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Database: UniProt
Entry: D2RJC2_ACIFV
LinkDB: D2RJC2_ACIFV
Original site: D2RJC2_ACIFV 
ID   D2RJC2_ACIFV            Unreviewed;       462 AA.
AC   D2RJC2;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase NAD-binding protein {ECO:0000313|EMBL:ADB47174.1};
GN   OrderedLocusNames=Acfer_0786 {ECO:0000313|EMBL:ADB47174.1};
OS   Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / CCUG 9996 / CIP
OS   106432 / VR4).
OC   Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC   Acidaminococcus.
OX   NCBI_TaxID=591001 {ECO:0000313|EMBL:ADB47174.1, ECO:0000313|Proteomes:UP000001902};
RN   [1] {ECO:0000313|EMBL:ADB47174.1, ECO:0000313|Proteomes:UP000001902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25085 / DSM 20731 / CCUG 9996 / CIP 106432 / VR4
RC   {ECO:0000313|Proteomes:UP000001902};
RX   PubMed=21304687; DOI=10.4056/sigs.1002553;
RA   Chang Y.J., Pukall R., Saunders E., Lapidus A., Copeland A., Nolan M.,
RA   Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Han C.,
RA   Detter J.C., Bruce D., Goodwin L., Pitluck S., Mikhailova N., Liolios K.,
RA   Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Acidaminococcus fermentans type strain
RT   (VR4).";
RL   Stand. Genomic Sci. 3:1-14(2010).
CC   -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009463}.
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DR   EMBL; CP001859; ADB47174.1; -; Genomic_DNA.
DR   RefSeq; WP_012938163.1; NZ_CP085936.1.
DR   AlphaFoldDB; D2RJC2; -.
DR   STRING; 591001.Acfer_0786; -.
DR   GeneID; 78335898; -.
DR   KEGG; afn:Acfer_0786; -.
DR   eggNOG; COG1051; Bacteria.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_591383_0_0_9; -.
DR   OrthoDB; 9815331at2; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000001902; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0019605; P:butyrate metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0044248; P:cellular catabolic process; IEA:UniProt.
DR   GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR   CDD; cd02883; Nudix_Hydrolase; 1.
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; IPR006180; 3-OHacyl-CoA_DH_CS.
DR   InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR   InterPro; IPR006108; 3HC_DH_C.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
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   PANTHER; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR48075:SF1; LAMBDA-CRYSTALLIN HOMOLOG; 1.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 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; PS00067; 3HCDH; 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:UP000001902}.
FT   DOMAIN          29..168
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
SQ   SEQUENCE   462 AA;  51793 MW;  00E40992BA9A3F23 CRC64;
     MEYWDIYDSS KQVTGRKMVR NDWHMKPGDY HLTVLALIRD AAGRILITQR KGDKEWAPLK
     WEIPGGGVRA GETSQEAVLR EVAEETGLHF TPEQGRCIHT YRSDSPAEQN NYFVDIYEFR
     GIFMPEQVKI QEDEVESFRL ATPGEIRQLG KQDDFLHFQR IEGLLTMDIK KITIAGAGTM
     GYSMADIFAQ NGYEVTLWNH RQPTLDKAKT KISPAAAEKI TFTTSLDAFR GRDLIVESIA
     ENLDIKLDFY RQMSLLADPE TIIATNTSGL SINKLAEAVT GPERFLGMHW FNPPTLIPLI
     EIIKNAKTRP DVARTIYDLS LAIGKKPALV EKDVPGFAAN RIQLAVLREA LALVRDGVVS
     VEGADAVMKY GLGFRWACLG PLETVDFGGL DVFYHISEYL MPDLEDSHAV PELLAKKFQA
     GEYGVKNGKG FYDYAGDKAR EATAARDKKL QAVYDALYGE KK
//
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