ID M7BY94_CHEMY Unreviewed; 462 AA.
AC M7BY94;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 ORFNames=UY3_01916 {ECO:0000313|EMBL:EMP40790.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP40790.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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; KB503068; EMP40790.1; -; Genomic_DNA.
DR AlphaFoldDB; M7BY94; -.
DR STRING; 8469.M7BY94; -.
DR eggNOG; KOG1403; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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 Aminotransferase {ECO:0000313|EMBL:EMP40790.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Transferase {ECO:0000313|EMBL:EMP40790.1}.
SQ SEQUENCE 462 AA; 51144 MW; CC0B237641BBA3E0 CRC64;
MYDENGEKYL DCINNVAHVG HSHPDVIKAA VKQMELLNTN SRFLHDNLVQ YAKRLTTTLP
EKLSICYFVN SGSEANDLAL RLARQYRGHQ DVITLDHAYH GHVSSLIDIS PYKFNQLGKE
GKKEFVHVAH SPDIYRGKYR EDHPDPANAY ADDVKKIIEE AEKSGRKIAA FIAESMQSCG
GQIIPPAGYF QKVAEYVHKA GGVFIADEVQ VGFGRVGKHF WGFQLQGKDF VPDIVTMGKP
IGNGHPMSCV VTTREIAEAF GASGLEYFNT FGGNPVSCAI GLAVLDVIEK DDLQGNAIRV
GNYLTELLNK QKEKHPLIGD VRGIGLFVGV DLVKDQLTRT PATAEAQHII YKLKEQRILL
SADGPHRNIL KFKPPMCFTM EDAKLVVDQI DELLTALEEA TGARTGNGRS TTAQHKKKMI
NEGNSQSDCI GESINHINGT ACRQKNGLYT DNRTVPCKRI RT
//
