR   eggNOG; COG2986; Bacteria.
DR   HOGENOM; CLU_014801_4_0_5; -.
DR   OMA; CAPQVAG; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000006375; 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_0000161008"
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"
SQ   SEQUENCE   515 AA;  54544 MW;  4C90754A0E81D485 CRC64;
     MTTSIFTLTP GKITLSDLRD FYFGQMDVRL DDGTFEALQR AAESVERIVG RGEPVYGVNT
     GFGKLAKTRI PDDRLRDLQR NLVLSHAAGI GQPMPERVVR LILLLKANGL ARGYSGVRPQ
     IVQLLLDMLN QGVVPVIPEK GSVGASGDLA PLAHMSAVVI GEGEAFYQGK RLKGDEALKA
     AGLEPLVLGA KEGLALLNGT QASTALAIAA LLDAERLFHA ALITGGLTLD AARGTDAPFD
     PRLHELRGQK GQIECAAVYR ALMQGSAIRA SHLEDDERVQ DPYCLRCQPQ VMGACLDNLR
     QAARVLVIEA NAVSDNPIHF PDTDEMISGG NFHAEPVAIA ADLMAIAVSE VGAIAERRLA
     LLVDAQMSGL PPFLVQDSGL NSGFMIAQVT AAALASENKT LAHPASVDSL PTSANQEDHV
     SMATFAARRV GDIVDNVRTI IAVEYLAAVQ GLDFLAPLET SAPLLEVAKT LRKTVPFFAQ
     DRLFTPDMEA ARALIIDGAL GSCVGSGVAL PALEG