ID A4ITC1_GEOTN Unreviewed; 331 AA.
AC A4ITC1;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Pyridoxal phosphate biosynthesis {ECO:0000313|EMBL:ABO68575.1};
GN OrderedLocusNames=GTNG_3232 {ECO:0000313|EMBL:ABO68575.1};
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246 {ECO:0000313|EMBL:ABO68575.1, ECO:0000313|Proteomes:UP000001578};
RN [1] {ECO:0000313|EMBL:ABO68575.1, ECO:0000313|Proteomes:UP000001578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2 {ECO:0000313|EMBL:ABO68575.1,
RC ECO:0000313|Proteomes:UP000001578};
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968};
CC -!- SIMILARITY: Belongs to the PdxA family. PdxA2 subfamily.
CC {ECO:0000256|ARBA:ARBA00009464}.
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DR EMBL; CP000557; ABO68575.1; -; Genomic_DNA.
DR RefSeq; WP_011888339.1; NC_009328.1.
DR AlphaFoldDB; A4ITC1; -.
DR KEGG; gtn:GTNG_3232; -.
DR eggNOG; COG1995; Bacteria.
DR HOGENOM; CLU_040168_0_1_9; -.
DR Proteomes; UP000001578; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ SEQUENCE 331 AA; 35469 MW; C5BC35C5BC294594 CRC64;
MKPTIGITMG DAAGVGPEII VKALQNSSIY EQCHPLVIGD AKILERAVRI TNAGLTVRPI
SDIAEADYRY GMIDCLHLDL LPVDLPFGQV SAAAGDAAFQ FLKRAIELAQ NGEIDAICTA
PLNKEAMHKG GHLYPGHTEI LADLTGTEDY AMMLSSPQLK VIHLTTHVGL IQAIEMINPE
RTYKVIKLAH DTLTRAGKEH PSIAVCGINP HAGENGLFGN GEEEEKLIPA IHKAQAEGIN
VTGPYPADTL FYRAVRGDFD IVVACYHDQG HAPIKVLGLE AGVNITVGLK GGIIRTSVDH
GTAFDIAGKN LADERSMLEA IRVAVELAPK R
//
