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 27-MAR-2024, entry version 103.
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; 9913-ENSBTAP00000013587; -.
DR Ensembl; ENSBTAT00000013587.5; ENSBTAP00000013587.4; ENSBTAG00000010284.5.
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; GAIETMK; -.
DR OrthoDB; 345661at2759; -.
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 cell types or 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688:SF1; ETHANOLAMINE-PHOSPHATE PHOSPHO-LYASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 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
//
