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
//