ID   HUTH_MARMM              Reviewed;         507 AA.
AC   Q0AP92;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=Mmar10_1603;
OS   Maricaulis maris (strain MCS10).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Maricaulales; Maricaulaceae;
OC   Maricaulis.
OX   NCBI_TaxID=394221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS10;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P.,
RA   Stephens C., Richardson P.;
RT   "Complete sequence of Maricaulis maris MCS10.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000449; ABI65895.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0AP92; -.
DR   SMR; Q0AP92; -.
DR   STRING; 394221.Mmar10_1603; -.
DR   EnsemblBacteria; ABI65895; ABI65895; Mmar10_1603.
DR   KEGG; mmr:Mmar10_1603; -.
DR   eggNOG; COG2986; Bacteria.
DR   HOGENOM; CLU_014801_4_0_5; -.
DR   OMA; CAPQVAG; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000001964; 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..507
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_0000336585"
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   507 AA;  52202 MW;  BB3F77F890CA662E CRC64;
     MTTVTIKPGA MVLADWADIW RGATIRIDPE AKAGVDAAAA TVDRLIASGE AVYGLNTGFG
     KLAQTRIADD ELATLQERLV LSHAAGIGEA LDSRIVRLVM ALKLASLGRG ASGVRWTTIA
     AMQALLDADV LPVIPSQGSV GASGDLAPLA HMSAALIGAG EATWQGQRMP ASDALAKAGL
     KPVQLGPKEG LALLNGTQTS TALALAGLFE VEAGFQAALV SGALSVDAAK GSVAPFDPRI
     HSLRGHPGQI DVAAALRGLL DGSGILSSHE GCEKIQDPYC LRCQPQVMGA VLDLLRQAGA
     VLEREANAVT DNPLIFTDTD EAISGGNFHA EPVAFAADQI AMAACEIGSI CERRIALLTD
     PAVSGLPAFL TPNPGINSGF MIAHVTAAAL VSENKQKAYP ASVDSIPTSA NQEDHVSMAT
     HGAFRLLKMA ENLHVVVGIE LLCGAQGTDF HAGLTSSPTL ETAKATLRKQ VPAYGDDRYF
     ATDIANARDL VTGRGLVADA GTLPGIA