ID R1EDX5_EMIHU Unreviewed; 946 AA.
AC R1EDX5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Putative aminotransferase {ECO:0000313|EMBL:EOD24900.1};
GN ORFNames=EMIHUDRAFT_457672 {ECO:0000313|EMBL:EOD24900.1};
OS Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC Noelaerhabdaceae; Emiliania.
OX NCBI_TaxID=2903 {ECO:0000313|EMBL:EOD24900.1};
RN [1] {ECO:0000313|EMBL:EOD24900.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP1516 {ECO:0000313|EMBL:EOD24900.1};
RG DOE Joint Genome Institute;
RA Read B., Kegel J., Klute M., Kuo A., Lefebvre S.C., Maumus F., Mayer C.,
RA Miller J., Allen A., Bidle K., Borodovsky M., Bowler C., Brownlee C.,
RA Claverie J.-M., Cock M., De Vargas C., Elias M., Frickenhaus S.,
RA Gladyshev V.N., Gonzalez K., Guda C., Hadaegh A., Herman E.,
RA Iglesias-Rodriguez D., Jones B., Lawson T., Leese F., Lin Y.-C.,
RA Lindquist E., Lobanov A., Lucas S., Malik S.-H.B., Marsh M.E., Mock T.,
RA Monier A., Moreau H., Mueller-Roeber B., Napier J., Ogata H., Parker M.,
RA Probert I., Quesneville H., Raines C., Rensing S., Riano-Pachon D.M.,
RA Richier S., Rokitta S., Salamov A., Sarno A.F., Schmutz J., Schroeder D.,
RA Shiraiwa Y., Soanes D.M., Valentin K., Van Der Giezen M., Van Der Peer Y.,
RA Vardi A., Verret F., Von Dassow P., Wheeler G., Williams B., Wilson W.,
RA Wolfe G., Wurch L.L., Young J., Dacks J.B., Delwiche C.F., Dyhrman S.,
RA Glockner G., John U., Richards T., Worden A.Z., Zhang X., Grigoriev I.V.;
RT "Genome variability drives Emilianias global distribution.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000013827}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP1516 {ECO:0000313|Proteomes:UP000013827};
RX PubMed=23760476; DOI=10.1038/nature12221;
RA Read B.A., Kegel J., Klute M.J., Kuo A., Lefebvre S.C., Maumus F.,
RA Mayer C., Miller J., Monier A., Salamov A., Young J., Aguilar M.,
RA Claverie J.M., Frickenhaus S., Gonzalez K., Herman E.K., Lin Y.C.,
RA Napier J., Ogata H., Sarno A.F., Shmutz J., Schroeder D., de Vargas C.,
RA Verret F., von Dassow P., Valentin K., Van de Peer Y., Wheeler G.,
RA Dacks J.B., Delwiche C.F., Dyhrman S.T., Glockner G., John U., Richards T.,
RA Worden A.Z., Zhang X., Grigoriev I.V., Allen A.E., Bidle K., Borodovsky M.,
RA Bowler C., Brownlee C., Cock J.M., Elias M., Gladyshev V.N., Groth M.,
RA Guda C., Hadaegh A., Iglesias-Rodriguez M.D., Jenkins J., Jones B.M.,
RA Lawson T., Leese F., Lindquist E., Lobanov A., Lomsadze A., Malik S.B.,
RA Marsh M.E., Mackinder L., Mock T., Mueller-Roeber B., Pagarete A.,
RA Parker M., Probert I., Quesneville H., Raines C., Rensing S.A.,
RA Riano-Pachon D.M., Richier S., Rokitta S., Shiraiwa Y., Soanes D.M.,
RA van der Giezen M., Wahlund T.M., Williams B., Wilson W., Wolfe G.,
RA Wurch L.L.;
RT "Pan genome of the phytoplankton Emiliania underpins its global
RT distribution.";
RL Nature 499:209-213(2013).
RN [3] {ECO:0000313|EnsemblProtists:EOD24900}
RP IDENTIFICATION.
RG EnsemblProtists;
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-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR EMBL; KB865375; EOD24900.1; -; Genomic_DNA.
DR RefSeq; XP_005777329.1; XM_005777272.1.
DR STRING; 2903.R1EDX5; -.
DR PaxDb; 2903-EOD24900; -.
DR EnsemblProtists; EOD24900; EOD24900; EMIHUDRAFT_457672.
DR GeneID; 17270445; -.
DR KEGG; ehx:EMIHUDRAFT_457672; -.
DR eggNOG; KOG0257; Eukaryota.
DR eggNOG; KOG2380; Eukaryota.
DR eggNOG; KOG2797; Eukaryota.
DR HOGENOM; CLU_004330_0_0_1; -.
DR OMA; HHNDEEL; -.
DR Proteomes; UP000013827; Unassembled WGS sequence.
DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 1.
DR CDD; cd04905; ACT_CM-PDT; 1.
DR CDD; cd13631; PBP2_Ct-PDT_like; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR001086; Preph_deHydtase.
DR InterPro; IPR018528; Preph_deHydtase_CS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 2.
DR Pfam; PF00800; PDT; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
DR PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:EOD24900.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000013827};
KW Transferase {ECO:0000313|EMBL:EOD24900.1}.
FT DOMAIN 5..187
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
SQ SEQUENCE 946 AA; 99601 MW; 0BDB7300891547C1 CRC64;
MSQPTVGFQG VPGAYSESAS IEAFAAAGVD EIQARGFHTF EDVFVALSKG AIDYAVLPVE
NTLGGSIHVN YDLLLRFHGA VHILGEYTLR VRHTLLALPG VQLNDIKKAM SHPQALAQTE
SYLRTAGIAP LVGYDTAGSA ELVVQQGLRD TAAIASIHAA KVHGLEVLDY GIEDDPNNFT
RFLILSRAAP PPGALLGFAA KTSVVFTPHR DEAGVLFKAM SVFAVRDINL SKIESRPHKP
GVLGAGAGPA AGASGGAEAR RASAANGTAV VPAASFEYTF YVDLLARRRT DASPPASSGA
RVSHGPATRL RVGIVGFGTF GQFLARRWVG RGHAVFAHSR GDYAKTAAGM GVAWVPDAAA
LSELSVDVLF VATSILSFEK ALVVDVLSVK AHAKQTMLAV LPPTADVLCT HPMFGPDSGR
HGWQGLPCVY DQARAAPDAA DCRGAVNGAS GRCQMVKLSC ERHDALAAAS QFVTHLTGRL
LSKLQLQPSP IATQGFKALL QLVDNTRAPP SLGLFCARER RLFTAAGVWT GAAFSELRRE
ILDFGAAPPA PAGEIAISRT VAAMPASATV AISDLAIELK RQGKPVISLS VGEPDFSPPP
EVMEAAHEAL REGKVKYTAL AGSHELRSAV CDDLLRRKGL KYEPSQVVCC CGAKQAILQA
VLALCNPGGD VTAPTPRCDM SRTRPLDATG DEIIVPTPYW PSHLGTAQLR GAMLILCNPS
NPTGALLPRA ALEGVAAVLR RHPQVVVLAD EIYELIAYDE PHVAFATLEG MYERTLTVNG
FSKGAAMTGF RLGYVCGPHG AIKAMAKVQG NNTSCPSSIA QHAGVAAVTH AHGAFAEAAT
ANFRRKRDYV VGRLRGMAGV SCPVPQGAFY VFPTVSAFYG RTAPSGAAPH DSTSLCDYLL
REEHLALVPG AGFGAPGCVR ISYATSMEAL QEAMDRMERG LAKLCK
//
