OLED_XANCP
ID OLED_XANCP Reviewed; 337 AA.
AC Q8PDW5;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=2-alkyl-3-oxoalkanoate reductase {ECO:0000305};
DE EC=1.1.1.412 {ECO:0000250|UniProtKB:B2FI29};
GN Name=oleD {ECO:0000303|PubMed:21266575};
GN OrderedLocusNames=XCC0219 {ECO:0000312|EMBL:AAM39538.1};
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
RN [2]
RP FUNCTION IN OLEFIN BIOSYNTHESIS.
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=21266575; DOI=10.1074/jbc.m110.216127;
RA Frias J.A., Richman J.E., Erickson J.S., Wackett L.P.;
RT "Purification and characterization of OleA from Xanthomonas campestris and
RT demonstration of a non-decarboxylative Claisen condensation reaction.";
RL J. Biol. Chem. 286:10930-10938(2011).
RN [3]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=28223313; DOI=10.1128/jb.00890-16;
RA Christenson J.K., Jensen M.R., Goblirsch B.R., Mohamed F., Zhang W.,
RA Wilmot C.M., Wackett L.P.;
RT "Active multienzyme assemblies for long-chain olefinic hydrocarbon
RT biosynthesis.";
RL J. Bacteriol. 199:E00890-E00890(2017).
CC -!- FUNCTION: Involved in olefin biosynthesis (PubMed:21266575,
CC PubMed:28223313). Catalyzes the reversible stereospecific NADPH-
CC dependent reduction of 2-alkyl-3-oxoalkanoic acids to 2-alkyl-3-
CC hydroxyalkanoic acids (By similarity). {ECO:0000250|UniProtKB:B2FI29,
CC ECO:0000269|PubMed:21266575, ECO:0000269|PubMed:28223313}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2R,3S)-2-alkyl-3-hydroxyalkanoate + NADP(+) = an (R)-2-
CC alkyl-3-oxoalkanoate + H(+) + NADPH; Xref=Rhea:RHEA:54796,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:138340, ChEBI:CHEBI:138341; EC=1.1.1.412;
CC Evidence={ECO:0000250|UniProtKB:B2FI29};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54798;
CC Evidence={ECO:0000250|UniProtKB:B2FI29};
CC -!- SUBUNIT: Forms multimers. Forms a complex with OleB and OleC.
CC {ECO:0000269|PubMed:28223313}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:28223313}.
CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. {ECO:0000305}.
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DR EMBL; AE008922; AAM39538.1; -; Genomic_DNA.
DR RefSeq; NP_635614.1; NC_003902.1.
DR AlphaFoldDB; Q8PDW5; -.
DR SMR; Q8PDW5; -.
DR STRING; 340.xcc-b100_0241; -.
DR EnsemblBacteria; AAM39538; AAM39538; XCC0219.
DR KEGG; xcc:XCC0219; -.
DR PATRIC; fig|190485.4.peg.246; -.
DR eggNOG; COG0451; Bacteria.
DR HOGENOM; CLU_007383_6_1_6; -.
DR OMA; WGPGDTQ; -.
DR BioCyc; MetaCyc:MON-20171; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:InterPro.
DR InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01073; 3Beta_HSD; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..337
FT /note="2-alkyl-3-oxoalkanoate reductase"
FT /id="PRO_0000446919"
FT ACT_SITE 140
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:B2FI29"
FT BINDING 144
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:B2FI29"
SQ SEQUENCE 337 AA; 36252 MW; 256FAB348F6FA91D CRC64;
MMKILVTGGG GFLGQALCRG LVARGHEVVS FQRGDYPVLH TLGVGQIRGD LADPQAVRHA
LAGIDAVFHN AAKAGAWGSY DSYHQANVVG TQNVLDACRA NGVPRLIYTS TPSVTHRATN
PVEGLGADEV PYGEDLRAPY AATKAIAERA VLAANDAQLA TVALRPRLIW GPGDNHLLPR
LAARARAGRL RMVGDGSNLV DSTYIDNAAQ AHFDAFAHLA PGAACAGKAY FISNGEPLPM
RELLNRLLAA VDAPAVTRSL SFKTAYRIGA VCETLWPLLR LPGEVPLTRF LVEQLCTPHW
YSMEPARRDF GYVPQISIEE GLQRLRSSSS RDISITR
