GenomeNet

Database: UniProt
Entry: D1C9L4_SPHTD
LinkDB: D1C9L4_SPHTD
Original site: D1C9L4_SPHTD 
ID   D1C9L4_SPHTD            Unreviewed;       356 AA.
AC   D1C9L4;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465};
DE            EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014};
DE   AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024};
GN   OrderedLocusNames=Sthe_3107 {ECO:0000313|EMBL:ACZ40507.1};
OS   Sphaerobacter thermophilus (strain DSM 20745 / S 6022).
OC   Bacteria; Thermomicrobiota; Thermomicrobia; Sphaerobacterales;
OC   Sphaerobacterineae; Sphaerobacteraceae; Sphaerobacter.
OX   NCBI_TaxID=479434 {ECO:0000313|EMBL:ACZ40507.1, ECO:0000313|Proteomes:UP000002027};
RN   [1] {ECO:0000313|Proteomes:UP000002027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49802 / DSM 20745 / S 6022
RC   {ECO:0000313|Proteomes:UP000002027};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., LaButti K.M., Clum A., Sun H.I., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F.,
RA   Hugenholtz P., Woyke T., Wu D., Steenblock K., Schneider S., Pukall R.,
RA   Goeker M., Klenk H.P., Eisen J.A.;
RT   "The complete chromosome 2 of Sphaerobacter thermophilus DSM 20745.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACZ40507.1, ECO:0000313|Proteomes:UP000002027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49802 / DSM 20745 / S 6022
RC   {ECO:0000313|Proteomes:UP000002027};
RX   PubMed=21304676;
RA   Spring S., Nolan M., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA   Cheng J.F., Lucas S., Land M., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Munk C., Kiss H., Chain P., Han C.,
RA   Brettin T., Detter J.C., Schuler E., Goker M., Rohde M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Desulfohalobium retbaense type strain
RT   (HR(100)).";
RL   Stand. Genomic Sci. 2:38-48(2010).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC       pantoic acid. {ECO:0000256|ARBA:ARBA00002919}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:16233, ChEBI:CHEBI:11561, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15980, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.169; Evidence={ECO:0000256|ARBA:ARBA00000784};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00004994}.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
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; CP001824; ACZ40507.1; -; Genomic_DNA.
DR   RefSeq; WP_012873542.1; NC_013524.1.
DR   AlphaFoldDB; D1C9L4; -.
DR   STRING; 479434.Sthe_3107; -.
DR   KEGG; sti:Sthe_3107; -.
DR   eggNOG; COG1893; Bacteria.
DR   HOGENOM; CLU_031468_0_0_0; -.
DR   InParanoid; D1C9L4; -.
DR   OMA; CAQNGVE; -.
DR   OrthoDB; 9796561at2; -.
DR   Proteomes; UP000002027; Chromosome 2.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR003710; ApbA.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00745; apbA_panE; 1.
DR   PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ACZ40507.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002027};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          13..158
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          187..325
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   356 AA;  36630 MW;  3F4B61D0E753C2CD CRC64;
     MPTEPVASLP PTLIYGAGAV GCLLGGVLAA ADAPVTLLGR PAVAEAVNEQ GLTIVQPSST
     RRIRIPAVTS IDAISAPPAL VLLTVKAYAV AAALPDLRRL AASGAAIVAL QNGVGTVETL
     LAEPDMPRLA SGTITASVMR DSPATVRQET TGGVMLAPVR GGVPLDQLAA ALTATGLPAG
     VVPRYQDLTW SKLLLNIMAN ATSALLALPP AAIYADPRLF AVERAAFIEA LAVMLGAGIR
     PIPLPGFNVP LLAHAMRLPA PLARRLIAAR AARGRGEKRP SLWLDIERGL GTTEVRWLNG
     AVADLGARLG IPTPVNATLT ELLEEAARNP ERRRAFAGRP DALLAALGRT SGTAQA
//
DBGET integrated database retrieval system