ID   AT2L1_DANRE             Reviewed;         492 AA.
AC   Q7SY54;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Ethanolamine-phosphate phospho-lyase;
DE            EC=4.2.3.2;
DE   AltName: Full=Alanine--glyoxylate aminotransferase 2-like 1;
GN   Name=etnppl; Synonyms=agxt2l1; ORFNames=zgc:63486;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the pyridoxal-phosphate-dependent breakdown of
CC       phosphoethanolamine, converting it to ammonia, inorganic phosphate and
CC       acetaldehyde. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + phosphoethanolamine = acetaldehyde + NH4(+) + phosphate;
CC         Xref=Rhea:RHEA:17889, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:43474, ChEBI:CHEBI:58190; EC=4.2.3.2;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
CC   -!- CAUTION: Does not seem to possess aminotransferase activity.
CC       {ECO:0000250|UniProtKB:Q8TBG4}.
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DR   EMBL; BC055122; AAH55122.1; -; mRNA.
DR   RefSeq; NP_956743.1; NM_200449.1.
DR   AlphaFoldDB; Q7SY54; -.
DR   SMR; Q7SY54; -.
DR   STRING; 7955.ENSDARP00000051523; -.
DR   PaxDb; Q7SY54; -.
DR   Ensembl; ENSDART00000051524; ENSDARP00000051523; ENSDARG00000035544.
DR   GeneID; 393421; -.
DR   KEGG; dre:393421; -.
DR   CTD; 64850; -.
DR   ZFIN; ZDB-GENE-040426-1133; etnppl.
DR   eggNOG; KOG1403; Eukaryota.
DR   GeneTree; ENSGT00940000157910; -.
DR   HOGENOM; CLU_016922_8_0_1; -.
DR   InParanoid; Q7SY54; -.
DR   OMA; MVPNYNP; -.
DR   OrthoDB; 145181at2759; -.
DR   PhylomeDB; Q7SY54; -.
DR   TreeFam; TF320468; -.
DR   Reactome; R-DRE-1483213; Synthesis of PE.
DR   PRO; PR:Q7SY54; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 7.
DR   Bgee; ENSDARG00000035544; Expressed in liver and 14 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0050459; F:ethanolamine-phosphate phospho-lyase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   GO; GO:0035162; P:embryonic hemopoiesis; IMP:ZFIN.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   2: Evidence at transcript level;
KW   Lyase; Mitochondrion; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..492
FT                   /note="Ethanolamine-phosphate phospho-lyase"
FT                   /id="PRO_0000287665"
FT   REGION          462..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..482
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         280
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   492 AA;  54735 MW;  A95F48326640276E CRC64;
     MATETLDKQK TIDLRKKHVG PSCKVFFDHD PIKIVRAKGQ YMYNEKDEKY LDCINNVAHV
     GHCHPDVVSA GAKQMELLNT NSRFLHDSLV LYAQRLQATL PEKLSVCYFV NSGSEANDLA
     LRLAWQYTGH KDIITLDNAY HGHVSSLIDI SPYKFHQMAG AEPSQHVHVA LSPDTYRGKY
     REDHPDPATA YAENVKEVIE EAHKKGHEIA AFIAESLQSC GGQVIPPMGY FQKVAQHVRN
     AGGIFIADEV QVGFGRVGTH FWGFQLQGED FVPDIVTMGK PIGNGHPMSC VITSREIAES
     FMSSGMEYFN TFGGNPVSCA IGLAVLNVIE KEDLQGNALH VGGYLTQLLE DLKKRHPLVG
     DVRGRGLFVG LELVRNQSKR TPATAEAQEV IYRLKEQRIL LSADGPHRNV LKFKPPMCFS
     REDAEFAVEK IDQILTDLEK AMVLQRPEAA ILETGHIKRK DASDENGLVH PSNGNSHKHT
     STIPLSKKTK RN