ID W5KVF0_ASTMX Unreviewed; 490 AA.
AC W5KVF0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 51.
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};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000011562.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000011562.2}
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}.
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 AlphaFoldDB; W5KVF0; -.
DR STRING; 7994.ENSAMXP00000011562; -.
DR Ensembl; ENSAMXT00000011562.2; ENSAMXP00000011562.2; ENSAMXG00000011256.2.
DR eggNOG; KOG1403; Eukaryota.
DR GeneTree; ENSGT00940000157910; -.
DR HOGENOM; CLU_016922_8_0_1; -.
DR InParanoid; W5KVF0; -.
DR OrthoDB; 345661at2759; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000011256; Expressed in mesonephros and 13 other cell types or tissues.
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; IEA:Ensembl.
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; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000018467}.
FT REGION 442..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 490 AA; 54734 MW; B802B2B2BA0631A8 CRC64;
MATQVFKKQK TIELRKKHIG PSCKVFFGHD PIKIVRARGQ YMYNEKDEQY LDCINNVAHV
GHSHPDVVRA GAKQMELLNT NSRFLHDNLV QYAQRLQATL PEKLSVCYFV NSGSEANDLA
LRLAWQYTGH RDIITLDNAY HGHVSSLIDI SPYKFHQLAH PQQSQHVHVA PSPDIYRGKY
REDHPDPATA YADDVKDIIE KAHAKGHKIA VFIAESLQSC GGQVIPPVGY FQKVAQHVRE
AGGLFIADEV QVGFGRVGSH FWAFQLQGED FVPDIVTMGK PIGNGHPISC VVTTREVAEG
FMSSGMEYFN TFGGNPVSCA IGLAVLDVIE KEALQSNALR VGGYLTDLLE KLKQKHPLIG
DIRGRGLFVG VELVKNRIER TPATDEAQTV IYRLKDQRIL LSADGPHRNV LKFKPPMCFT
TEDADLAVDK IDQILTDLEK ASDLSMPADK DPETIPSKRK ETLKENGHEI HSNGPTDIHS
ITKTNKRRRT
//
