ID   W1WTV3_9ZZZZ            Unreviewed;       300 AA.
AC   W1WTV3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=2-dehydropantoate 2-reductase {ECO:0000313|EMBL:ETJ21311.1};
GN   ORFNames=Q604_UNBC18341G0011 {ECO:0000313|EMBL:ETJ21311.1};
OS   human gut metagenome.
OC   unclassified sequences; metagenomes; organismal metagenomes.
OX   NCBI_TaxID=408170 {ECO:0000313|EMBL:ETJ21311.1};
RN   [1] {ECO:0000313|EMBL:ETJ21311.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Brown C.T., Sharon I., Thomas B.C., Castelle C.J., Morowitz M.J.,
RA   Banfield J.F.;
RT   "A Varibaculum cambriense genome reconstructed from a premature infant gut
RT   community with otherwise low bacterial novelty that shifts toward anaerobic
RT   metabolism during the third week of life.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
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:ETJ21311.1}.
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DR   EMBL; AZMM01018341; ETJ21311.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1WTV3; -.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:InterPro.
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;
FT   DOMAIN          14..147
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          170..291
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   300 AA;  34470 MW;  2CB4EA9F2D194320 CRC64;
     MNRKKKGKNK VMTIAIIGPG AVGTTLAFEL KKVLPDTELI GRQDKLMTYF PENTSNGSDV
     KVTSFNHINQ TFDVIIIAVK THQLDDVIKQ LPKITHDDSL IILAQNGYGQ LNKLPYQHVF
     QAVVYISGQK VNNNVQHFRD YQLYIQDSTL TRQFKQMVHP SKIEVVLQEN IEKSIWYKLL
     VNLGINTITA IGQQPAKILK SPHIESLCRR ILVDGLKVAR AEQIDFEDHI VDDILNIYKG
     YPDEMGTSMY YDVINKHPLE VEAIQGYIYK CAKKHHLETP YLDMAYTFLY AYHLEYTQPD
//