ID B6ITC2_RHOCS Unreviewed; 728 AA.
AC B6ITC2;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Fatty acid oxidation complex alpha subunit {ECO:0000313|EMBL:ACI99140.1};
DE EC=1.1.1.35 {ECO:0000313|EMBL:ACI99140.1};
DE EC=4.2.1.17 {ECO:0000313|EMBL:ACI99140.1};
DE EC=5.1.2.3 {ECO:0000313|EMBL:ACI99140.1};
GN Name=fadJ {ECO:0000313|EMBL:ACI99140.1};
GN OrderedLocusNames=RC1_1743 {ECO:0000313|EMBL:ACI99140.1};
OS Rhodospirillum centenum (strain ATCC 51521 / SW).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=414684 {ECO:0000313|EMBL:ACI99140.1, ECO:0000313|Proteomes:UP000001591};
RN [1] {ECO:0000313|Proteomes:UP000001591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RA Touchman J.W., Bauer C., Blankenship R.E.;
RT "Genome sequence of Rhodospirillum centenum.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACI99140.1, ECO:0000313|Proteomes:UP000001591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RX PubMed=20500872; DOI=10.1186/1471-2164-11-325;
RA Lu Y.K., Marden J., Han M., Swingley W.D., Mastrian S.D., Chowdhury S.R.,
RA Hao J., Helmy T., Kim S., Kurdoglu A.A., Matthies H.J., Rollo D.,
RA Stothard P., Blankenship R.E., Bauer C.E., Touchman J.W.;
RT "Metabolic flexibility revealed in the genome of the cyst-forming alpha-1
RT proteobacterium Rhodospirillum centenum.";
RL BMC Genomics 11:325-325(2010).
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; CP000613; ACI99140.1; -; Genomic_DNA.
DR RefSeq; WP_012566925.1; NC_011420.2.
DR AlphaFoldDB; B6ITC2; -.
DR STRING; 414684.RC1_1743; -.
DR KEGG; rce:RC1_1743; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_15_3_5; -.
DR OrthoDB; 9803287at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000001591; Chromosome.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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 Isomerase {ECO:0000313|EMBL:ACI99140.1};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ACI99140.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000313|EMBL:ACI99140.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001591}.
FT DOMAIN 323..499
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 502..599
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 728 AA; 77622 MW; 35190E466B2DA8AD CRC64;
MTNAIAYAVD ADGICTLTID QPGRSMNVID ASFADEFAAA VDRAVADAAV KGVIVTSGKK
AFLAGADLMQ LEARFEQAAS LPVDQLFRQF FSFSAALRRM ETSGKPFACA LNGTALGGGF
EIALACHYRV AADDPSAKLG LPEVQVGLLP GAGGTQRVPR LIGIAAALPL LLEGRQLAPK
KALSTGLIHA VVPADQLLTA AKEWLTKSPN AVQPWDAKGY RVPGGAGGMD PKVIPVFMAG
NSMLREKTQG NYPAPAAIMS CVYEGTQLPI DTALRVEVKY FATLFRNPVA RNMIRTLFIN
KGKADKLDRR PAGVPRTTFR RMGMLGAGMM GAGIAHVAAM AGIEVELIDQ SQEAAEKGKG
YSAKLLADQV AKGRLTQEAA DAILARIRPT TSYDGLADVD IVIEAVFEDR AIKADVTKRA
EAVMPATATF GSNTSTLPIT GLAENSSRPA QFIGIHFFSP VDRMPLVEII RGKATDDATL
ARALDFVQAI RKTPIVVNDA RGFFTSRFCG TYINEGQTLL QEGVVPALIE NAGKQAGMPV
GPLALADEVA LDLSWKIRNQ WKKDLGEQYR PASGEGVSDI MVEKLGRIGR KGRKGFYDYP
EGGKKRLWAG LGEVWPQRPE ADQPDVDEVR KRLLYAQALD AVRCLEEGVL TDPADGDVGA
ILGLGYAPYT GGPLSMIDTI GVARFVAECD ALAQKYGERF SPPTLLRDMA AEGRSFYGSG
SAARVAAE
//
