ID HUTH_STAA8 Reviewed; 504 AA.
AC Q2G2P7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 98.
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};
GN OrderedLocusNames=SAOUHSC_00008;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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; CP000253; ABD29199.1; -; Genomic_DNA.
DR RefSeq; WP_000177464.1; NZ_LS483365.1.
DR RefSeq; YP_498616.1; NC_007795.1.
DR AlphaFoldDB; Q2G2P7; -.
DR SMR; Q2G2P7; -.
DR STRING; 93061.SAOUHSC_00008; -.
DR PaxDb; 1280-SAXN108_0010; -.
DR GeneID; 3919181; -.
DR KEGG; sao:SAOUHSC_00008; -.
DR PATRIC; fig|93061.5.peg.8; -.
DR eggNOG; COG2986; Bacteria.
DR HOGENOM; CLU_014801_4_0_9; -.
DR OrthoDB; 9806955at2; -.
DR UniPathway; UPA00379; UER00549.
DR PRO; PR:Q2G2P7; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004397; F:histidine ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0006548; P:histidine catabolic process; IBA:GO_Central.
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; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 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 NCBIfam; TIGR01225; hutH; 1.
DR PANTHER; PTHR10362; HISTIDINE AMMONIA-LYASE; 1.
DR PANTHER; PTHR10362:SF7; HISTIDINE AMMONIA-LYASE; 1.
DR Pfam; PF00221; Lyase_aromatic; 1.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00488; PAL_HISTIDASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Histidine metabolism; Lyase; Reference proteome.
FT CHAIN 1..504
FT /note="Histidine ammonia-lyase"
FT /id="PRO_1000021570"
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; 56076 MW; 4A906763DA51275D 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
HAVRNFQEQI NVAARMRDWL EGSTLTTRQS EIRVQDAYTL RCIPQIHGAS FQVFNYVKQQ
LEFEMNAAND NPLIFEEANE TFVISGGNFH GQPIAFALDH LKLGVSELAN VSERRLERLV
NPQLNGDLPA FLSPEPGLQS GAMIMQYAAA SLVSENKTLA HPASVDSITS SANQEDHVSM
GTTAARHGYQ IIENARRVLA IECVIALQAA ELKGVEGLSP KTRRKYDEFR SIVPSITHDR
QFHKDIEAVA QYLKQSIYQT TACH
//
