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Database: UniProt
Entry: A8KCI3_9BURK
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ID   A8KCI3_9BURK            Unreviewed;       515 AA.
AC   A8KCI3;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
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   ECO:0000313|EMBL:CAL80815.1};
GN   ORFNames=AAW51_2395 {ECO:0000313|EMBL:AKJ29086.1};
OS   Caldimonas brevitalea.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Caldimonas.
OX   NCBI_TaxID=413882 {ECO:0000313|EMBL:CAL80815.1};
RN   [1] {ECO:0000313|EMBL:CAL80815.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Type strain: K481-B101 {ECO:0000313|EMBL:CAL80815.1};
RX   PubMed=17564599; DOI=10.1111/j.1462-2920.2007.01278.x;
RA   Schellenberg B., Bigler L., Dudler R.;
RT   "Identification of genes involved in the biosynthesis of the cytotoxic
RT   compound glidobactin from a soil bacterium.";
RL   Environ. Microbiol. 9:1640-1650(2007).
RN   [2] {ECO:0000313|EMBL:AKJ29086.1, ECO:0000313|Proteomes:UP000035352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7029 {ECO:0000313|EMBL:AKJ29086.1,
RC   ECO:0000313|Proteomes:UP000035352};
RA   Tang B., Yu Y.;
RL   Submitted (MAY-2015) 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: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}.
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DR   EMBL; CP011371; AKJ29086.1; -; Genomic_DNA.
DR   EMBL; AM412319; CAL80815.1; -; Genomic_DNA.
DR   RefSeq; WP_047194807.1; NZ_CP011371.1.
DR   AlphaFoldDB; A8KCI3; -.
DR   STRING; 413882.AAW51_2395; -.
DR   KEGG; pbh:AAW51_2395; -.
DR   PATRIC; fig|413882.6.peg.2507; -.
DR   OrthoDB; 9806955at2; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000035352; 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; 1.20.200.10; 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:UP000035352}.
FT   MOD_RES         147
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00229"
FT   CROSSLNK        146..148
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00229"
SQ   SEQUENCE   515 AA;  54132 MW;  3C2A370A73B28F45 CRC64;
     MSPSERLTLH PGRLGLLDLR GIAAAFQPIE LDLECRAGIA ASAATVQRIS AGAEPAYGIN
     TGFGKLAKVQ IPHDQLAQLQ ANLVRSHAVG VGPLLDDDTV RLVLALKIAS LARGYSGVRP
     EVIDALVAMF NAQIWPCIPS QGSVGASGDL APLAHLTLPL MGEGEVRVDG RIVPAAQALQ
     RAGLQPVRFA PKEGLALLNG TQVSTGIALM GLLRAEQVFA AAVVAGALSV DAAKGSDAPF
     DDRIQQVRGH RGQIEVAALY RDLLAGSAIR ASHRTGDDRV QDPYSLRCQP QVMGACLELI
     RNAAATLVIE ANAVSDNPLV FADSGEVLSG GNFHAEPVAF AADTLALAIA EVGALSERRI
     ALLIDASLSG LPPFLVQEPG LNSGFMIAHV TAAALASENK TLAHPASVDS LPTSANQEDH
     VSMATFAARK LADMALNVRH IIAIELLAAA QGIDFHRPLR SSQPLEEAHA AIRRRVPHYT
     QDRYFAPDIA AVEQLIDAGS FTPYAGQVLP SWSRS
//
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