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Database: UniProt
Entry: N9AN27_9GAMM
LinkDB: N9AN27_9GAMM
Original site: N9AN27_9GAMM 
ID   N9AN27_9GAMM            Unreviewed;       710 AA.
AC   N9AN27;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ENV45090.1};
GN   ORFNames=F955_00946 {ECO:0000313|EMBL:ENV45090.1};
OS   Acinetobacter schindleri CIP 107287.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1217988 {ECO:0000313|EMBL:ENV45090.1, ECO:0000313|Proteomes:UP000018440};
RN   [1] {ECO:0000313|EMBL:ENV45090.1, ECO:0000313|Proteomes:UP000018440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 107287 {ECO:0000313|EMBL:ENV45090.1,
RC   ECO:0000313|Proteomes:UP000018440};
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 schindleri CIP 107287.";
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   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005}.
CC   -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}.
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:ENV45090.1}.
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DR   EMBL; APPQ01000023; ENV45090.1; -; Genomic_DNA.
DR   RefSeq; WP_004891563.1; NZ_KB849575.1.
DR   AlphaFoldDB; N9AN27; -.
DR   PATRIC; fig|1217988.3.peg.909; -.
DR   HOGENOM; CLU_009834_15_3_6; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000018440; Unassembled WGS sequence.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   CDD; cd06558; crotonase-like; 1.
DR   Gene3D; 1.10.1040.50; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR43612:SF3; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          316..494
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          497..597
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   710 AA;  77018 MW;  8E2ACF0CE44D210A CRC64;
     MSAIQFEKTA DNIVVLTFDS PNQSANTMNA DFRTALSEVV DRLKVDDEIS GIIFRSAKKT
     FFAGGDLDEL IQATPEHATE FFNMIEEMKV QLRYIETRGI PVVAALNGTA LGGGWEIALC
     AHHRIALNDP KSKFGLPEVT LGLLPGGGGI VRTVRLLGLQ TALPLLMEGK QLGVEKAKAL
     GLIHDTADSP DELLEKAVVC IKAHPKSVQP FDEKGYKIPG GSPSTPAVAQ MLAIAPAMLR
     DKTKACYPAP EAIMSAAVEG AQVDVDTALR IESRYFTYLA TGQISKNMIG TFWHGMNSIK
     SGVHRPKDCA KWQAKKVGIL GAGMMGAGIA YVTASRGIQV VLKDISIEAA EKGKAYSQKL
     LDKKVSQGRL TAGQREQILN LIHPTANTED LTGCDLIIEA VFENQELKAQ VIQEAEQYLA
     ADGVMASNTS TLPISNLAQA SKDQDKFIGL HFFSPVDKMQ LVEIIRGQNT LDETLAKAFD
     FVQQIGKLPI VVNDSRGFFT SRVFGTFVQE GLRLLSEGVH PARIEMAALK AGMPVGPLAV
     QDEVSLTLTE HVSNETRKVL QAEGKERQAS PADAVIQTMI HQFNRKGKAA GAGFYDYPEG
     GKKQLWSGLS HWNKNTEISE QEMIERFLFV QALDTVRCLE EGVLQSTAEG NIGSIFGIGF
     PAWTGGAVQY LNQYGLAKAL ARANVLEKKY GERFKAPALL KNKVSAAETF
//
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