ID   AT2L1_BOVIN             Reviewed;         497 AA.
AC   Q5E9S4;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) 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; BT020846; AAX08863.1; -; mRNA.
DR   EMBL; BC123420; AAI23421.1; -; mRNA.
DR   RefSeq; NP_001015605.1; NM_001015605.1.
DR   AlphaFoldDB; Q5E9S4; -.
DR   SMR; Q5E9S4; -.
DR   STRING; 9913.ENSBTAP00000013587; -.
DR   PaxDb; Q5E9S4; -.
DR   Ensembl; ENSBTAT00000013587; ENSBTAP00000013587; ENSBTAG00000010284.
DR   GeneID; 515186; -.
DR   KEGG; bta:515186; -.
DR   CTD; 64850; -.
DR   VEuPathDB; HostDB:ENSBTAG00000010284; -.
DR   VGNC; VGNC:53712; ETNPPL.
DR   eggNOG; KOG1403; Eukaryota.
DR   GeneTree; ENSGT00940000157910; -.
DR   HOGENOM; CLU_016922_8_0_1; -.
DR   InParanoid; Q5E9S4; -.
DR   OMA; MVPNYNP; -.
DR   OrthoDB; 145181at2759; -.
DR   TreeFam; TF320468; -.
DR   Reactome; R-BTA-1483213; Synthesis of PE.
DR   Proteomes; UP000009136; Chromosome 6.
DR   Bgee; ENSBTAG00000010284; Expressed in rectus femoris and 67 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   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..497
FT                   /note="Ethanolamine-phosphate phospho-lyase"
FT                   /id="PRO_0000287662"
FT   REGION          440..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..458
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..476
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         278
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   497 AA;  55313 MW;  5D9130D11A0BD752 CRC64;
     MCELYSKQET LALRRKHIGP SCKVFFAADP IKIVRAQRQY MFDEKGDQYL DCINNVAHVG
     HCHPEVVKAA QKQMELLNTN SRFLHDNIVE YAKRLSATLP DRLSVCYFTN SGSEANDLAL
     RLARQFRGHQ DVITLDHAYH GHLSSLIEIS PYKFQKGKDV KKEFVHVAPA PDTYRGKYRE
     DHVDPASAYA DEVKKIIDEA HNSGRKIAAF IAESMQSCGG QIIPPAGYFQ KVAEYVRGAG
     GVFIADEVQV GFGRVGKHFW SFQMFGEDFV PDIVTMGKPM GNGHPMACVV TTKEIAEAFS
     ASGMEYFNTY GGNPVSSAVG LAVLDVIKNE DLQGNATRVG NYLTELLNKQ KTKHTLIGDI
     RGVGLFIGID LVKDHQQRTP ATAEAQHIIY KMKEKRVLLS ADGPHRNVLK IKPPMCFTEE
     DAKFMVEQLD GILTGLEEAT GAETESGISK NTPCRTKMPK EAQSELLRDS SLESRENPSQ
     KRNGLCTDSL LSKRLRT