ID A0A384BYG8_URSMA Unreviewed; 459 AA.
AC A0A384BYG8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:ENSUMAP00000000549};
OS Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=29073 {ECO:0000313|Ensembl:ENSUMAP00000000549};
RN [1] {ECO:0000313|Ensembl:ENSUMAP00000000549}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2019) 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 RefSeq; XP_008687637.1; XM_008689415.1.
DR AlphaFoldDB; A0A384BYG8; -.
DR STRING; 29073.ENSUMAP00000000549; -.
DR Ensembl; ENSUMAT00000000776.1; ENSUMAP00000000549.1; ENSUMAG00000000654.1.
DR OMA; GAIETMK; -.
DR OrthoDB; 345661at2759; -.
DR GO; GO:0050459; F:ethanolamine-phosphate phospho-lyase activity; IEA:Ensembl.
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; 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}.
SQ SEQUENCE 459 AA; 50996 MW; AF90A79688AB2381 CRC64;
MFDERGEQYL DCVNNVAHVG HCHPEVVKAA LKQMELLNTN SRFLHDNIVE YARRLSATLP
EKLSVCYFTN SGSEANDLAL RLARQFRGHQ DVITLDHAYH GHLSSLIEIS PYKFRKGKDV
KKAFVHVAPT PDTYRGKYRE DHADPASAYA DEVKEIIEEA HNSGRKIAAF IAESMQSCGG
QIIPPAGYFQ KVAEYVHRAG GVFIADEVQV GFGRVGKHFW SFQMHGEDFV PDIVTMGKPM
GNGHPMACVV TTKEIAEAFS SSGMEYFNTY GGNPVSSAVG LAVLNIIENE DLQGNATRVG
DYLTELLNKQ KAKHTLIGDI RGVGLFIGID LVKEGQKRPP ATEEAQHVIY KMKEKRVLLS
ADGPHRNVLK IKPPMCFTEE DAKFMVDQLD EILTVLEEAI GAQSESVISE SAPCRAKMPN
EARSERLSDG TSEPRENPSR KRNGLCTDKH SLLSKRLRT
//
