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Database: UniProt
Entry: A0A135VFX3_9ARCH
LinkDB: A0A135VFX3_9ARCH
Original site: A0A135VFX3_9ARCH 
ID   A0A135VFX3_9ARCH        Unreviewed;       329 AA.
AC   A0A135VFX3;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-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=AM324_08395 {ECO:0000313|EMBL:KXH71550.1};
OS   Candidatus Thorarchaeota archaeon SMTZ1-83.
OC   Archaea; Asgard group; Candidatus Thorarchaeota.
OX   NCBI_TaxID=1706445 {ECO:0000313|EMBL:KXH71550.1, ECO:0000313|Proteomes:UP000070043};
RN   [1] {ECO:0000313|EMBL:KXH71550.1, ECO:0000313|Proteomes:UP000070043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMTZ1-83 {ECO:0000313|EMBL:KXH71550.1};
RX   PubMed=26824177;
RA   Seitz K.W., Lazar C.S., Hinrichs K.U., Teske A.P., Baker B.J.;
RT   "Genomic reconstruction of a novel, deeply branched sediment archaeal
RT   phylum with pathways for acetogenesis and sulfur reduction.";
RL   ISME J. 0:0-0(2016).
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}.
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:KXH71550.1}.
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DR   EMBL; LRSK01000225; KXH71550.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135VFX3; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000070043; Unassembled WGS sequence.
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; 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   Coenzyme A biosynthesis {ECO:0000256|RuleBase:RU362068};
KW   NADP {ECO:0000256|RuleBase:RU362068};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362068}.
FT   DOMAIN          3..150
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          177..301
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   329 AA;  35412 MW;  59BDEDA5E177462B CRC64;
     MRIVIMGSGA IGCLYGGFLS KAGEDVRLLV GRHPIVDAIN NRGLRIKGVL GDHLLRLNAT
     QNAKEIDEAD LVLITTKAYD SEEAAKRIKH LTDKGAYVLV LQNGIGTEKK VAEVLGTRRV
     LRATTCMGAI MTGPGEVTVT GCGITEIGSH YSENMKTVEK VVSILRNAGF DVRSSENIEG
     VVWTKTIVNC GINPIGALTG MTNGEIYNDA RLRSLVVKLV QEAVEVATAI GVSLTADDPI
     RYALGTAKAT GDNINSMLQD IQQCKQTEID AITGEVVRLA REHDIETPYS DSVYSLVKAL
     ESKVVKMDAD DPKVIPYSAE EVERAISNV
//
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