ID A0A0C9Q8M9_9BACT Unreviewed; 509 AA.
AC A0A0C9Q8M9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Histidine ammonia-lyase {ECO:0000256|ARBA:ARBA00012994, ECO:0000256|HAMAP-Rule:MF_00229};
DE Short=Histidase {ECO:0000256|HAMAP-Rule:MF_00229};
DE EC=4.3.1.3 {ECO:0000256|ARBA:ARBA00012994, ECO:0000256|HAMAP-Rule:MF_00229};
GN Name=hutH {ECO:0000256|HAMAP-Rule:MF_00229};
GN ORFNames=BROSI_A3679 {ECO:0000313|EMBL:GAN35133.1};
OS Candidatus Brocadia sinica JPN1.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Brocadiaceae; Brocadia.
OX NCBI_TaxID=1197129 {ECO:0000313|EMBL:GAN35133.1, ECO:0000313|Proteomes:UP000032309};
RN [1] {ECO:0000313|EMBL:GAN35133.1, ECO:0000313|Proteomes:UP000032309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPN1 {ECO:0000313|EMBL:GAN35133.1,
RC ECO:0000313|Proteomes:UP000032309};
RA Oshiki M., Shinyako-Hata K., Satoh H., Okabe S.;
RT "Draft Genome Sequence of an Anaerobic Ammonium-Oxidizing Bacterium,
RT "Candidatus Brocadia sinica".";
RL Genome Announc. 3:e00267-15(2015).
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:0000256|ARBA:ARBA00000171, ECO:0000256|HAMAP-
CC Rule:MF_00229, ECO:0000256|RuleBase:RU004479};
CC -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3.
CC {ECO:0000256|ARBA:ARBA00005113, ECO:0000256|HAMAP-Rule:MF_00229,
CC ECO:0000256|RuleBase:RU004479}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00229,
CC ECO:0000256|RuleBase:RU004480}.
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:0000256|HAMAP-Rule:MF_00229}.
CC -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000256|HAMAP-
CC Rule:MF_00229, ECO:0000256|RuleBase:RU003954}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAN35133.1}.
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DR EMBL; BAFN01000001; GAN35133.1; -; Genomic_DNA.
DR RefSeq; WP_052565148.1; NZ_BAFN01000001.1.
DR AlphaFoldDB; A0A0C9Q8M9; -.
DR OrthoDB; 9806955at2; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000032309; Unassembled WGS sequence.
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; 1.20.200.10; 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 {ECO:0000256|HAMAP-Rule:MF_00229};
KW Histidine metabolism {ECO:0000256|ARBA:ARBA00022808, ECO:0000256|HAMAP-
KW Rule:MF_00229};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00229};
KW Reference proteome {ECO:0000313|Proteomes:UP000032309}.
FT MOD_RES 144
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00229"
FT CROSSLNK 143..145
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00229"
SQ SEQUENCE 509 AA; 54901 MW; AC87883DAA538CCE CRC64;
MEYIVLNGND LTFDQFMKGV RNGYQVMLSD AAEVRVMKAR ETIQCALNSK RIIYGLTTGF
GALSDVVISK EQTKQLQKNI LMSHAAGVGN FLDEETTKAT LLLKINDFAK GHAGIKPETL
RTLVEMLNKG VYPLMPEKGS VGASGDLAPL AHMALVLVGQ GQALFKGRIF SGKTAMEEAG
IQLVDLDAGE GLALINGTQV MTAIGAITVC DAVNLLKAAD IAAGMSLEVL LASNVELDKK
IHDVRPHPGQ IISADNLRRI IQNSEIVSSH KDCSRVQDAY SIRCSPQVHG ASLNALHYAR
RVLEIEMNAA TDNPLIFSDT DQIISGGNFH GQPVALALDF LAIGLSEIAN ISERRTERLV
NPQLSGLPAF LIKDAGLNSG FMIAQYTAAA LVSENKVLAH PASVDSIPTS ANKEDHVSMG
AIAARKCREV LKNAEQVISI ELLCAAQAMD LFTNLKAGAG TMEAYRLIRK HISHMEQDRI
LSDDINTMYK LIHEGKILNA VESKIGPLN
//
