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Database: UniProt
Entry: W5LF85_ASTMX
LinkDB: W5LF85_ASTMX
Original site: W5LF85_ASTMX 
ID   W5LF85_ASTMX            Unreviewed;       654 AA.
AC   W5LF85;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 46.
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   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000018497.2, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000018497.2}
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_007235228.1; XM_007235166.2.
DR   AlphaFoldDB; W5LF85; -.
DR   STRING; 7994.ENSAMXP00000018497; -.
DR   Ensembl; ENSAMXT00000018497.2; ENSAMXP00000018497.2; ENSAMXG00000017914.2.
DR   GeneID; 103041200; -.
DR   KEGG; amex:103041200; -.
DR   CTD; 3034; -.
DR   eggNOG; KOG0222; Eukaryota.
DR   GeneTree; ENSGT00390000009047; -.
DR   HOGENOM; CLU_014801_4_0_1; -.
DR   InParanoid; W5LF85; -.
DR   OrthoDB; 1030318at2759; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000017914; Expressed in head kidney and 7 other cell types or tissues.
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:UP000018467}.
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;  72364 MW;  4E6E79A195BF7B58 CRC64;
     MPRFTVHVRD EWLTVPCKDT SYTINWLGVE ALKRYVKNKP DNGGIPQAKE VRFAARRCQG
     QGLLDADDII EDVLEDNDFV ELEIEGDTMS SDFIPSQPGM SYLTRPYREP SEYIFLDGSS
     LSSTDLVNLG RCRYKIKLTP EAEKKVEQSR ELLDTIVKEK KVVYGITTGF GKFARTVIPI
     SKLKELQENL IRSHSAGLGR PLSPERTRML LALRINVLAK GYSGISLETL HNMIQAFNAS
     CLSYVPEKGT VGASGDLAPL AHLALGLMGE GKMWSPKSGW ADAKYVLEAH GLKPVSLKPK
     EGLALINGTQ MITSLGAEAV ERAESIAMQA DVIAALTLEV LKGTTKAFDS DIHELRPHPG
     QKEVALRFRA LLDSDHHPSE IAESHRFCDR VQDAYTMRCC PQVHGVVNDT IAFVRNIINT
     EINSATDNPM VFSERGETIS GGNFHGEYPA KALDYLAIGV HELASISERR IERLCNPSLS
     ELPAFLVNEG GLNSGFMIAH CTAAALVSEN KVLCHPSSVD SLSTSAATED HVSMGGWAAR
     KALRVIEHVE QVLAIELLAA CQGIEFLRPV RTTTPLEKVY DLVRSVVKPW IKDRFMSADI
     EAVHRLLVDQ KVWNVAKPYI EKYCTELLPE SRPSSPTAFS LDPPTSPRKR VRHE
//
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