HUTH_CHLAA
ID HUTH_CHLAA Reviewed; 523 AA.
AC A9WHT8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=Caur_0974;
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
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; CP000909; ABY34206.1; -; Genomic_DNA.
DR RefSeq; WP_012256862.1; NC_010175.1.
DR RefSeq; YP_001634595.1; NC_010175.1.
DR AlphaFoldDB; A9WHT8; -.
DR SMR; A9WHT8; -.
DR STRING; 324602.Caur_0974; -.
DR EnsemblBacteria; ABY34206; ABY34206; Caur_0974.
DR KEGG; cau:Caur_0974; -.
DR PATRIC; fig|324602.8.peg.1113; -.
DR eggNOG; COG2986; Bacteria.
DR HOGENOM; CLU_014801_4_0_0; -.
DR InParanoid; A9WHT8; -.
DR OMA; CAPQVAG; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000002008; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016841; F:ammonia-lyase activity; IBA:GO_Central.
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; 1.10.275.10; -; 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..523
FT /note="Histidine ammonia-lyase"
FT /id="PRO_1000078225"
FT MOD_RES 149
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
FT CROSSLNK 148..150
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
SQ SEQUENCE 523 AA; 55890 MW; 274A8EA4BC7A94F8 CRC64;
MQIREVILDG ESLTIEQVLA VAYGQPGTPV VRLAPIARQR VERAAQAVQD LLARGVVAYG
ITTGFGAFKD RVIAPDQVER LQYNILVSHA VGVGPVFDIP TTRAIMLIRA NTLARGHSGV
RLQTVERLLD MLNQGIHPRI PCKGSLGASG DLAPLAHMAL PLIGLGEVEW QGEVLPAATA
LERLGWQPLH LAAKEGLALT NGTAVMCALG VIETARAETL SATADIAGCL SLEALYGTPA
AFDARLHALR PFPRQIECAA HLRRLLAGST FVRNNDPRHV QDAYTLRCIP QVHGAVRDAI
AYARWVFAIE LNAVTDNPLL FVDDDGNVEV ISGGNFHGEP LAIALDYLGL AVAELGNIAE
RRLMRLTDEA SNTHVLPAFL TRAGGLNSGF MIVQYTAAAL ATENKVLAHP ASVDSIPTSA
NVEDHVSMGV TAGLKLRSII DNVSQILALE LFAAAQGIDF RRQELGSQAR LGRGTGPVYE
LIRQYVPFIA EDTLLHPYIT IISELVAQGK IAAAAAVHDD ADA