ID   A0A3Q2DZE0_CYPVA        Unreviewed;       654 AA.
AC   A0A3Q2DZE0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
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   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000024354.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000024354.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   RefSeq; XP_015232220.1; XM_015376734.1.
DR   AlphaFoldDB; A0A3Q2DZE0; -.
DR   STRING; 28743.ENSCVAP00000024354; -.
DR   Ensembl; ENSCVAT00000004404.1; ENSCVAP00000024354.1; ENSCVAG00000000237.1.
DR   GeneID; 107086014; -.
DR   KEGG; cvg:107086014; -.
DR   CTD; 3034; -.
DR   GeneTree; ENSGT00390000009047; -.
DR   OMA; YSLRCMP; -.
DR   OrthoDB; 1030318at2759; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000265020; Unplaced.
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; 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:UP000265020}.
FT   REGION          631..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   654 AA;  72106 MW;  AC0003AD4D370B75 CRC64;
     MPRFTVHIRD EWLAVSCRDT SNTIQWLGQE ALKRYMKNKP DNGGIGSVKE TRFFVRRCQG
     LGLLDAEDTI DDVLEDNDFV ELAIEGDTMS SDFIPCEPGV SNITAAYKEP AEYISLDGNS
     LTSTDLVNLG RGLYKIKLTE EAERKVVQSR ELLDTIVKEN KVVYGITTGF GKFARTVIPV
     SKLKELQENL VRSHSAGLGN PLSPERTRML LALRINVLAK GYSGISLETL QAMIQAFNAS
     CLSFVPEKGT VGASGDLAPL SHLALGLMGE GKMWSPKSGW ADAKYVLEAH GLKPISLKPK
     EGLALINGTQ MITSLGAEAV ERAQAIAQQA DIVAALTLEV LKGTTKAFDS DIHSLRPHPG
     QTEVALRFRS LLDSDHHPSE IAESHRFCDR VQDAYTMRCC PQVHGIANDT IKFVQNIINT
     EINSATDNPM VFAERGETIS GGNFHGEYPA KALDFLCIAV HELASISERR IERLCNPSLS
     ELPAFLVNEG GLNSGFMIAH CTAASLVSEN KVLCHPSSVD SLSTSAATED HVSMGGWAAR
     KALRVVEHVE QVLAIELLAA CQGIEFLRPL RTTTPLEKVY DLVRSVVRPW IKDRFMSPDI
     EAVHRLLVDQ KVWNVAKPYI DKYQREYVPE SRPCSPTAFS LDTPASPRKR FRHE
//