ID I3JQ61_ORENI Unreviewed; 458 AA.
AC I3JQ61;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 24-JAN-2024, entry version 64.
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:ENSONIP00000011005.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000011005.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000011005.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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 AlphaFoldDB; I3JQ61; -.
DR STRING; 8128.ENSONIP00000040988; -.
DR Ensembl; ENSONIT00000011014.2; ENSONIP00000011005.2; ENSONIG00000008754.2.
DR eggNOG; KOG1403; Eukaryota.
DR GeneTree; ENSGT00940000157910; -.
DR HOGENOM; CLU_016922_8_0_1; -.
DR TreeFam; TF320468; -.
DR Proteomes; UP000005207; Linkage group LG3.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR45688; -; 1.
DR PANTHER; PTHR45688:SF1; ETHANOLAMINE-PHOSPHATE PHOSPHO-LYASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207}.
SQ SEQUENCE 458 AA; 50866 MW; 9D7FA3FF0163F19E CRC64;
MFAERFEKKE TIDLRKRYIG PSCKIFFSHD PIKIVRAKGQ YMYDEKGQRY LDCINNVAHV
GHCHPDVVKA GAQQMELLNT NSRFLHDNLV LYAQRLQATL PDKLGVCYFV NSGSEANDLA
LRLARQYTGH TDIITLENAY HGHVSSLIDI SPYKFHQLSD AEQNQFVHVA SSPDVYRGKY
RADHPDPATA YADEVKDIIS KAHKKGGKIA AFIAESLQSC GGQVIPPVGY FQQVAQHVRK
AGGIFIADEV QVGFGRVGSH FWAFQLQGED FVPDIVTMGK PIGNGHPMSC VVTTKEVAEA
FMTSGMEYFN TFGGNPVSCA IGLAVLDVIE KEDLQGNALR VGQYLTSLLE KQKEKHLLIG
DIRGRGLFVG VELVRDRLKI TPATAEAQEV IYRLKEQHIL LSADGPHRNV LKFKPPMCFT
TEDAELVVEK IDVILTDGKY LLSFIKGNKD LLSGSGLV
//