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Database: UniProt
Entry: I8T4C6_9GAMM
LinkDB: I8T4C6_9GAMM
Original site: I8T4C6_9GAMM 
ID   I8T4C6_9GAMM            Unreviewed;       281 AA.
AC   I8T4C6;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=3-hydroxybutyryl-CoA dehydrogenase {ECO:0000313|EMBL:EIT68553.1};
GN   ORFNames=WQQ_37480 {ECO:0000313|EMBL:EIT68553.1};
OS   Hydrocarboniphaga effusa AP103.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC   Hydrocarboniphaga.
OX   NCBI_TaxID=1172194 {ECO:0000313|EMBL:EIT68553.1, ECO:0000313|Proteomes:UP000003704};
RN   [1] {ECO:0000313|EMBL:EIT68553.1, ECO:0000313|Proteomes:UP000003704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP103 {ECO:0000313|EMBL:EIT68553.1,
RC   ECO:0000313|Proteomes:UP000003704};
RX   PubMed=22933753; DOI=10.1128/JB.01017-12;
RA   Chang H.K., Zylstra G.J., Chae J.C.;
RT   "Genome Sequence of n-Alkane-Degrading Hydrocarboniphaga effusa Strain
RT   AP103T (ATCC BAA-332T).";
RL   J. Bacteriol. 194:5120-5120(2012).
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:EIT68553.1}.
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DR   EMBL; AKGD01000003; EIT68553.1; -; Genomic_DNA.
DR   RefSeq; WP_007186683.1; NZ_AKGD01000003.1.
DR   AlphaFoldDB; I8T4C6; -.
DR   STRING; 1172194.WQQ_37480; -.
DR   PATRIC; fig|1172194.4.peg.3637; -.
DR   OrthoDB; 5389341at2; -.
DR   Proteomes; UP000003704; 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; 1.
DR   InterPro; IPR022694; 3-OHacyl-CoA_DH.
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   PANTHER; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR48075:SF5; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   PIRSF; PIRSF000105; HCDH; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00067; 3HCDH; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRSR:PIRSR000105-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003704}.
FT   DOMAIN          4..182
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          185..281
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   BINDING         9..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         32
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         48
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-3"
FT   BINDING         55
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-3"
FT   BINDING         91
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         96
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         118
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-3"
FT   BINDING         118
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         142
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         273
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   SITE            139
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ   SEQUENCE   281 AA;  29859 MW;  A2EA997FBE2447A5 CRC64;
     MSKTIGVIGA GIMGNGIAQV SAAAGLNVIM VDINDAALER GLASIAASLD KLVKKDKISA
     AEREATLARI SRTTDYGQLA TADLVIEAAT ENLEIKKRIL KQADGVMRAD AILATNTSSI
     SITELAASTT RPDRFVGLHF FNPVPLMQLV EVISGLATSQ QTQESIAEFA RAIGKAPIGV
     RNSPGFAVNR ILCPMINEAI FTLQEGVATA EDIDTGMKLG CGHPIGPLAL ADLVGLDTLL
     SVMEVFYRDF GDTKYRPAPL LREMVAAGRY GRKSGEGFYK Y
//
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