ID N9PIP4_9GAMM Unreviewed; 611 AA.
AC N9PIP4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=F890_00102 {ECO:0000313|EMBL:ENX33419.1};
OS Acinetobacter sp. CIP 64.7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1144673 {ECO:0000313|EMBL:ENX33419.1, ECO:0000313|Proteomes:UP000013258};
RN [1] {ECO:0000313|EMBL:ENX33419.1, ECO:0000313|Proteomes:UP000013258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 64.7 {ECO:0000313|EMBL:ENX33419.1,
RC ECO:0000313|Proteomes:UP000013258};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. CIP 64.7.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC Evidence={ECO:0000256|ARBA:ARBA00023693};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
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:ENX33419.1}.
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DR EMBL; APRY01000015; ENX33419.1; -; Genomic_DNA.
DR RefSeq; WP_005265410.1; NZ_KB850177.1.
DR AlphaFoldDB; N9PIP4; -.
DR PATRIC; fig|1144673.3.peg.92; -.
DR HOGENOM; CLU_009834_21_1_6; -.
DR OrthoDB; 9803287at2; -.
DR Proteomes; UP000013258; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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 PANTHER; PTHR43561; -; 1.
DR PANTHER; PTHR43561:SF3; HYDROXYACYL-COENZYME A DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF00725; 3HCDH; 2.
DR Pfam; PF02737; 3HCDH_N; 2.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
PE 4: Predicted;
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 12..191
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 195..292
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 317..495
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 500..596
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 611 AA; 66827 MW; 118DDFCFA3C1F899 CRC64;
MSESNPLVNF THITVAGSGV LGYQIAVQAA FHGFKVVVYD INDEVLNKAK TKFANIAKRH
QDDLSETSEQ AKQAEQNLSY TSDLIAALKD ADLLIEAVPE DVAIKKDFYQ KASAAAPEKT
VFVSNSSTML PSDLVKFTDR PAKFLMMHFA NEIWKRNLAE IMSHADTDPN VFDAVTAFAK
QIGMVPIIVN KETSGYVLNS LLNPWLNAGM QLYIQGIADI QTIDKTWMLG TGSPMGPFAF
YDMLGLTTPY NIYKLAVAKG KQQDQAVVDM LKKDYIEKNK LGVPTGEGFY QYPNPAFKNP
DFLKPPKADL SKVPYKNITV AGSGVLGNQI AVQCAFHGFN VTIYDINDDA IAKAKTRFTD
LANQHQHDLG ETDAQVAAAS NNLAYTTDLN EALKDADLLI EAVPESLDIK KDFYSKASAA
APAKTVFASN SSTLLPSVLS TFTNRPEKFL MLHFANHIHI RNTVELMAAP SCDPQVYADV
IEFAKAIAML PIAVKKEQSG YVLDSLLIPL LVAGLKLWAN GVANAATIDK TWMIATGSPF
GPMAILDKNG MTTNYNILNE LAKTDPSLQQ PAEKLKAELV DTNKLGEATG EGFYQYPNPA
YLAKDFLSLI H
//
