ID   A0A2A2LIY4_9BILA        Unreviewed;       665 AA.
AC   A0A2A2LIY4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Histidine ammonia-lyase {ECO:0000256|ARBA:ARBA00017271, ECO:0000256|RuleBase:RU004479};
DE            EC=4.3.1.3 {ECO:0000256|ARBA:ARBA00012994, ECO:0000256|RuleBase:RU004479};
GN   ORFNames=WR25_02649 {ECO:0000313|EMBL:PAV86161.1};
OS   Diploscapter pachys.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX   NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV86161.1, ECO:0000313|Proteomes:UP000218231};
RN   [1] {ECO:0000313|EMBL:PAV86161.1, ECO:0000313|Proteomes:UP000218231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF1309 {ECO:0000313|EMBL:PAV86161.1};
RA   Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA   Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT   "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL   Curr. Biol. 0:0-0(2017).
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   -!- SIMILARITY: Belongs to the PAL/histidase family.
CC       {ECO:0000256|ARBA:ARBA00007238, 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:PAV86161.1}.
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DR   EMBL; LIAE01006699; PAV86161.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2LIY4; -.
DR   STRING; 2018661.A0A2A2LIY4; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000218231; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; IPR021922; Par3/HAL_N.
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   Pfam; PF12053; Par3_HAL_N_term; 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:UP000218231}.
FT   DOMAIN          1..80
FT                   /note="Par3/HAL N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12053"
SQ   SEQUENCE   665 AA;  73220 MW;  C4206463088A0C80 CRC64;
     MRLQVQVGVE CIVVPCSETE TVHQVAERAV AKIRRLRPDC LQSDNYLEVR RTVGNSLLDP
     TDVISQVLKD GDFILIAVEE CETGAGKLQR RLSEIETTEK QLKHFDPRER KVSFAFDPSP
     DLPHVIKPTK LLIIDGNSLE PIDLVRCERG ECAIQLSMEA EERVRKSRLL LEKIAADHKT
     VYGVTTGFGT FSNVRISPEN IKKLQVNLIR SHSTGYGKPL SPSKTRMLLA LRINILAKGY
     SGISVENLKR MIAAFNAYCV SYVPQQGTVG CSGDLCPLAH LALGLLGEGK MWSPSTGWGS
     AEIVLKKNHL EPLVLGPKEG LALINGTQMV TALGAYTVER ANNIARQADV IAALSLDVLK
     GTTRAYDPDI HRIRPHAGQN LSALRLRSLL HSEANPSQIA ESHRNCSKVQ DAYTLRCVPQ
     VHGIVHDTIE FVKGIIRVEM NSATDNPLVF ADREEIISGG NFHGEYPAKA LDYLAIAVAE
     LAQMSERRLE RLVNHDLSGL PTFLTPDGGL NSGFMTVQLC AASLVSENKE DHVSMGGFAA
     RKALTIVEHV EAVLAMELLA ACQGIEFLLP LRSTAPLHKV YKLVRQISAP LTEDRSMHGD
     IEAVVALLRE NKVWETVLPH LETLEAMEEL DPDALRLSAK TPTGIVMADR VDLHETDESD
     DEHKH
//