ID A0A347ZSX0_9CHLR Unreviewed; 346 AA.
AC A0A347ZSX0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 02-APR-2025, entry version 21.
DE SubName: Full=Ketopantoate reductase {ECO:0000313|EMBL:REG11024.1};
GN ORFNames=DFR64_0896 {ECO:0000313|EMBL:REG11024.1};
OS Pelolinea submarina.
OC Bacteria; Bacillati; Chloroflexota; Anaerolineae; Anaerolineales;
OC Anaerolineaceae; Pelolinea.
OX NCBI_TaxID=913107 {ECO:0000313|EMBL:REG11024.1, ECO:0000313|Proteomes:UP000256388};
RN [1] {ECO:0000313|EMBL:REG11024.1, ECO:0000313|Proteomes:UP000256388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23923 {ECO:0000313|EMBL:REG11024.1,
RC ECO:0000313|Proteomes:UP000256388};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:REG11024.1}.
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; QUMS01000001; REG11024.1; -; Genomic_DNA.
DR RefSeq; WP_116224173.1; NZ_AP018437.1.
DR AlphaFoldDB; A0A347ZSX0; -.
DR OrthoDB; 9796561at2; -.
DR Proteomes; UP000256388; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
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; IPR013752; KPA_reductase.
DR InterPro; IPR051402; KPR-Related.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR21708:SF26; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000256388};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..346
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030063624"
FT DOMAIN 4..145
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 176..316
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 346 AA; 37999 MW; CA2DB8901AA3AE8A CRC64;
MKVLCIGAGA IGLLAGGSAA AQGAAVTFLV KPGQESKLAG REIHIQNQTQ NWQVSDFTVV
SSLKDLDRDE VFDAIFIAVK TFDTESVISQ LEKAMINFRS ILCLQNGVEN EDKFRIAFPR
AEIVAASVVS AVSRLDDTSI RVEKNRGIGL SGKDEYVQPV FAILKNAGLK PQIFADMRSM
KWSKMLSNLF SNAVSGILDM SPNEVYSHKE LFRIEKAQIL ETASVMRRSG LKIENLPGLP
LRPLITIMRI TPDVLLQPLL KKMVAGGRGE KMPSFYIEKM KGSSRSEVND LNGAVVRKGE
ALSVPTPINR ALTETFNLIL KDAKARQAFS RHPEKLVETT AAVNRI
//
