ID   HUTH_SHEON              Reviewed;         513 AA.
AC   Q8EKJ4;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=SO_0098;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(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         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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014299; AAN53185.1; -; Genomic_DNA.
DR   RefSeq; NP_715740.1; NC_004347.2.
DR   RefSeq; WP_011070508.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EKJ4; -.
DR   SMR; Q8EKJ4; -.
DR   STRING; 211586.SO_0098; -.
DR   PaxDb; Q8EKJ4; -.
DR   KEGG; son:SO_0098; -.
DR   PATRIC; fig|211586.12.peg.98; -.
DR   eggNOG; COG2986; Bacteria.
DR   HOGENOM; CLU_014801_4_0_6; -.
DR   OMA; CAPQVAG; -.
DR   OrthoDB; 715502at2; -.
DR   PhylomeDB; Q8EKJ4; -.
DR   BioCyc; SONE211586:G1GMP-96-MON; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016841; F:ammonia-lyase activity; IBA:GO_Central.
DR   GO; GO:0004397; F:histidine ammonia-lyase activity; IBA:GO_Central.
DR   GO; GO:0006548; P:histidine catabolic process; IBA:GO_Central.
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..513
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_0000161027"
FT   MOD_RES         147
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
FT   CROSSLNK        146..148
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
SQ   SEQUENCE   513 AA;  54431 MW;  29869D7886AA6802 CRC64;
     MKSVNHLVLT PGSLSLAQLR EISRHKLTLE LAPEAINDIN ISAQIVQKVL DEGRTVYGIN
     TGFGLLANTK IAPEDLQLLQ RSIVLSHAAG TGQYMQDATV RLMMVLKINS LSRGFSGIRL
     EVINFLISLV NAEVYPCVPE KGSVGASGDL APLAHMCLPL LGEGEMSYQG QIISAAEGLE
     IAGLKPIDLA AKEGLALLNG TQASTALALE GLFHAEDLFA ASSVIGAMSV EAAMGSRSPF
     DPRIHAARGQ KGQIDSAMVF RYLLGEESEI SLSHANCEKV QDPYSLRCQP QVLGACLTQI
     RQAAEVLATE ANGVTDNPLV FQDTGDIISG GNFHAEPVAM AADNLAIAIA ELGAIAERRI
     ALLIDSSLSK LPPFLVKNGG VNSGFMIAQV TAAALASENK TYAHPASVDS LPTSANQEDH
     VSMATFAARR LRDMSENTRG VLAIELLAAA QGLDFRAPLT PSKAVAQAKA ELREVVAYYD
     KDRYFAPDIE AATDLLYTAS FNAYLPLGVL PSL