ID A0A0S8B4G8_9CHLR Unreviewed; 354 AA.
AC A0A0S8B4G8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMJ56_14900 {ECO:0000313|EMBL:KPK06148.1};
OS Anaerolineae bacterium SG8_19.
OC Bacteria; Chloroflexota; Anaerolineae.
OX NCBI_TaxID=1703386 {ECO:0000313|EMBL:KPK06148.1, ECO:0000313|Proteomes:UP000050892};
RN [1] {ECO:0000313|EMBL:KPK06148.1, ECO:0000313|Proteomes:UP000050892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_19 {ECO:0000313|EMBL:KPK06148.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK06148.1}.
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DR EMBL; LJNN01000213; KPK06148.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8B4G8; -.
DR PATRIC; fig|1703386.3.peg.644; -.
DR Proteomes; UP000050892; Unassembled WGS sequence.
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 3..142
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 180..319
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 354 AA; 38815 MW; 4731943554265B47 CRC64;
MEVLVLGAGA VGCYLGGQLA RSGHKVTLVS RRPTAEAIKR NGLTIIEGEK QYRTKPVIVS
ALREAFQNDS HFDLILLTVK AYDAQAALYE MVAFCPTVPK VITMQNGIGI EEIFIDEFTP
ERIVAGSLTT PLSHETANSV IVERSDRGLA LAPAQPGTDI STWAALFQQA GIETISLNDY
RSMKWSKALL NMVGNATSAI LNRHPKLVYN YGPTYDLEME MLKESLAVMK AQKLKTIDLP
GVQPNRLAVA VNRLPKSLVK PILTNIVTSG RGNKMPSFHI DLMAGREQNE VTYHNGAVAQ
AGEALGIPTP VNEALNDILV KIAHGEIDYE VFNGRPKRLV AEVQKYKKAR KKKK
//