ID G2FIF4_9GAMM Unreviewed; 233 AA.
AC G2FIF4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000313|EMBL:EGW53425.1};
DE EC=1.1.1.35 {ECO:0000313|EMBL:EGW53425.1};
DE EC=4.2.1.17 {ECO:0000313|EMBL:EGW53425.1};
DE EC=5.1.2.3 {ECO:0000313|EMBL:EGW53425.1};
GN Name=fadJ1 {ECO:0000313|EMBL:EGW53425.1};
GN ORFNames=TevJSym_bc00250 {ECO:0000313|EMBL:EGW53425.1};
OS endosymbiont of Tevnia jerichonana (vent Tica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW53425.1, ECO:0000313|Proteomes:UP000005167};
RN [1] {ECO:0000313|EMBL:EGW53425.1, ECO:0000313|Proteomes:UP000005167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA Sievert S.M., Schweder T.;
RT "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT jerichonana share an identical physiology as revealed by proteogenomic
RT analyses.";
RL ISME J. 0:0-0(2011).
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:EGW53425.1}.
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DR EMBL; AFZB01000029; EGW53425.1; -; Genomic_DNA.
DR AlphaFoldDB; G2FIF4; -.
DR eggNOG; COG1250; Bacteria.
DR Proteomes; UP000005167; Unassembled WGS sequence.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0070403; F:NAD+ binding; 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; 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 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 SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR PROSITE; PS00067; 3HCDH; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:EGW53425.1};
KW Lyase {ECO:0000313|EMBL:EGW53425.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EGW53425.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005167}.
FT DOMAIN 1..35
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 39..130
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 233 AA; 26118 MW; 38438BD01F0DA755 CRC64;
MQLVEVVHGE QTTAEQVSRG ASFARRIGKL PVPVKSYPGF LVNRVLMPYL LEAMELLEEG
VPGPVIDKAA VDFGMPAGPI ELADRVGLDI CLAVAKELSA HYPFKLPGQL EFMVRESKLG
LKSGEGFYRW EKKRPLKQRF DAFYHAPNDL AERLIFRLLN EAVACFREGV VEDADLLDAG
IIFGTGFAPF RGGPMHYIKN GGLQQMRQRI QELERRHGKQ FHPDSGWTNL GRV
//
