ID A0A8J2TXZ6_9MICO Unreviewed; 304 AA.
AC A0A8J2TXZ6;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 18-JUN-2025, entry version 17.
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=GCM10011333_15780 {ECO:0000313|EMBL:GGA13698.1};
OS Sediminivirga luteola.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC Brevibacteriaceae; Sediminivirga.
OX NCBI_TaxID=1774748 {ECO:0000313|EMBL:GGA13698.1, ECO:0000313|Proteomes:UP000616114};
RN [1] {ECO:0000313|EMBL:GGA13698.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.12785 {ECO:0000313|EMBL:GGA13698.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [2] {ECO:0000313|EMBL:GGA13698.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.12785 {ECO:0000313|EMBL:GGA13698.1};
RA Sun Q., Zhou Y.;
RL Submitted (SEP-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 + 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|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:GGA13698.1}.
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DR EMBL; BMFY01000006; GGA13698.1; -; Genomic_DNA.
DR RefSeq; WP_188550395.1; NZ_BMFY01000006.1.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000616114; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:InterPro.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
DR FunFam; 1.10.1040.10:FF:000017; 2-dehydropantoate 2-reductase; 1.
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; IPR013752; KPA_reductase.
DR InterPro; IPR051402; KPR-Related.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR00745; apbA_panE; 1.
DR NCBIfam; NF005091; PRK06522.2-2; 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|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000616114}.
FT DOMAIN 11..148
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 174..296
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 304 AA; 31992 MW; F4CA126391845072 CRC64;
MGTTASGRPL AVIGAGAIGL ALAAAFARGG REVIVCGGTR FERIEVTEAG AVEQWPVRHA
ETPGDLAEAD TAVLAVKAHH TEAAATWLRA LARPEVRLLV AQNGVEHRER VAPYAGPAQI
VPAIVYLNVE RSAPGRALVR HAGTRDLALP DEDAARDLAP ELAAGGLRVE LETDLRTVAW
AKLLTNITLN PLTALTGRRV DVVRDPGVGG IALQLMLEAA QVARAEGAQL GPDDAHAALT
WLENVPAGAP TSMLQDLLAG RPLEYDALTG AVIRAAERHG IEVPVNRMVL ALLAAIRPEE
LHTR
//
