ID A0A2G0QF47_9GAMM Unreviewed; 560 AA.
AC A0A2G0QF47;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Putative 3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:PHM57852.1};
GN ORFNames=Xhom_00855 {ECO:0000313|EMBL:PHM57852.1};
OS Xenorhabdus hominickii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351679 {ECO:0000313|EMBL:PHM57852.1, ECO:0000313|Proteomes:UP000225433};
RN [1] {ECO:0000313|EMBL:PHM57852.1, ECO:0000313|Proteomes:UP000225433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17903 {ECO:0000313|EMBL:PHM57852.1,
RC ECO:0000313|Proteomes:UP000225433};
RX PubMed=28993611; DOI=10.1038/s41564-017-0039-9;
RA Tobias N.J., Wolff H., Djahanschiri B., Grundmann F., Kronenwerth M.,
RA Shi Y.M., Simonyi S., Grun P., Shapiro-Ilan D., Pidot S.J., Stinear T.P.,
RA Ebersberger I., Bode H.B.;
RT "Natural product diversity associated with the nematode symbionts
RT Photorhabdus and Xenorhabdus.";
RL Nat. Microbiol. 2:1676-1685(2017).
CC -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC {ECO:0000256|ARBA:ARBA00005086}.
CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009463}.
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:PHM57852.1}.
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DR EMBL; NJAI01000001; PHM57852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G0QF47; -.
DR STRING; 351679.A9255_15735; -.
DR OrthoDB; 5389341at2; -.
DR Proteomes; UP000225433; Unassembled WGS sequence.
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:0044248; P:cellular catabolic process; IEA:UniProt.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 3.30.750.190; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR041040; 3HCDH_RFF.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR48075:SF5; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR Pfam; PF00725; 3HCDH; 2.
DR Pfam; PF02737; 3HCDH_N; 1.
DR Pfam; PF18321; 3HCDH_RFF; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00067; 3HCDH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 23..199
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 203..300
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 384..452
FT /note="3-hydroxybutyryl-CoA dehydrogenase reduced Rossmann-
FT fold"
FT /evidence="ECO:0000259|Pfam:PF18321"
FT DOMAIN 457..535
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT REGION 308..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 560 AA; 61450 MW; 29863D4AEFC98525 CRC64;
MTMPLLHSPI STIDADIIDA GIIGIIGAGT MGIGIAQVAA QAGHSVLLFD VNSEASSHAL
DNLRARLRQR VEAGKAEADA TELLLKRITR VDSLQTLAPC ALVIEAIVEQ LEAKQDLFRQ
LDAICPAQTL FASNTSSLSI TAIARVLSSP QRMAGLHFFN PAPLMKLVEI VQGLETSPQT
VTTLKMLATN WKKQPVICRS SPGFIVNRIA RPFYAEALRA LEEQVASPAT LDTVMKESGG
FAMGPLQLTD LIGHDVNYAV TESLFHAFHN DPRFQPSLRQ KELVDAGHLG RKRGRGFYLY
NMQGNNVQGN SGKKEAQPLP KIEPKQSKEK KQPTRLKATG NWAALPHFVS LLQKPKLQQY
GIVFEEGKND RFHSPTLHID DIILTLTKGR TCAQLADEVR VPVMQFDLSA NHLSAPVITL
STACQNTPHQ TAKVVGFLQS LGKQVILLPD YPALLTMRTV AMLCNEALDA LNKGLASAED
IDLAMLDGVN YPIGPLAWGE QLGWKHILST LENLQKFYGE PRYRPAPLLR QLAADHAKLQ
LHGQHENYNE NHNKESADAR
//
