ID   W7IKQ3_9PSEU            Unreviewed;       512 AA.
AC   W7IKQ3;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Histidine ammonia-lyase {ECO:0000256|ARBA:ARBA00012994, ECO:0000256|RuleBase:RU004479};
DE            EC=4.3.1.3 {ECO:0000256|ARBA:ARBA00012994, ECO:0000256|RuleBase:RU004479};
GN   ORFNames=UO65_3188 {ECO:0000313|EMBL:EWC61450.1};
OS   Actinokineospora spheciospongiae.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinokineospora.
OX   NCBI_TaxID=909613 {ECO:0000313|EMBL:EWC61450.1, ECO:0000313|Proteomes:UP000019277};
RN   [1] {ECO:0000313|EMBL:EWC61450.1, ECO:0000313|Proteomes:UP000019277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EG49 {ECO:0000313|EMBL:EWC61450.1,
RC   ECO:0000313|Proteomes:UP000019277};
RX   PubMed=24604655;
RA   Harjes J., Ryu T., Abdelmohsen U.R., Moitinho-Silva L., Horn H., Ravasi T.,
RA   Hentschel U.;
RT   "Draft Genome Sequence of the Antitrypanosomally Active Sponge-Associated
RT   Bacterium Actinokineospora sp. Strain EG49.";
RL   Genome Announc. 2:e00160-14(2014).
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,
CC         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|RuleBase:RU004479}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004480}.
CC   -!- SIMILARITY: Belongs to the PAL/histidase family.
CC       {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:EWC61450.1}.
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DR   EMBL; AYXG01000109; EWC61450.1; -; Genomic_DNA.
DR   RefSeq; WP_035283193.1; NZ_AYXG01000109.1.
DR   AlphaFoldDB; W7IKQ3; -.
DR   STRING; 909613.UO65_3188; -.
DR   PATRIC; fig|909613.9.peg.3190; -.
DR   eggNOG; COG2986; Bacteria.
DR   OrthoDB; 9806955at2; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000019277; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004397; F:histidine ammonia-lyase activity; IEA:UniProtKB-EC.
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   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   Histidine metabolism {ECO:0000256|ARBA:ARBA00022808,
KW   ECO:0000256|RuleBase:RU004479};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003954};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019277}.
SQ   SEQUENCE   512 AA;  52615 MW;  C2CABCADD0CF49B7 CRC64;
     MERVVLDGGP LSRDEVVAVA RGLAGVEVAA PALAGVTATR AHVELLAEAT TPTYGVSTGF
     GALATRHIPL DRRAALQRSL IRSHAAGAGP EVEPEVVRAL MLLRLRTLTT GRTGVHPSTV
     NALAALLDRG IVPVVHEFGS LGCSGDLAPL SAVALALMGE GMVRDPAGEL RPAADALAEA
     GLEPVVLAEK EGLALINGTD GMLGMLALAA ADLRLLLDTA DLTAAMSVEA LLGTDRVFAA
     DLQALRPHPG QAESAARIAA FLAGSPIVAS HRGPDCTRVQ DAYSLRCAPQ VHGAARDTVA
     HAETVADREL AAAIDNPVVL ADGRVESNGN FHGAPLAYVL DFLAIPVADV ASMAERRTDR
     MLDPARSHGL PPFLAADPGV DSGHMIAQYT QAAVVAELKR LAVPASVDSI PSSAMQEDHV
     SMGWSAARKL RRAVDGLTTV LAVELLTAAR ALDLRAPLTP GPATAAAVAA LRAHVPGPGP
     DRHLAPEIAT AEALVRSGAV LAAAHTATRR NP
//