(data stored in SCRATCH zone)

SWISSPROT: D1CDF3_THET1

ID   D1CDF3_THET1            Unreviewed;       358 AA.
AC   D1CDF3;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=Pyridoxal 5'-phosphate synthase subunit PdxS {ECO:0000256|HAMAP-Rule:MF_01824};
DE            Short=PLP synthase subunit PdxS {ECO:0000256|HAMAP-Rule:MF_01824};
DE            EC=4.3.3.6 {ECO:0000256|HAMAP-Rule:MF_01824};
DE   AltName: Full=Pdx1 {ECO:0000256|HAMAP-Rule:MF_01824};
GN   Name=pdxS {ECO:0000256|HAMAP-Rule:MF_01824};
GN   OrderedLocusNames=Tter_0036 {ECO:0000313|EMBL:ACZ40959.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ40959.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ40959.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
CC   -!- FUNCTION: Catalyzes the formation of pyridoxal 5'-phosphate from
CC       ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and
CC       ammonia. The ammonia is provided by the PdxT subunit. Can also use
CC       ribulose 5-phosphate and dihydroxyacetone phosphate as substrates,
CC       resulting from enzyme-catalyzed isomerization of RBP and G3P,
CC       respectively. {ECO:0000256|HAMAP-Rule:MF_01824}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-
CC         phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate
CC         + pyridoxal 5'-phosphate; Xref=Rhea:RHEA:31507,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58273, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:59776, ChEBI:CHEBI:597326; EC=4.3.3.6;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01824};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01824}.
CC   -!- SUBUNIT: In the presence of PdxT, forms a dodecamer of
CC       heterodimers. {ECO:0000256|HAMAP-Rule:MF_01824}.
CC   -!- SIMILARITY: Belongs to the PdxS/SNZ family. {ECO:0000256|HAMAP-
CC       Rule:MF_01824, ECO:0000256|PROSITE-ProRule:PRU00481}.
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DR   EMBL; CP001825; ACZ40959.1; -; Genomic_DNA.
DR   STRING; 525904.Tter_0036; -.
DR   EnsemblBacteria; ACZ40959; ACZ40959; Tter_0036.
DR   KEGG; ttr:Tter_0036; -.
DR   eggNOG; ENOG4105CD9; Bacteria.
DR   eggNOG; COG0214; LUCA.
DR   HOGENOM; HOG000227586; -.
DR   KO; K06215; -.
DR   OMA; IGVDMID; -.
DR   UniPathway; UPA00245; -.
DR   Proteomes; UP000000323; Chromosome 1.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04727; pdxS; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01824; PdxS; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001852; PdxS/SNZ.
DR   InterPro; IPR033755; PdxS/SNZ_N.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   PANTHER; PTHR31829; PTHR31829; 1.
DR   Pfam; PF01680; SOR_SNZ; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   TIGRFAMs; TIGR00343; TIGR00343; 1.
DR   PROSITE; PS01235; PDXS_SNZ_1; 1.
DR   PROSITE; PS51129; PDXS_SNZ_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1CDF3.
DR   SWISS-2DPAGE; D1CDF3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01824};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01824};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Schiff base {ECO:0000256|HAMAP-Rule:MF_01824};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     12     35       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       72    276       SOR_SNZ. {ECO:0000259|Pfam:PF01680}.
FT   REGION      299    300       D-ribose 5-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01824}.
FT   ACT_SITE    145    145       Schiff-base intermediate with D-ribose 5-
FT                                phosphate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01824}.
FT   BINDING      88     88       D-ribose 5-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01824}.
FT   BINDING     217    217       D-ribose 5-phosphate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01824}.
FT   BINDING     229    229       Glyceraldehyde 3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01824}.
FT   BINDING     278    278       D-ribose 5-phosphate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01824}.
SQ   SEQUENCE   358 AA;  39277 MW;  785D6F72420E81B8 CRC64;
     MTIYRKHFTK YNLYVATKMV IVCVITFITS IRVSYKNFSA TPVFVCAKMI YWSNPNTPYI
     QEAIEVEKST ELTKRGLAEM LKGGVIMDVV NAEQARIAEA AGAVAVMALE RVPADIRAQG
     GVARMSDPAL IEEIMNAVTI PVMAKVRIGH FVEAQILEAL GVDYIDESEV LTPADEMHHI
     DKKKFKVPFV CGARDLGEAL RRVGEGASML RLKGEAGTGN IVEAVRHARL IYSEVRRLST
     MPEDEWMAYA KQIQAPYELV AEVARTGKLP VVNFAAGGIA TPADAALMMQ LGVDGIFVGS
     GIFKSSDPYK RAKAIVEATT HYNDPEVLVR VSKGLGEAMH GIDIRTLSQE ELMAPRGW
//

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