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Database: UniProt
Entry: B1VTX8_STRGG
LinkDB: B1VTX8_STRGG
Original site: B1VTX8_STRGG 
ID   B1VTX8_STRGG            Unreviewed;       724 AA.
AC   B1VTX8;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=Putative fatty acid oxidation complex alpha-subunit {ECO:0000313|EMBL:BAG17822.1};
GN   OrderedLocusNames=SGR_993 {ECO:0000313|EMBL:BAG17822.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG17822.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG17822.1, ECO:0000313|Proteomes:UP000001685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX   PubMed=18375553; DOI=10.1128/JB.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT   griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(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}.
CC   -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}.
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DR   EMBL; AP009493; BAG17822.1; -; Genomic_DNA.
DR   RefSeq; WP_003964882.1; NC_010572.1.
DR   AlphaFoldDB; B1VTX8; -.
DR   GeneID; 6212730; -.
DR   KEGG; sgr:SGR_993; -.
DR   PATRIC; fig|455632.4.peg.989; -.
DR   eggNOG; COG1024; Bacteria.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_009834_15_3_11; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000001685; Chromosome.
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}.
FT   DOMAIN          322..500
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          503..603
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   724 AA;  77664 MW;  BB0536F17AE701BB CRC64;
     MTESTTIRWE QDETGVVTLV LDDPNQSANT MNQAFKDSIA AVADRAEAEK DSIRGIIYTS
     AKKTFFAGGD LKDMIKVGPE NAQDAFDAGN AIKASLRRIE TLGKPVVAAI NGAALGGGYE
     IALACHHRVA LDAPGSRIGL PEVTLGLLPA GGGVTRTVRL MGIADALLKV LLQGTQYTPR
     RALENGLVHE VAATREEMTE KARAFIDAHP ESQQPWDVKG YRIPGGTPSN PKFAANLPAF
     PANLKKQLAG APMPAPRNIL AAAVEGSQVD FETALTIEAR YFTELVTGQV SKNMIQAFFF
     DLQAVNSGAN RPGGIPERPV RKVAVLGAGM MGAGIAYSCA RAGIDVVLKD VSAEAAAKGK
     AYSEKLLAKA LSRGRTTEAK RDELLARITP TGDAADLAGC DAVIEAVFED TALKHKVFQE
     IQDVIEPDAL LCSNTSTLPI TVLAEGVSRP VDFIGLHFFS PVDKMPLVEI IKGERTGDEA
     LARAFDLVRR IKKTPIVVND SRGFFTSRVI GQFINEGVAM VGEGVEPASI EQAAAQSGYP
     AKVLSLMDEL TLTLPRKIRN ETRRAVEEAG GSWPGHPSDE VIDRMVDEFG RTGRSGGAGF
     YDYDEDGKRA GLWPGLREHF TGKADGDVPF EDMKERMLFS EALDSVRCLE ENVLISVADA
     NIGSIMGIGF PPWTGGVLQY INGYEGGLPG FVARARELAE RYGDRFLPPA LLVEKAEKGE
     TFHD
//
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