ID C7NUS2_HALUD Unreviewed; 294 AA.
AC C7NUS2;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00013014, ECO:0000256|RuleBase:RU362068};
DE EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014, ECO:0000256|RuleBase:RU362068};
DE AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024, ECO:0000256|RuleBase:RU362068};
GN OrderedLocusNames=Huta_0902 {ECO:0000313|EMBL:ACV11085.1};
OS Halorhabdus utahensis (strain DSM 12940 / JCM 11049 / AX-2).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halorhabdus.
OX NCBI_TaxID=519442 {ECO:0000313|EMBL:ACV11085.1, ECO:0000313|Proteomes:UP000002071};
RN [1] {ECO:0000313|EMBL:ACV11085.1, ECO:0000313|Proteomes:UP000002071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12940 / JCM 11049 / AX-2
RC {ECO:0000313|Proteomes:UP000002071};
RX PubMed=21304660; DOI=10.4056/sigs.31864;
RA Anderson I., Tindall B.J., Pomrenke H., Goker M., Lapidus A., Nolan M.,
RA Copeland A., Glavina Del Rio T., Chen F., Tice H., Cheng J.F., Lucas S.,
RA Chertkov O., Bruce D., Brettin T., Detter J.C., Han C., Goodwin L.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Pitluck S., Pati A.,
RA Mavromatis K., Ivanova N., Ovchinnikova G., Chen A., Palaniappan K.,
RA Chain P., Rohde M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Halorhabdus utahensis type strain (AX-2).";
RL Stand. Genomic Sci. 1:218-225(2009).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000256|RuleBase:RU362068}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantoate + NAD(+) = 2-dehydropantoate + H(+) + NADH;
CC Xref=Rhea:RHEA:61292, ChEBI:CHEBI:11561, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15980, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000256|ARBA:ARBA00000108};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:61294;
CC Evidence={ECO:0000256|ARBA:ARBA00000108};
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:ARBA00000825};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16235;
CC Evidence={ECO:0000256|ARBA:ARBA00000825};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004724, ECO:0000256|RuleBase:RU362068}.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870, ECO:0000256|RuleBase:RU362068}.
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DR EMBL; CP001687; ACV11085.1; -; Genomic_DNA.
DR RefSeq; WP_015788662.1; NC_013158.1.
DR AlphaFoldDB; C7NUS2; -.
DR STRING; 519442.Huta_0902; -.
DR GeneID; 8383175; -.
DR KEGG; hut:Huta_0902; -.
DR eggNOG; arCOG04139; Archaea.
DR HOGENOM; CLU_031468_0_0_2; -.
DR OrthoDB; 201845at2157; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000002071; Chromosome.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniPathway.
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 Coenzyme A biosynthesis {ECO:0000256|ARBA:ARBA00022993,
KW ECO:0000256|RuleBase:RU362068}; NADP {ECO:0000256|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362068,
KW ECO:0000313|EMBL:ACV11085.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002071}.
FT DOMAIN 3..142
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 169..285
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 294 AA; 30527 MW; FCDA3465A232B956 CRC64;
MDVVVFGAGS LGSLIGGLLA REHVVTLVGR EDHVHAVQED GLRITGEIQA VVRPRASKTV
SGAADLAIVT VKSYDTPAAV EALSGCDCDA VLSLQNGMGN EERLASLVAT VLAGTATYGA
LQDEPGSVRC TGIGEIVLGP PDGGQSTIAD RIGEAFSTAG IETTVAADMP RRRWEKLAVN
AGINATTALS RVPNGALSDG PLSDVARRAA RETARVARDH GVDLPDEAAI AALESVVDAT
ADNESSMYRD VQSGRRTEVE AINGYVADSD VETPVNETLA ALLRGWERES KLGK
//
