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Database: UniProt
Entry: I3JQ61_ORENI
LinkDB: I3JQ61_ORENI
Original site: I3JQ61_ORENI 
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
//
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