ID F1S126_PIG Unreviewed; 499 AA.
AC F1S126;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Ethanolamine-phosphate phospho-lyase {ECO:0000256|ARBA:ARBA00040022};
DE EC=4.2.3.2 {ECO:0000256|ARBA:ARBA00039127};
DE AltName: Full=Alanine--glyoxylate aminotransferase 2-like 1 {ECO:0000256|ARBA:ARBA00041584};
GN Name=ETNPPL {ECO:0000313|Ensembl:ENSSSCP00000009751.3,
GN ECO:0000313|VGNC:VGNC:97987};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000009751.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000009751.3, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000009751.3,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HDB22510.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000009751.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the pyridoxal-phosphate-dependent breakdown of
CC phosphoethanolamine, converting it to ammonia, inorganic phosphate and
CC acetaldehyde. {ECO:0000256|ARBA:ARBA00037113}.
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 Evidence={ECO:0000256|ARBA:ARBA00036990};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR EMBL; DQIR01167033; HDB22510.1; -; Transcribed_RNA.
DR RefSeq; XP_013834417.1; XM_013978963.1.
DR STRING; 9823.ENSSSCP00000009751; -.
DR Ensembl; ENSSSCT00000010013.5; ENSSSCP00000009751.3; ENSSSCG00000009144.5.
DR VGNC; VGNC:97987; ETNPPL.
DR GeneTree; ENSGT00940000157910; -.
DR HOGENOM; CLU_016922_8_0_1; -.
DR OMA; GAIETMK; -.
DR OrthoDB; 345661at2759; -.
DR Reactome; R-SSC-1483213; Synthesis of PE.
DR Proteomes; UP000008227; Chromosome 8.
DR Bgee; ENSSSCG00000009144; Expressed in dorsal plus ventral thalamus and 27 other cell types or tissues.
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 1: Evidence at protein level;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:HDB22510.1};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1S126};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT REGION 466..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 499 AA; 55725 MW; 758263CAA175D87B CRC64;
MCELYSKQDT LALRRKHIGP SCKVFFAADP IKIVRAQRQY MFDEKGDRYL DCINNVAHVG
HCHPEVVQAA QKQMELLNTN SRFLHDNIVE YAKRLSATLP DKLSVCYFTN SGSEANDLAL
RLARQFRGHQ DVITLDHAYH GHLTSLIEIS PYKFQQGKDV KKEFVHVAPS PDTYRGKYRE
DHADPAGAYA DEVKKIIEEA HNRGRKIAAF IAESMQSCGG QIIPPAGYFQ KVAEYVRGAG
GVFIADEVQV GFGRVGKHFW SFQMLGEDFV PDIITMGKPM GNGHPMACVV TTREIAEAFS
SSGIEYFNTY GGNPVSSAVG LAVLDVIENE DLQGNATRVG NYLTELLNKQ KAKHTLIGDI
RGVGLFIGID LVKDREKRTP ATAEAQHIIY KMKEKRVLLS ADGPHRNVLK IKPPMCFTEE
DAKFMVDQLD GILTDLEDAF GAKMENVISE NSPCRTRMPN EARSEMLRDG APDPQENPSH
KRNGLCTDKH SLLSKRLKT
//
