ID AT2L1_DANRE Reviewed; 492 AA.
AC Q7SY54;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 114.
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; ORFNames=zgc:63486;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2003) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC055122; AAH55122.1; -; mRNA.
DR RefSeq; NP_956743.1; NM_200449.1.
DR AlphaFoldDB; Q7SY54; -.
DR SMR; Q7SY54; -.
DR STRING; 7955.ENSDARP00000051523; -.
DR PaxDb; 7955-ENSDARP00000051523; -.
DR GeneID; 393421; -.
DR KEGG; dre:393421; -.
DR AGR; ZFIN:ZDB-GENE-040426-1133; -.
DR CTD; 64850; -.
DR ZFIN; ZDB-GENE-040426-1133; etnppl.
DR eggNOG; KOG1403; Eukaryota.
DR HOGENOM; CLU_016922_8_0_1; -.
DR InParanoid; Q7SY54; -.
DR OMA; GAIETMK; -.
DR OrthoDB; 345661at2759; -.
DR PhylomeDB; Q7SY54; -.
DR TreeFam; TF320468; -.
DR Reactome; R-DRE-1483213; Synthesis of PE.
DR PRO; PR:Q7SY54; -.
DR Proteomes; UP000000437; Chromosome 7.
DR Bgee; ENSDARG00000035544; Expressed in liver and 14 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 GO; GO:0035162; P:embryonic hemopoiesis; IMP:ZFIN.
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 PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 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..492
FT /note="Ethanolamine-phosphate phospho-lyase"
FT /id="PRO_0000287665"
FT REGION 462..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 280
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 492 AA; 54735 MW; A95F48326640276E CRC64;
MATETLDKQK TIDLRKKHVG PSCKVFFDHD PIKIVRAKGQ YMYNEKDEKY LDCINNVAHV
GHCHPDVVSA GAKQMELLNT NSRFLHDSLV LYAQRLQATL PEKLSVCYFV NSGSEANDLA
LRLAWQYTGH KDIITLDNAY HGHVSSLIDI SPYKFHQMAG AEPSQHVHVA LSPDTYRGKY
REDHPDPATA YAENVKEVIE EAHKKGHEIA AFIAESLQSC GGQVIPPMGY FQKVAQHVRN
AGGIFIADEV QVGFGRVGTH FWGFQLQGED FVPDIVTMGK PIGNGHPMSC VITSREIAES
FMSSGMEYFN TFGGNPVSCA IGLAVLNVIE KEDLQGNALH VGGYLTQLLE DLKKRHPLVG
DVRGRGLFVG LELVRNQSKR TPATAEAQEV IYRLKEQRIL LSADGPHRNV LKFKPPMCFS
REDAEFAVEK IDQILTDLEK AMVLQRPEAA ILETGHIKRK DASDENGLVH PSNGNSHKHT
STIPLSKKTK RN
//
