ID   HUTH_STAAM              Reviewed;         504 AA.
AC   P64415; Q99XG3;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Histidine ammonia-lyase;
DE            Short=Histidase;
DE            EC=4.3.1.3;
GN   Name=hutH; OrderedLocusNames=SAV0008;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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   -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC       glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB56170.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000017; BAB56170.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000177465.1; NC_002758.2.
DR   AlphaFoldDB; P64415; -.
DR   SMR; P64415; -.
DR   PaxDb; P64415; -.
DR   EnsemblBacteria; BAB56170; BAB56170; SAV0008.
DR   KEGG; sav:SAV0008; -.
DR   HOGENOM; CLU_014801_4_0_9; -.
DR   OMA; CAPQVAG; -.
DR   PhylomeDB; P64415; -.
DR   BioCyc; SAUR158878:SAV_RS00185-MON; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000002481; 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..504
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_0000161030"
FT   MOD_RES         143
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        142..144
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   504 AA;  56090 MW;  FD906A1940472302 CRC64;
     MTLYLDGETL TIEDIKSFLQ QQSKIEIIDD ALERVKKSRA VVERIIENEE TVYGITTGFG
     LFSDVRIDPT QYNELQVNLI RSHACGLGEP FSKEVALVMM ILRLNTLLKG HSGATLELVR
     QLQFFINERI IPIIPQQGSL GASGDLAPLS HLALALIGEG KVLYRGEEKD SDDVLRELNR
     QPLNLQAKEG LALINGTQAM TAQGVISYIE AEDLGYQSEW IAALTHQSLN GIIDAYRHDV
     HSVRNFQEQI NVAARMRDWL EGSTLTTRQA EIRVQDAYTL RCIPQIHGAS FQVFNYVKQQ
     LEFEMNAAND NPLIFEEANE TFVISGGNFH GQPIAFALDH LKLGVSELAN VSERRLERLV
     NPQLNGDLPA FLSPEPGLQS GAMIMQYAAA SLVSENKTLA HPASVDSITS SANQEDHVSM
     GTTAARHGYQ IIENARRVLA IECVIALQAA ELKGVEGLSP KTRRKYEEFR SIVPSITHDR
     QFHKDIEAVA QYLKQSIYQT TACH