(data stored in ACNUC7421 zone)

SWISSPROT: Q145L2_PARXL

ID   Q145L2_PARXL            Unreviewed;       336 AA.
AC   Q145L2;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 94.
DE   RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00536, ECO:0000256|SAAS:SAAS00956571};
DE            EC=1.1.1.262 {ECO:0000256|HAMAP-Rule:MF_00536, ECO:0000256|SAAS:SAAS00956565};
DE   AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00536};
GN   Name=pdxA {ECO:0000256|HAMAP-Rule:MF_00536};
GN   ORFNames=Bxe_A4022 {ECO:0000313|EMBL:ABE28977.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE28977.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE28977.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE28977.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Catalyzes the NAD(P)-dependent oxidation of 4-
CC       (phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-
CC       (phosphooxy)butyric acid which spontaneously decarboxylates to
CC       form 3-amino-2-oxopropyl phosphate (AHAP). {ECO:0000256|HAMAP-
CC       Rule:MF_00536, ECO:0000256|SAAS:SAAS01062167}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl
CC         phosphate + CO2 + NADH; Xref=Rhea:RHEA:32275, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57279, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58452; EC=1.1.1.262; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00536, ECO:0000256|SAAS:SAAS01115138};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00536};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00536};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00536};
CC       Note=Binds 1 divalent metal cation per subunit. Can use ions such
CC       as Zn(2+), Mg(2+) or Co(2+). {ECO:0000256|HAMAP-Rule:MF_00536};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate
CC       biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
CC       phosphate: step 4/5. {ECO:0000256|HAMAP-Rule:MF_00536,
CC       ECO:0000256|SAAS:SAAS00956575}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00536,
CC       ECO:0000256|SAAS:SAAS00956582}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00536,
CC       ECO:0000256|SAAS:SAAS00956573}.
CC   -!- MISCELLANEOUS: The active site is located at the dimer interface.
CC       {ECO:0000256|HAMAP-Rule:MF_00536}.
CC   -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00536, ECO:0000256|SAAS:SAAS00701249}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000270; ABE28977.1; -; Genomic_DNA.
DR   RefSeq; WP_011486803.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A4022; -.
DR   EnsemblBacteria; ABE28977; ABE28977; Bxe_A4022.
DR   GeneID; 4003385; -.
DR   KEGG; bxe:Bxe_A4022; -.
DR   PATRIC; fig|266265.5.peg.463; -.
DR   eggNOG; ENOG4105CEZ; Bacteria.
DR   eggNOG; COG1995; LUCA.
DR   HOGENOM; HOG000221592; -.
DR   KO; K00097; -.
DR   OMA; HKGVINE; -.
DR   OrthoDB; 1414545at2; -.
DR   BioCyc; BXEN266265:BXE_RS02200-MONOMER; -.
DR   UniPathway; UPA00244; UER00312.
DR   Proteomes; UP000001817; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050570; F:4-hydroxythreonine-4-phosphate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00536; PdxA; 1.
DR   InterPro; IPR037510; PdxA.
DR   InterPro; IPR005255; PdxA_fam.
DR   PANTHER; PTHR30004; PTHR30004; 1.
DR   Pfam; PF04166; PdxA; 1.
DR   TIGRFAMs; TIGR00557; pdxA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q145L2.
DR   SWISS-2DPAGE; Q145L2.
KW   Cobalt {ECO:0000256|HAMAP-Rule:MF_00536};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00536,
KW   ECO:0000256|SAAS:SAAS00956585};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00536};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00536,
KW   ECO:0000256|SAAS:SAAS00701256};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00536, ECO:0000256|SAAS:SAAS00701266};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00536, ECO:0000256|SAAS:SAAS00956572};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00536,
KW   ECO:0000256|SAAS:SAAS00701261, ECO:0000313|EMBL:ABE28977.1};
KW   Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00536,
KW   ECO:0000256|SAAS:SAAS00956552};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00536}.
FT   METAL       171    171       Divalent metal cation; shared with
FT                                dimeric partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   METAL       216    216       Divalent metal cation; shared with
FT                                dimeric partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   METAL       271    271       Divalent metal cation; shared with
FT                                dimeric partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   BINDING     138    138       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   BINDING     139    139       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   BINDING     279    279       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   BINDING     288    288       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   BINDING     297    297       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
SQ   SEQUENCE   336 AA;  35363 MW;  627A860277D3B45C CRC64;
     MTTAAQSVRP PLQIAITTGE PAGVGPELTA QALAGAAAHW PHAQFIVLGD ADLLAERARA
     VGVDWRALVA DGKRVRLQHR PLAAPAVAGK LNAANGRYVL DLLDSAIDAA VAGTFDAIVT
     APLQKSTIND AGVPFTGHTE YLAERTHTPR VVMMLAGTGK RPLRVALATT HLPLKDVSAA
     LSIEGILETL RIIDHDLRHH FGLPAPRILV TGLNPHAGEN GYLGREEIEV ITPALKLADA
     QGIDARGPYP ADTLFQPRYL EQADCVLAMF HDQGLPVLKY ATFGEGINVT LGLPIIRTSV
     DHGTALDLAG TGRADAGSLI AAIDTAVSMA QHRRAG
//

If you have problems or comments...

PBIL Back to PBIL home page