ID B6ITP2_RHOCS Unreviewed; 781 AA.
AC B6ITP2;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase, putative {ECO:0000313|EMBL:ACI99343.1};
GN OrderedLocusNames=RC1_1947 {ECO:0000313|EMBL:ACI99343.1};
OS Rhodospirillum centenum (strain ATCC 51521 / SW).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=414684 {ECO:0000313|EMBL:ACI99343.1, 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:ACI99343.1, 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}.
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DR EMBL; CP000613; ACI99343.1; -; Genomic_DNA.
DR RefSeq; WP_012567128.1; NC_011420.2.
DR AlphaFoldDB; B6ITP2; -.
DR STRING; 414684.RC1_1947; -.
DR KEGG; rce:RC1_1947; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_010448_0_0_5; -.
DR OrthoDB; 5389341at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000001591; 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; 2.
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:UP000001591}.
FT DOMAIN 6..194
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 196..297
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 348..400
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 781 AA; 84015 MW; E5AFF2D596BB58C0 CRC64;
MEIRSAAVIG AGVMGSGIAA HIANAGIPVF LLDIVPQAVK DGQGNDRSVV ARTAVEKMLK
TDPAPFMHRK AAGLITPGNL EDDLDKLAGV DWIVEAIVEN PAIKSDLYRK LDAVRKPGSV
VSSNTSTIPL RILLDGQSEQ FAQDFLITHF FNPPRYMRLL EIVKGERTRA DAVEAVARFC
DVALGKGVVT CKDTPGFIAN RIGTYFMQAA VNEAIDGGLT VEEADAISGR PMGLPKTGTF
GLIDLVGLDL MPLIAKSLLA TLPADDDYRR IFRTSPVIER MIAEGYTGRK GKGGFYRQQK
LPGGKRSREA LDLGTGQYRP QQRTALESAG VKGLRALVDH PDKGGRYAWR VLSQALTYAA
DLVPQIADTV VEVDEAMRLG YNWKWGPFEM IDQLGTGWFA EKLAAEGKRV PELLAVAAGR
PFYRVENGKL QFLGVDGDYR DVKRPDGVLL LSDVKRASKP VAKNGSAALW DIGDGVLCLE
FTSKMNALDT DIMAMIRKAI ETIGNGKAGP FKALVIHNES DNFSVGANLG LAMFAVNIGL
WPQIEAGTAE GQATYKALKY APFPTVGAPS GMALGGGCEI LLHCSAVQAH AESYIGLVEV
GVGLIPGWGG CKELLTRATV NKKRPGGPMP PIAQVFETIS TAKVAKSAFE AKELLFLRPT
DGITFNRYRL LADAKKKALE MAAAYEPPQP VEIRLPGPSA KMALEMAVEG FALQGKATPH
DITVSKALAF ILSGGNTDIT KPVTEDDLLA LERDAFIGLV KTTQTIDRIE HMLETGKPLR
N
//
