ID R1E1E0_EMIHU Unreviewed; 570 AA.
AC R1E1E0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=pyridoxal 5'-phosphate synthase (glutamine hydrolyzing) {ECO:0000256|ARBA:ARBA00012084};
DE EC=4.3.3.6 {ECO:0000256|ARBA:ARBA00012084};
GN ORFNames=EMIHUDRAFT_427499 {ECO:0000313|EMBL:EOD16846.1};
OS Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC Noelaerhabdaceae; Emiliania.
OX NCBI_TaxID=2903 {ECO:0000313|EMBL:EOD16846.1};
RN [1] {ECO:0000313|EMBL:EOD16846.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP1516 {ECO:0000313|EMBL:EOD16846.1};
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:EOD16846}
RP IDENTIFICATION.
RG EnsemblProtists;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate +
CC L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-
CC phosphate; Xref=Rhea:RHEA:31507, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:58359, ChEBI:CHEBI:59776,
CC ChEBI:CHEBI:597326; EC=4.3.3.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000017};
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004737}.
CC -!- SIMILARITY: Belongs to the PdxS/SNZ family.
CC {ECO:0000256|ARBA:ARBA00007281, ECO:0000256|PROSITE-ProRule:PRU00481}.
CC -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family.
CC {ECO:0000256|ARBA:ARBA00008345}.
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DR EMBL; KB866687; EOD16846.1; -; Genomic_DNA.
DR RefSeq; XP_005769275.1; XM_005769218.1.
DR STRING; 2903.R1E1E0; -.
DR PaxDb; 2903-EOD16846; -.
DR EnsemblProtists; EOD16846; EOD16846; EMIHUDRAFT_427499.
DR GeneID; 17263006; -.
DR KEGG; ehx:EMIHUDRAFT_427499; -.
DR eggNOG; KOG1606; Eukaryota.
DR eggNOG; KOG3210; Eukaryota.
DR HOGENOM; CLU_034702_0_0_1; -.
DR OMA; CIVEASM; -.
DR Proteomes; UP000013827; Unassembled WGS sequence.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR001852; PdxS/SNZ.
DR InterPro; IPR033755; PdxS/SNZ_N.
DR InterPro; IPR002161; PdxT/SNO.
DR InterPro; IPR021196; PdxT/SNO_CS.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR NCBIfam; TIGR03800; PLP_synth_Pdx2; 1.
DR PANTHER; PTHR31829; PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNZ1-RELATED; 1.
DR PANTHER; PTHR31829:SF0; PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNZ1-RELATED; 1.
DR Pfam; PF01174; SNO; 1.
DR Pfam; PF01680; SOR_SNZ; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51129; PDXS_SNZ_2; 1.
DR PROSITE; PS01236; PDXT_SNO_1; 1.
DR PROSITE; PS51130; PDXT_SNO_2; 1.
PE 3: Inferred from homology;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000013827};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..570
FT /note="pyridoxal 5'-phosphate synthase (glutamine
FT hydrolyzing)"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014591885"
FT DOMAIN 263..466
FT /note="PdxS/SNZ N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01680"
FT ACT_SITE 115
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 213
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 215
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 570 AA; 59672 MW; D16E60F3D46AF8F3 CRC64;
MLVAALAVSG VLVGPAARPA APRSAPHALS MAAAGESFSV GVLALQGGFK EHLSAVERQA
GVTGVEVRTP ADLASVDALI LPGGESTAQG HCIVEASMLK PLQEFAASKP VWGVCAGMIL
LADGLKQSEP QALVGGLHAT IERNAFGRQI DSRFRSMSLQ GSAAAAGVSE AAYFIRAPAV
AECGEGVEVL ATLPDGETAV AVRQDNLLAT CFHPEISGDD SWLRFFLSTV AGRDLDEAEP
HPDLTTVAPW QPLPRPDSAV DTAVKRAFAV FQQGGVIMDV VDGEQARIAE EAGAVAVMAL
ERIPADIKRD GGVARSSDPA MIQDVMSSTS LPVMAKSRIG HFYEARLLEA LGVDCIDESE
VLTAADETHH IDKRDFAIPF VCAQDLGEAL RRIAEGAAMI RLKGNAGTGN VIQAVRHARD
VYSQIRQLRS LRPDEVFGFA KEHRVPVELV EQVRDAGRLP VVTFAAGGLA TPADVGLLME
LGVDGVFVGS GIFKGENPAK RAAAMVKACA HYKDPAVVVE ASTNLGKAMV GLLEHEDPAS
VAHLDDLGLE GRVLRTAENA IGGIDRSVAA
//
