HUTH_BACC2
ID HUTH_BACC2 Reviewed; 505 AA.
AC B7ISJ2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=BCG9842_B1556;
OS Bacillus cereus (strain G9842).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405531;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G9842;
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus G9842.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001186; ACK93309.1; -; Genomic_DNA.
DR RefSeq; WP_000631844.1; NC_011772.1.
DR AlphaFoldDB; B7ISJ2; -.
DR SMR; B7ISJ2; -.
DR EnsemblBacteria; ACK93309; ACK93309; BCG9842_B1556.
DR KEGG; bcg:BCG9842_B1556; -.
DR HOGENOM; CLU_014801_4_0_9; -.
DR OMA; CAPQVAG; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000006744; 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..505
FT /note="Histidine ammonia-lyase"
FT /id="PRO_1000190490"
FT MOD_RES 142
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
FT CROSSLNK 141..143
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
SQ SEQUENCE 505 AA; 55327 MW; D673B984D586B629 CRC64;
MITLTGHTLT IEEMKRLLLE GEGVTACPTS MQKVAECREV VEKIVEDGKV VYGITTGFGK
FSDVLIQKDD VKALQHNLIQ SHACGIGDPF PEEVSRGMLI LRANTMLKGV SGVRPLVVNM
LLEFVNRKIH PVVPQQGSLG ASGDLAPLSH LALVLLGEGE VFYKGKRVHA MVALTEEGLE
PIELEAKEGL ALINGTQAMT AQGVLSYIEA EATAYQAELI ASMTIEGLQG IIDAFDENVH
KARGYKEQVD VASRIRDILH DSKLTTKQGE LRVQDAYSLR CIPQVHGASW QVLNYVKEKL
EIEMNAATDN PLIFDGGEKV ISGGNFHGQP IAFAMDFLKV GMAELANISE RRIERLVNPQ
LNDLPPFLSP EPGLQSGAMI MQYAAASLVS ENKTLAHPAS VDSIPSSANQ EDHVSMGTIA
SRHAHQIIQN ARRVLSIEMI CAMQAAEYRG IENMSTVTKS FYHQGRQQVP SITNDRIFST
DIENIAHWLK TNYSIKERLD VNAAL
