ID B2GHG7_KOCRD Unreviewed; 699 AA.
AC B2GHG7;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Fatty oxidation complex alpha subunit {ECO:0000313|EMBL:BAG30443.1};
GN Name=fadB {ECO:0000313|EMBL:BAG30443.1};
GN OrderedLocusNames=KRH_20960 {ECO:0000313|EMBL:BAG30443.1};
OS Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=378753 {ECO:0000313|EMBL:BAG30443.1, ECO:0000313|Proteomes:UP000008838};
RN [1] {ECO:0000313|EMBL:BAG30443.1, ECO:0000313|Proteomes:UP000008838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201
RC {ECO:0000313|Proteomes:UP000008838};
RX PubMed=18408034; DOI=10.1128/JB.01853-07;
RA Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL J. Bacteriol. 190:4139-4146(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; AP009152; BAG30443.1; -; Genomic_DNA.
DR RefSeq; WP_012399164.1; NC_010617.1.
DR AlphaFoldDB; B2GHG7; -.
DR STRING; 378753.KRH_20960; -.
DR KEGG; krh:KRH_20960; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_16_2_11; -.
DR OrthoDB; 9771883at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000008838; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000008838}.
FT DOMAIN 325..504
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 508..588
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 699 AA; 74371 MW; 87523658C1CBBFDB CRC64;
MSDQSFPSTV TITVTHPVLP GREKPIALVS LDSTAPNGLV IWGSEAMRDL QRELSAIDTS
QVEAVVVTGN TKSFGAGANL KEIRAAQLSG TSDEYVGSGH DAFGVLAEMD VPTFSLITGV
ALGGGLELAL HTDYRLSTSG KAPMGLPECH LGFFPGWGGV YLLPHLVGAE AALSIIVTDS
MRGKNLNPAK AAQIGLVDAV LNGAPGTDEW ETSWQTWVVE TLEGKHEPRR TTDDEQTWTA
AVEKAAAKAE SAWHGAAPGP VAAIELVGRA RTESRVVNGE AAVEAFTQIV QSDAARASLY
AFELVSARSK QAANVPDAPV REIKKAAVIG AGLMAGQLAS LIAQGARIPV VMTDLDDERL
AAGVQRTRDR FAAQAEKGRM TPEQAEQLGS LITGARSPED LADADFVIEA VFEELDVKRQ
VFAQWEPVIK EDAILATNTS SLSITAMGRD LQHPERLVGF HVFNPVEVTP LLEIVAGEKT
DDSTLATAFD LAAKLRRIAV RVEDAPSFVV NRVLTRMFDS IGRAMDAGGD PETVDHALDA
MGLPMTPLQL LDFVGPAVLV HITHTMNDAY PQRFTLSPWL DAVADAGLKN TLPARGESSE
TYLSEGANEA LERTRRENGV TAQSGDGAGG QLLTRVQDAL AEEIGYMLDE GVVASARDID
LCMILGANYP FHLGGITPYL DRCGAAERVR GARFDAAQQ
//
