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Database: UniProt
Entry: F1ZAH1_9SPHN
LinkDB: F1ZAH1_9SPHN
Original site: F1ZAH1_9SPHN 
ID   F1ZAH1_9SPHN            Unreviewed;       776 AA.
AC   F1ZAH1;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:EGD58421.1};
GN   ORFNames=Y88_0476 {ECO:0000313|EMBL:EGD58421.1};
OS   Novosphingobium nitrogenifigens DSM 19370.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=983920 {ECO:0000313|EMBL:EGD58421.1, ECO:0000313|Proteomes:UP000004728};
RN   [1] {ECO:0000313|EMBL:EGD58421.1, ECO:0000313|Proteomes:UP000004728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19370 {ECO:0000313|EMBL:EGD58421.1,
RC   ECO:0000313|Proteomes:UP000004728};
RX   PubMed=22156397; DOI=10.1128/JB.06381-11;
RA   Strabala T.J., Macdonald L., Liu V., Smit A.M.;
RT   "Draft Genome Sequence of Novosphingobium nitrogenifigens Y88T.";
RL   J. Bacteriol. 194:201-201(2012).
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   -!- 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:EGD58421.1}.
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DR   EMBL; AEWJ01000041; EGD58421.1; -; Genomic_DNA.
DR   RefSeq; WP_008066815.1; NZ_GL876926.1.
DR   AlphaFoldDB; F1ZAH1; -.
DR   STRING; 983920.Y88_0476; -.
DR   eggNOG; COG1024; Bacteria.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_010448_0_0_5; -.
DR   InParanoid; F1ZAH1; -.
DR   OrthoDB; 5389341at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000004728; Unassembled WGS sequence.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR48075:SF7; 3-HYDROXYACYL-COA DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00725; 3HCDH; 2.
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   4: Predicted;
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004728}.
FT   DOMAIN          11..194
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          196..297
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   DOMAIN          350..394
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   776 AA;  81486 MW;  127509897DDE75BE CRC64;
     MSSIATEPVR KVCVIGAGVM GAGIAAQVAN AGVPVLLLDI VRDPADRNAV AAGALKRLQK
     AEPAAFMSKR AAKLVEVGNI EDDLARVAEC DWVIEAIIER LDLKHALYEK LEAVRRPGTA
     VTSNTSTIPL GHLVAGRSEG FARDFFITHF FNPPRYMRLL EVVAGPASDA ALVARISDFA
     DRALGKTIVA CKDTPGFLAN RVGTFWLQSA VNAAFDLGLT VEEADAIAGK PMGVPKTGIF
     GLVDLVGIDL MPHLKASLTS TLPADDPYHA IAIDHPLITR MIGEGLTGRK GKGGFYRINR
     EAGKRREAID LASGEYRPQA KPASLPSAAQ KDLKALLALP GKAGAYAWAI LGATLTYAAS
     LLPQAADDVV AIDAAMKLGY NWKYGPFELI DRIGGADFVA RLEADGKAVP EVLRIAAGRP
     FYRIEAGKRQ YLGLDGAYHD LVRPDGVLLL EDIKLGAKPI IRNASAALWD IGDGVAALEF
     TSKMNAIDGE ILKLIGQAVP LVASKFKALV VYNEGSAFSA GANLGLALFA INIAAWGEIE
     KMVSGGQMAL KALKYAPFPV VAAPAGLALG GGCEIVLHAD AVQAHAESYI GLVECGVGLV
     PGWGGCGEML ARWQAAKGLP KGPVPAVSKV FETISTATVS KSAAEAMDLG FLRPTDGITM
     NRDRLLADAK ARALALAEGY QPPAPPTYRL PGAGGKAALE LAVAGFRARG MATPHDAVVA
     GHLADVLTGG EADLVDTVAE GDLLALERKA FLALVRHPGT QNRIEHMLKT GKPLRN
//
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