ID   HUTH_CAUVN              Reviewed;         513 AA.
AC   B8H2S1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=CCNA_01010;
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(2010).
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; CP001340; ACL94475.1; -; Genomic_DNA.
DR   RefSeq; WP_012640105.1; NC_011916.1.
DR   RefSeq; YP_002516383.1; NC_011916.1.
DR   AlphaFoldDB; B8H2S1; -.
DR   SMR; B8H2S1; -.
DR   PRIDE; B8H2S1; -.
DR   EnsemblBacteria; ACL94475; ACL94475; CCNA_01010.
DR   GeneID; 7329758; -.
DR   KEGG; ccs:CCNA_01010; -.
DR   PATRIC; fig|565050.3.peg.992; -.
DR   HOGENOM; CLU_014801_4_0_5; -.
DR   OMA; CAPQVAG; -.
DR   OrthoDB; 715502at2; -.
DR   PhylomeDB; B8H2S1; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000001364; 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..513
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_1000125092"
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;  53412 MW;  368ED01EC8DC2E71 CRC64;
     MERPVTELVL NPGAVPLAEW KAIYRGASAR LAESAWPVIA ESAAAVQRIL AKGEPVYGIN
     TGFGKLASVR IGDADLETLQ RNIVLSHAAG VGEPSPVPVI RLMMALKLAS LAQGASGVRV
     ETVRMLEEML VEGLTPVVPC QGSVGASGDL APLSHMAATM IGVGEIFVGG QRLPAAQALA
     QAGLEPLTLG PKEGLALLNG TQFSTANALA GLFEAERLFQ SALVTGALST EAAKGSDTPF
     DPRIHTLRRH VGQIETAAAL RALMSASEIR ASHLKEDERV QDPYCLRCQP QVMGAALDIL
     RQAATTLATE ANCVSDNPLI FPEADEALSG GNFHAEPVAF AADMIALAVC EIGSIAERRI
     AMLVDPALSG LPAFLTPKPG LNSGFMIPQV TAAALVSENK QRAYPASVDS IPTSANQEDH
     VSMAAHGARR LLAMVENADA VLGIELLAAA QGCDFHAPLR SSAALEAVRA LTRSKVPHLS
     DDRHFHPDME AANTLVRSGA VIAAVGALPG VTA