ID E4TJ78_CALNY Unreviewed; 442 AA.
AC E4TJ78;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=2-dehydropantoate 2-reductase {ECO:0000313|EMBL:ADR18114.1};
GN OrderedLocusNames=Calni_0201 {ECO:0000313|EMBL:ADR18114.1};
OS Calditerrivibrio nitroreducens (strain DSM 19672 / NBRC 101217 / Yu37-1).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Calditerrivibrionaceae.
OX NCBI_TaxID=768670 {ECO:0000313|EMBL:ADR18114.1, ECO:0000313|Proteomes:UP000007039};
RN [1] {ECO:0000313|EMBL:ADR18114.1, ECO:0000313|Proteomes:UP000007039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19672 / NBRC 101217 / Yu37-1
RC {ECO:0000313|Proteomes:UP000007039};
RX PubMed=21475587; DOI=10.4056/sigs.1523807;
RA Pitluck S., Sikorski J., Zeytun A., Lapidus A., Nolan M., Lucas S.,
RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L.,
RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A., Chen A.,
RA Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Brambilla E., Djao O.D., Rohde M., Spring S., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Land M.;
RT "Complete genome sequence of Calditerrivibrio nitroreducens type strain
RT (Yu37-1).";
RL Stand. Genomic Sci. 4:54-62(2011).
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870}.
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DR EMBL; CP002347; ADR18114.1; -; Genomic_DNA.
DR RefSeq; WP_013450331.1; NC_014758.1.
DR AlphaFoldDB; E4TJ78; -.
DR STRING; 768670.Calni_0201; -.
DR KEGG; cni:Calni_0201; -.
DR eggNOG; COG1051; Bacteria.
DR eggNOG; COG1893; Bacteria.
DR HOGENOM; CLU_031468_6_0_0; -.
DR Proteomes; UP000007039; Chromosome.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 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 InterPro; IPR020476; Nudix_hydrolase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
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 Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000007039}.
FT DOMAIN 306..432
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 442 AA; 49581 MW; CA5DE710CD9D0AD7 CRC64;
MKMLCFGAGA VGSLFCGLMA NKGYDIDFIA RGEHLKKLQD NGTLSINSYR YGDIVVPIKA
FATPQSQYDI VFIAVKSQDT ANACSTIKSF IKPESIIVSM QNGIDNPSII ASLLPDHKVV
AASVFVGSSV DTPGHVTHSA DGRIILGAFT SNVSANDLQN IKMIFDRIDV PCVISDDIKL
VMWKKLLWNL IFNPLSALLE ATCGKLVEND YSRHLMQKML EEGYLAAKRD GVEIPQDYLD
KIMDVKGNLY NYKTSMLQDI QKLKIPEVDG IMLPVINRLK DTTPAAYTET IYNLLKYKYG
KKYIYTPKLT VDMIVYNSNN EILLIERKNP PYGWAIPGGF VDYGETVENA AKRELEEETG
ITVDKFEMLG VYSDPTRDSR FHTVSIVYYT FSDDAPKAAD DAKDAKFFNL NKLPENIAFD
HKKIIEDFKH ILKKRRSDGP KS
//
