ID A0A0B2JZT2_9FIRM Unreviewed; 350 AA.
AC A0A0B2JZT2;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000313|EMBL:KHM51467.1};
GN ORFNames=NZ47_10370 {ECO:0000313|EMBL:KHM51467.1};
OS Anaerovibrio lipolyticus.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Anaerovibrio.
OX NCBI_TaxID=82374 {ECO:0000313|EMBL:KHM51467.1, ECO:0000313|Proteomes:UP000030993};
RN [1] {ECO:0000313|EMBL:KHM51467.1, ECO:0000313|Proteomes:UP000030993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5S {ECO:0000313|EMBL:KHM51467.1,
RC ECO:0000313|Proteomes:UP000030993};
RX PubMed=23950883;
RA Prive F., Kaderbhai N.N., Girdwood S., Worgan H.J., Pinloche E.,
RA Scollan N.D., Huws S.A., Newbold C.J.;
RT "Identification and characterization of three novel lipases belonging to
RT families II and V from Anaerovibrio lipolyticus 5ST.";
RL PLoS ONE 8:E69076-E69076(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHM51467.1}.
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DR EMBL; JSCE01000195; KHM51467.1; -; Genomic_DNA.
DR RefSeq; WP_039210281.1; NZ_JSCE01000195.1.
DR AlphaFoldDB; A0A0B2JZT2; -.
DR STRING; 82374.NZ47_10370; -.
DR Proteomes; UP000030993; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000030993}.
SQ SEQUENCE 350 AA; 37757 MW; 7ECE39FFB6E349D5 CRC64;
MSKLPILAIT SGDPAGSGPE ITIKAFLNGN IHNICRPLVI GDTCVLKQAI NFVGAEDKLQ
INTIHDISEA QFAPNVIDVY DIGLIRDYNS IGVGTINAIA GEAAFNYVIT AIDLAMRNIV
DGTITNAISK EAINLAGHHY SGHTEIYAEY THTKKYCMML AHNDFRVAHV STHVSLREAC
DLCKKDRVLE VIGLANQACL AVDIKQPKVA VAGLNPHCGE HGLFGNEEID EIIPAIEAAK
ELGINAIGPC PPDTVFSQAI GGWYDIVVCM YHDQGHIPTK VQGFVYNREK QQWNSVAGVN
ITLGLPIVRV SVDHGTAYDH AGKGDANELS LVNAIEYGAK LSSNRHNKGE
//
