HUTH_STAAW
ID HUTH_STAAW Reviewed; 504 AA.
AC Q8NYY3;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 100.
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=MW0008;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(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}.
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DR EMBL; BA000033; BAB93873.1; -; Genomic_DNA.
DR RefSeq; WP_000177468.1; NC_003923.1.
DR AlphaFoldDB; Q8NYY3; -.
DR SMR; Q8NYY3; -.
DR EnsemblBacteria; BAB93873; BAB93873; BAB93873.
DR KEGG; sam:MW0008; -.
DR HOGENOM; CLU_014801_4_0_9; -.
DR OMA; CAPQVAG; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000000418; 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_0000161034"
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 504 AA; 56090 MW; 378A3419C5A122FD CRC64;
MTLYLDGETL TIEDIKSFLQ QQSKIEIIDD ALERVKKSRA VVERIIENEE TVYGITTGFG
LFSDVRIDPT QYNELQVNLI RSHACGLGEP FSKEVALVMM ILRLNTLLKG HSGATLELVR
QLQFFINERI IPIIPQQGSL GASGDLAPLS HLALALIGEG KVLYRGEEKD SDDVLRELNR
QPLNLQAKEG LALINGTQAM TAQGVISYIE SEDLGYQSEW IAALTHQSLN GIIDAYRHDV
HAVRNFQEQI 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