PDXAL_RHIME
ID PDXAL_RHIME Reviewed; 348 AA.
AC Q92TP3;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Putative 4-hydroxythreonine-4-phosphate dehydrogenase 2 {ECO:0000250|UniProtKB:P19624};
DE EC=1.1.1.262 {ECO:0000250|UniProtKB:P19624};
DE AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase 2 {ECO:0000250|UniProtKB:P19624};
GN OrderedLocusNames=RB1464; ORFNames=SMb20772;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymB (megaplasmid 2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481431; DOI=10.1073/pnas.161294698;
RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT endosymbiont Sinorhizobium meliloti.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
CC -!- FUNCTION: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-
CC threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which
CC spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate
CC (AHAP). {ECO:0000250|UniProtKB:P19624}.
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;
CC Evidence={ECO:0000250|UniProtKB:P19624};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P19624};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P19624};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:P19624};
CC Note=Binds 1 divalent metal cation per subunit. Can use ions such as
CC Zn(2+), Mg(2+) or Co(2+). {ECO:0000250|UniProtKB:P19624};
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
CC {ECO:0000250|UniProtKB:P19624}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P19624}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P19624}.
CC -!- MISCELLANEOUS: The active site is located at the dimer interface.
CC {ECO:0000250|UniProtKB:P19624}.
CC -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000305}.
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DR EMBL; AL591985; CAC49864.1; -; Genomic_DNA.
DR PIR; H96024; H96024.
DR RefSeq; NP_438004.1; NC_003078.1.
DR RefSeq; WP_010976261.1; NC_003078.1.
DR AlphaFoldDB; Q92TP3; -.
DR SMR; Q92TP3; -.
DR STRING; 266834.SM_b20772; -.
DR PRIDE; Q92TP3; -.
DR EnsemblBacteria; CAC49864; CAC49864; SM_b20772.
DR GeneID; 25013369; -.
DR GeneID; 61601373; -.
DR KEGG; sme:SM_b20772; -.
DR PATRIC; fig|266834.11.peg.6391; -.
DR eggNOG; COG1995; Bacteria.
DR HOGENOM; CLU_040168_0_1_5; -.
DR OMA; CGREEID; -.
DR UniPathway; UPA00244; UER00312.
DR PRO; PR:Q92TP3; -.
DR Proteomes; UP000001976; Plasmid pSymB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050570; F:4-hydroxythreonine-4-phosphate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR005255; PdxA_fam.
DR PANTHER; PTHR30004; PTHR30004; 1.
DR Pfam; PF04166; PdxA; 1.
PE 3: Inferred from homology;
KW Cobalt; Cytoplasm; Magnesium; Metal-binding; NAD; NADP; Oxidoreductase;
KW Plasmid; Pyridoxine biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..348
FT /note="Putative 4-hydroxythreonine-4-phosphate
FT dehydrogenase 2"
FT /id="PRO_0000188823"
FT BINDING 180
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 224
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 279
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P19624"
SQ SEQUENCE 348 AA; 36868 MW; 76F1B36A1AD334A2 CRC64;
MTTSGADGTK ERRPVIALAM GDPAGISPEL TARLLALSDI RDAAHIIAIG DRRILDEGAR
VAGVTLDLEA ASLDALDNAG TARHVFVDLA HLDPADVVRG EATLAGGTFA TRNFRTALEL
AHAGKADAVC FTPFNKKAMR FAYPGYDDEI RFVADVLSFT GKVREFNVLE KVWNARVTSH
IPLKDVASHL SVEAILAELK LTQACLKDAG YEEAKIAVAG LNPHAGDGGS FGMEEIDIIE
PAVEKARALG FNVEGPFPAD TVFLRALKEG FNAVMTMYHD QGQIAMKIIG FDKGVTMMGG
LPFPLCTPAH GTAYDIAGKG IADIGATREA ILLAARMAKK KRALSAAA
