ID   HUTH_BACVZ              Reviewed;         512 AA.
AC   A7ZAE4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 88.
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=RBAM_036410;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
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   -!- SEQUENCE CAUTION:
CC       Sequence=ABS75970.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000560; ABS75970.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041482230.1; NC_009725.2.
DR   AlphaFoldDB; A7ZAE4; -.
DR   SMR; A7ZAE4; -.
DR   STRING; 326423.RBAM_036410; -.
DR   EnsemblBacteria; ABS75970; ABS75970; RBAM_036410.
DR   KEGG; bay:RBAM_036410; -.
DR   HOGENOM; CLU_014801_4_0_9; -.
DR   OMA; CAPQVAG; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000001120; 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..512
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_0000336583"
FT   MOD_RES         142
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
FT   CROSSLNK        141..143
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
SQ   SEQUENCE   512 AA;  56317 MW;  365FAB2EADA7E8D3 CRC64;
     MVTLDGSSLT TADAQRVLFD FEEVQASAES MERVKKSRAA VERIVQEEKT IYGITTGFGK
     FSDVLIQKED AADLQLNLIL SHACGVGDPF PESVSRAMLL LRANALLKGF SGVRTELIDQ
     LLAYLNHRIH PVIPQQGSLG ASGDLAPLSH LALALIGQGE VFYEGARMPT AHALEQTNLQ
     PAVLTSKEGL ALINGTQAMT AMGLIAYLEA EKLAYQSERI ASLTIEGLQG IIDAFDEDIH
     AARGYQEQMD VAERIRYYLS DSKLTTVQGE LRVQDAYSIR CIPQVHGASW QTLAYVKEKL
     EIEMNAATDN PLIFEDGAKI ISGGNFHGQP IAFAMDFLKV AAAELANISE RRIERLVNPQ
     LNDLPPFLSP QPGLQSGAMI MQYAAASLVS ENKTLAHPAS VDSIPSSANQ EDHVSMGTIA
     SRHAYQIIAN TRRVLAVEAI CALQAVEYRG EEHCASYTKQ LYHEMRNIVP SIQEDRVFSY
     DIEHLSDWLK KESFLPNEHH QKLMTNEGGL TR