ID A0A897NW55_9EURY Unreviewed; 296 AA.
AC A0A897NW55;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 02-APR-2025, entry version 17.
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 Name=apbA {ECO:0000313|EMBL:QSG14899.1};
GN ORFNames=HSEST_1367 {ECO:0000313|EMBL:QSG14899.1};
OS Halapricum desulfuricans.
OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC Halobacteria; Halobacteriales; Haloarculaceae; Halapricum.
OX NCBI_TaxID=2841257 {ECO:0000313|EMBL:QSG14899.1, ECO:0000313|Proteomes:UP000663292};
RN [1] {ECO:0000313|EMBL:QSG14899.1, ECO:0000313|Proteomes:UP000663292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HSR-Est {ECO:0000313|EMBL:QSG14899.1,
RC ECO:0000313|Proteomes:UP000663292};
RA Sorokin D.Y., Messina E., Smedile F., La Cono V., Hallsworth J.E.,
RA Yakimov M.M.;
RT "Carbohydrate-dependent, anaerobic sulfur respiration: A novel catabolism
RT in halophilic archaea.";
RL Submitted (NOV-2020) to the EMBL/GenBank/DDBJ databases.
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 + NADH + H(+);
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:ARBA00048196};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:61294;
CC Evidence={ECO:0000256|ARBA:ARBA00048196};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantoate + NADP(+) = 2-dehydropantoate + NADPH + H(+);
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:ARBA00047506};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16235;
CC Evidence={ECO:0000256|ARBA:ARBA00047506};
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; CP064791; QSG14899.1; -; Genomic_DNA.
DR RefSeq; WP_229122946.1; NZ_CP064791.1.
DR AlphaFoldDB; A0A897NW55; -.
DR GeneID; 68858006; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000663292; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
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; IPR003710; ApbA.
DR InterPro; IPR050838; Ketopantoate_reductase.
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:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR43765; 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};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000663292}.
FT DOMAIN 3..142
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 171..286
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 296 AA; 30551 MW; 4AAFBDE4BE5CB0E9 CRC64;
MRILVFGAGS LGSLIGGLLA ATHDVTLVGR EPHVSTVRDQ GLEITGEIET TTYPDADTTV
PDSAELAIVT VKSYDTGEAA QALRAADPDV VLSLQNGLGN EESLSEPLDG AVLAGTCTYG
ARLVEPGIVG CTGVGTVTLG ARGGGDSAVA ERTAGAFESA DVDTTVAADM PRRLWEKLAI
NAGINAITAL ARVENGALAE GAAGDVAARA AAETARVARD SGVELPDERA IDRLEAVVET
TAPNRSSMYQ DLEAGQRTEI DAINGAVCER ASEPVPINET LTALIETWER GRNLRS
//
