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Database: UniProt
Entry: G1SJ91_RABIT
LinkDB: G1SJ91_RABIT
Original site: G1SJ91_RABIT 
ID   G1SJ91_RABIT            Unreviewed;       408 AA.
AC   G1SJ91;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 2.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=5-phosphohydroxy-L-lysine phospho-lyase {ECO:0000313|Ensembl:ENSOCUP00000002790.3};
GN   Name=PHYKPL {ECO:0000313|Ensembl:ENSOCUP00000002790.3};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000002790.3, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000002790.3, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000002790.3,
RC   ECO:0000313|Proteomes:UP000001811};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSOCUP00000002790.3}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000002790.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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; AAGW02066641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G1SJ91; -.
DR   Ensembl; ENSOCUT00000003211.3; ENSOCUP00000002790.3; ENSOCUG00000003211.4.
DR   GeneTree; ENSGT00940000159222; -.
DR   HOGENOM; CLU_016922_8_0_1; -.
DR   TreeFam; TF320468; -.
DR   Proteomes; UP000001811; Chromosome 3.
DR   Bgee; ENSOCUG00000003211; Expressed in blood and 17 other cell types or tissues.
DR   ExpressionAtlas; G1SJ91; baseline.
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:SF6; 5-PHOSPHOHYDROXY-L-LYSINE PHOSPHO-LYASE; 1.
DR   PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 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   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001811}.
SQ   SEQUENCE   408 AA;  44661 MW;  EABA0F385F95AA20 CRC64;
     RAGGGPVEWA EWSRLCDGHG PLAVGHCHPL VVQAAHEQNQ VLNTNSRYLH DNIVDYAQRL
     SETLPEELCV FYFLNSGSEA NDLALRLARQ YTGHQDVVVL DHAYHGHLSS LIDISPYKFR
     DLDGQKEWVH VAPLPDTYRG LYREDHPSPA AAYASEVERV VRSAQERGRK IAAFFAESLP
     SVGGQIVPPA GYFSQVAGHI RRAGGLFVAD EIQVGFGRVG THFWAFQLQG QDFVPDIVTM
     GKSIGNGHPI ACVATTQAVA KAFEATGVEY FNTFGGSPVS CAVGLAVLDV LEKEQLQAHA
     TCVGRFLMEL LRQQKAKHAI IGDIRGAGLF IGVDLIKDKA TRTPATEEAD YLVSRLKENH
     ILLSTDGPGR NVLKFKPPMC FSLDNAQYLV AKLDAILTDR SQAITQHT
//
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