(data stored in SCRATCH zone)

SWISSPROT: Q13HF0_PARXL

ID   Q13HF0_PARXL            Unreviewed;       266 AA.
AC   Q13HF0;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 86.
DE   SubName: Full=Putative short-chain dehydrogenase/reductase {ECO:0000313|EMBL:ABE36489.1};
DE            EC=1.1.1.100 {ECO:0000313|EMBL:ABE36489.1};
GN   ORFNames=Bxe_C0591 {ECO:0000313|EMBL:ABE36489.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE36489.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE36489.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE36489.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
RN   [2] {ECO:0000213|PDB:5JY1}
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH NAD.
RG   Seattle Structural Genomics Center for Infectious Disease (SSGCID);
RT   "Crystal Structure of putative short-chain dehydrogenase/reductase
RT   from Burkholderia xenovorans LB400 bound to NAD.";
RL   Submitted (MAY-2016) to the PDB data bank.
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DR   EMBL; CP000272; ABE36489.1; -; Genomic_DNA.
DR   RefSeq; WP_011493745.1; NZ_CP008761.1.
DR   PDB; 5JY1; X-ray; 1.65 A; A/B/C/D=1-266.
DR   PDBsum; 5JY1; -.
DR   SMR; Q13HF0; -.
DR   STRING; 266265.Bxe_C0591; -.
DR   EnsemblBacteria; ABE36489; ABE36489; Bxe_C0591.
DR   GeneID; 4010105; -.
DR   KEGG; bxb:DR64_7855; -.
DR   KEGG; bxe:Bxe_C0591; -.
DR   PATRIC; fig|266265.5.peg.8350; -.
DR   eggNOG; ENOG4105CHR; Bacteria.
DR   eggNOG; ENOG410XNW1; LUCA.
DR   KO; K00059; -.
DR   OMA; IHYYLMA; -.
DR   OrthoDB; 1356861at2; -.
DR   BioCyc; BXEN266265:BXE_RS39470-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 3.
DR   GO; GO:0102131; F:3-oxo-glutaryl-[acp] methyl ester reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102132; F:3-oxo-pimeloyl-[acp] methyl ester reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q13HF0.
DR   SWISS-2DPAGE; Q13HF0.
KW   3D-structure {ECO:0000213|PDB:5JY1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   NAD {ECO:0000213|PDB:5JY1};
KW   Nucleotide-binding {ECO:0000213|PDB:5JY1};
KW   Oxidoreductase {ECO:0000313|EMBL:ABE36489.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   NP_BIND      63     64       NAD. {ECO:0000213|PDB:5JY1}.
FT   NP_BIND     186    191       NAD. {ECO:0000213|PDB:5JY1}.
FT   BINDING      18     18       NAD; via amide nitrogen.
FT                                {ECO:0000213|PDB:5JY1}.
FT   BINDING      37     37       NAD. {ECO:0000213|PDB:5JY1}.
FT   BINDING      90     90       NAD; via carbonyl oxygen.
FT                                {ECO:0000213|PDB:5JY1}.
FT   BINDING     156    156       NAD. {ECO:0000213|PDB:5JY1}.
FT   BINDING     160    160       NAD. {ECO:0000213|PDB:5JY1}.
SQ   SEQUENCE   266 AA;  28739 MW;  91D2505BB147E879 CRC64;
     MGLLEQRVAL VTGAGGGIGR GVARSFGNEG AAVIIAEINE STGRQVEQEI REMGGRSLFV
     KTDVTSKASI EAAVRSAVEQ FGSLDILVNN AFVPTPNVLL EEKTDEMLEQ TLTTSLWATW
     WAMRAAFVPM RERRWGRIVN FYSIDTETGA WLHGDYNTAK AGIVGLTRSA ASEWGRFNIT
     VNAIAPTAMG ATFFELAAKN PEFAERSAAA RPLGRSGDPE QDIGPAAVFF ASEMSRFVTG
     ETLHVDGGLH LPGYNSRPAG IKPREY
//

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