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Database: UniProt
Entry: A0A0V7ZXM8_9CYAN
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Original site: A0A0V7ZXM8_9CYAN 
ID   A0A0V7ZXM8_9CYAN        Unreviewed;       337 AA.
AC   A0A0V7ZXM8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|RuleBase:RU362068};
DE            EC=1.1.1.169 {ECO:0000256|RuleBase:RU362068};
DE   AltName: Full=Ketopantoate reductase {ECO:0000256|RuleBase:RU362068};
GN   ORFNames=BC008_03205 {ECO:0000313|EMBL:KST69211.1}, BC008_14805
GN   {ECO:0000313|EMBL:KST63725.1};
OS   Mastigocoleus testarum BC008.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC   Mastigocoleus.
OX   NCBI_TaxID=371196 {ECO:0000313|EMBL:KST69211.1, ECO:0000313|Proteomes:UP000053372};
RN   [1] {ECO:0000313|EMBL:KST69211.1, ECO:0000313|Proteomes:UP000053372}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC008 {ECO:0000313|EMBL:KST69211.1,
RC   ECO:0000313|Proteomes:UP000053372};
RA   Guida B.S., Garcia-Pichel F.;
RT   "Draft Genome of the Euendolithic (true boring) Cyanobacterium
RT   Mastigocoleus testarum strain BC008.";
RL   Genome Announc. 0:0-0(2015).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC       pantoic acid. {ECO:0000256|RuleBase:RU362068}.
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|RuleBase:RU362068};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC       {ECO:0000256|RuleBase:RU362068}.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870, ECO:0000256|RuleBase:RU362068}.
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:KST69211.1}.
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DR   EMBL; LMTZ01000133; KST63725.1; -; Genomic_DNA.
DR   EMBL; LMTZ01000032; KST69211.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V7ZXM8; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000053372; Unassembled WGS sequence.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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   3: Inferred from homology;
KW   NADP {ECO:0000256|RuleBase:RU362068};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053372}.
FT   DOMAIN          17..174
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          205..326
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   337 AA;  37613 MW;  C3A4148FAF662AF9 CRC64;
     MSSAALNFFN VTKNLTYAIL GTGALGGFYG AKLQQAGLEV HFLVRSDYES VRRNGLFVES
     VDGDFRLNRV NAYCDVRNMP ACDVAIVALK TTQNHLLPDI LLPILKENST VLVLQNGLGI
     EEEVAAIIDR YKVSGHKIGE TKIIGGLCFL CSNKVGDGHI RHLAYGKINL GEHKNNSQHG
     GIADEMQIIA NDFESAGIPI ELSSDLLLAR WKKLVWNIPY NGLSVVLDAT TEELMTNPNS
     LELVKELMHE VLRGAKSVEC DIPLEFIETM LEHTRNMHPY RTSMKIDYDE KRPLELTAIF
     SNALQAAFSR GVNLPKIRCL YQQLQFLDLR NRTNAVK
//
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