ID   A0A087Y349_POEFO        Unreviewed;       654 AA.
AC   A0A087Y349;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 2.
DT   27-MAR-2024, entry version 39.
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};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000012452.2, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000012452.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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}.
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DR   EMBL; AYCK01017529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007576418.1; XM_007576356.2.
DR   AlphaFoldDB; A0A087Y349; -.
DR   STRING; 48698.ENSPFOP00000012452; -.
DR   Ensembl; ENSPFOT00000012469.2; ENSPFOP00000012452.2; ENSPFOG00000012377.2.
DR   GeneID; 103154899; -.
DR   KEGG; pfor:103154899; -.
DR   CTD; 3034; -.
DR   eggNOG; KOG0222; Eukaryota.
DR   GeneTree; ENSGT00390000009047; -.
DR   OMA; YSLRCMP; -.
DR   OrthoDB; 1030318at2759; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000028760; 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:0060218; P:hematopoietic stem cell differentiation; IEA:Ensembl.
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:UP000028760}.
FT   DOMAIN          5..79
FT                   /note="Par3/HAL N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12053"
FT   REGION          629..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   654 AA;  71964 MW;  DA525D5113993B6F CRC64;
     MPRFTVHIRD EWVAVACRDT SNNIQWLGQE ALKRYIKNKP DNGGIVSVKE TRFLVRRCQG
     LGLLDADDTI DDVLEDNDFV ELAIEGDTMS PDFIPCEPGV SNITAAYKEP TEYISLDGNS
     LTSTDLVNLG RGLYKIKLTP EAEKKVVQSR ELLDTIVKEN RVVYGITTGF GKFARTVIPV
     GKLKELQENL VRSHSAGLGN PLSPERTRML LALRINVLAK GHSGISLETL QAMIQAFNAS
     CLSFVPEKGT VGASGDLAPL SHLALGLMGE GKMWSPKSGW ADAKYVLEAH GLKPISLKPK
     EGIALINGTQ MITSLGAEAV ERARAIAQQA DIVAALTLEV LKGTTKAFDS DIHSLRPHPG
     QTEVALRFRS LLDSDHHPSE IAESHRFCDR VQDAYTMRCC PQVHGIANDT IMFVQNIINT
     EINSATDNPM VFAERGETIS GGNFHGEYPA KALDFLSIAV HELASISERR IERLCNPSLS
     ELPAFLVNEG GLNSGFMIAH CTAASLVSEN KVLCHPSSVD SLSTSAATED HVSMGGWAAR
     KALRVVEHVE QVLAIELLAA CQGIEFLRPL RTTTPLEKVY DLVRTVVKPW IKDRFMSPDI
     EAVHRLLLDQ KVWKVAKPYI DKYQTEYIPE SRPNSPTAFS LDPPASPRKR VRHE
//