ID A2BTX5_PROM5 Unreviewed; 346 AA.
AC A2BTX5;
DT 20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 20-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Putative pyridoxal phosphate biosynthetic protein PdxA {ECO:0000313|EMBL:ABM71236.1};
DE EC=1.1.1.262 {ECO:0000313|EMBL:ABM71236.1};
GN Name=pdxA {ECO:0000313|EMBL:ABM71236.1};
GN OrderedLocusNames=P9515_00271 {ECO:0000313|EMBL:ABM71236.1};
OS Prochlorococcus marinus (strain MIT 9515).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=167542 {ECO:0000313|EMBL:ABM71236.1, ECO:0000313|Proteomes:UP000001589};
RN [1] {ECO:0000313|EMBL:ABM71236.1, ECO:0000313|Proteomes:UP000001589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9515 {ECO:0000313|EMBL:ABM71236.1,
RC ECO:0000313|Proteomes:UP000001589};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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DR EMBL; CP000552; ABM71236.1; -; Genomic_DNA.
DR RefSeq; WP_011819353.1; NC_008817.1.
DR AlphaFoldDB; A2BTX5; -.
DR STRING; 167542.P9515_00271; -.
DR GeneID; 60201167; -.
DR KEGG; pmc:P9515_00271; -.
DR eggNOG; COG1995; Bacteria.
DR HOGENOM; CLU_040168_0_0_3; -.
DR OrthoDB; 9801783at2; -.
DR Proteomes; UP000001589; Chromosome.
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 Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR005255; PdxA_fam.
DR NCBIfam; TIGR00557; pdxA; 1.
DR PANTHER; PTHR30004; 4-HYDROXYTHREONINE-4-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR30004:SF6; D-THREONATE 4-PHOSPHATE DEHYDROGENASE; 1.
DR Pfam; PF04166; PdxA; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABM71236.1}.
SQ SEQUENCE 346 AA; 38152 MW; 6FCECC2B57ACB495 CRC64;
MSNKRNTIDD RLKVIISVGD DSGIGPEIIL KALSSKEIPN NIDTLIVGSK INLKNTYKKL
KSLGVQNIVD PSNYQIHDIE IPFEINKPKQ SNGNSSFFYL KKAIEIVQKY RNAALVTGPI
CKKSWALAGH NYSGQTELLA ESCQVNNFGM LFTAKSPITN WRFNTLLATT HIPLCEVPKQ
LSTKLIHSKL NLLATFCKNY VEKPILKIAG LNPHAGEEGI LGSEEHDWIN DAVNSWSEQN
KDVHLLGPIS PDTCWNSSAK AWREDKAPTH NGILAMYHDQ GLIPIKVIAL NYSVNTTLGL
PFIRTSPDHG TGFDIAGKGI AQSQSMVEAI KTAIDLTKGS RLFNAH
//
