ID   AT2L1_XENLA             Reviewed;         509 AA.
AC   Q6DEB1;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
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;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC077219; AAH77219.1; -; mRNA.
DR   RefSeq; NP_001086637.1; NM_001093168.1.
DR   AlphaFoldDB; Q6DEB1; -.
DR   SMR; Q6DEB1; -.
DR   GeneID; 446472; -.
DR   KEGG; xla:446472; -.
DR   CTD; 446472; -.
DR   Xenbase; XB-GENE-6256217; etnppl.L.
DR   OMA; MVPNYNP; -.
DR   OrthoDB; 145181at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 446472; Expressed in intestine and 16 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0050459; F:ethanolamine-phosphate phospho-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
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   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..509
FT                   /note="Ethanolamine-phosphate phospho-lyase"
FT                   /id="PRO_0000287666"
FT   REGION          451..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..469
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         279
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   509 AA;  56971 MW;  211BE6D6961E9E11 CRC64;
     MCEEYTKEKI MEIRKKHIGP SCKVFFANDP IKIVHAKGQY MFDEKGERYL DCINNVAHVG
     HSHPEVTKAA LKQMELLNTN SRFLHDNLVR YAECLISTLP EKLSVCYFVN SGSEANDLAL
     RLARQYTGHQ DVITLDHAYH GHVTSLIDIS PYKFHQLGKD AQKEYIHVAP SPDTYRGKYR
     EDHPDPASAY AKDVEDIIQK AHQNKRQIAA FIAESMQSCG GQIIPPAGYF QKVSEFVHKA
     GGVFIADEVQ VGFGRVGKHF WSFQLQGEDF LPDIVTMGKP IGNGHPMSCV VTTKEIAEAF
     GATGMEYFNT FGGNPVSCAI GLAVLDIIEK EDLRGNATTV GNYLTELLNE QKQKHPLIGD
     IRGVGLFVGV DLVKDRLFRT PATAEAQHII YKLKEKRILL SADGPYRNVL KFKPPMCFNK
     EDAKLVVDEI DQCLTALEKA IGIQSNAGLH EKTSAKRKVH NENSGDTNAK EKETCSSNSQ
     ERNPNDHAYR QSNGLHPESP TFTRKRIRT