ID B0BZV2_ACAM1 Unreviewed; 794 AA.
AC B0BZV2;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase, C-domain family {ECO:0000313|EMBL:ABW27162.1};
GN OrderedLocusNames=AM1_2148 {ECO:0000313|EMBL:ABW27162.1};
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC Acaryochloridaceae; Acaryochloris.
OX NCBI_TaxID=329726 {ECO:0000313|EMBL:ABW27162.1, ECO:0000313|Proteomes:UP000000268};
RN [1] {ECO:0000313|EMBL:ABW27162.1, ECO:0000313|Proteomes:UP000000268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017 {ECO:0000313|Proteomes:UP000000268};
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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}.
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DR EMBL; CP000828; ABW27162.1; -; Genomic_DNA.
DR RefSeq; WP_012162643.1; NC_009925.1.
DR AlphaFoldDB; B0BZV2; -.
DR STRING; 329726.AM1_2148; -.
DR KEGG; amr:AM1_2148; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_010448_0_0_3; -.
DR OrthoDB; 9771883at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000000268; Chromosome.
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; 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 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:UP000000268}.
FT DOMAIN 8..190
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 193..292
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 794 AA; 88248 MW; 43994B517F14246A CRC64;
MLKPFRTAAV LGAGVMGTQI AAHLANAGLV VYLLDLPGPG VHKNAIVEAA FKKGLQQKPP
IFFTEKTARR VLLGNFEDDW HRLTHVDWVI EAVVEKLEVK QQLMARLEGH IRDDAVVSTN
TSGLSIQAIT AGRSDSFRRR FLGTHFFNPP RYLKLLELIP TIETDPQIVE RLKWFGHLHL
GKGVVVAKDT PNFIGNRIGV FISMLGIRAF TEQGYTIEEI DTLTGTLVGR PKSATFRTAD
IVGLDTLLYV AENLYPAIPD DENRDVFQVP EILRRLVEAG HLGSKTGQGF YQKVGKHILS
VNPQTLAYEK AQSLHLRNWK AIAKIKPLPE RLRTLYQDSG RAGTFFRQMM LKILSYSAHR
IPEIADHPLD IDQAMRWGFG WQLGPFEIWD AIGFSQVIQD MQAAGIVVPQ WVEKMQLAEI
DSFYQNIGPN GERFVYQPLH GYLPTEGPQD ELTVAQFKTD PARTLWQNAE AALLDIGDGV
TLFEFRSKGN TLGQVVVDGF SEALDIVEAG DYRGLVIGND GEHFSAGANL ADMIKFSHQD
KVNVFTDCEH GAIAHLLDQF QALMLRIHYF PKPIVAAIRG RILGGGCELV MASPHVVVAA
ETYIGLVELS VGLIPGAGGI MTMATWAAEQ AASDAPRDIQ PFLKQAFEHI GMAKVASSAH
EAQAWGYLPP TAQIVMNSDR RLYVAKEEVL RLDHESYVPP PKRNAIQVLG KPARALFETA
AYQMQQGGYI SDYDRFLANR LAYVLTGGDL SAPTLVSDDY LLGLERDMFL PLFSEKKTQE
RILHTLKTKK SLRN
//
