HUTH_BACAC
ID HUTH_BACAC Reviewed; 505 AA.
AC C3L982;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 61.
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=BAMEG_0922;
OS Bacillus anthracis (strain CDC 684 / NRRL 3495).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=568206;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 684 / NRRL 3495;
RA Dodson R.J., Munk A.C., Brettin T., Bruce D., Detter C., Tapia R., Han C.,
RA Sutton G., Sims D.;
RT "Genome sequence of Bacillus anthracis str. CDC 684.";
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; CP001215; ACP12403.1; -; Genomic_DNA.
DR RefSeq; WP_000631851.1; NC_012581.1.
DR AlphaFoldDB; C3L982; -.
DR SMR; C3L982; -.
DR GeneID; 45023433; -.
DR KEGG; bah:BAMEG_0922; -.
DR HOGENOM; CLU_014801_4_0_9; -.
DR OMA; CAPQVAG; -.
DR UniPathway; UPA00379; UER00549.
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_1000125088"
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; 55413 MW; F1B785A7614FD922 CRC64;
MITLTGHTLT IEEMKRLLLE GEGVTACPTS MQKVAECREV VEKIVENGKV VYGITTGFGK
FSDVLIQKDD VKALQHNLIQ SHACGIGDPF PEEVSRGMLI LRANTMLKGV SGVRPLVVNM
LLEFVNRKIH PVVPQQGSLG ASGDLAPLSH LALILLGEGE VFYKGKRVHA MVALTEEGLE
PIELEAKEGL ALINGTQAMT AQGVLSYIEA EATAYQAELI ASMTIEGLQG IIDAFDENVH
KARGYKEQVE VASRIRDILH DSKLTTKQGE LRVQDAYSLR CIPQVHGASW QVLNYVKEKL
EIEMNAATDN PLIFDGGEKV ISGGNFHGQP IAFAMDFLKV GMAELANISE RRIERLVNPQ
LNDLPPFLSP EPGLQSGAMI MQYAAASLVS ENKTLAHPAS VDSIPSSANQ EDHVSMGTIA
SRHAHQIIQN VRRVLSIEMI CAMQAAEYRG IENMSTVTKS FYHQGRQQVP SITNDRIFST
DIENITHWLK TNYSIKERLD VNAAL
