(data stored in ACNUC1104 zone)

SWISSPROT: A1SDE0_NOCSJ

ID   A1SDE0_NOCSJ            Unreviewed;       410 AA.
AC   A1SDE0;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   SubName: Full=(S)-2-hydroxy-acid oxidase {ECO:0000313|EMBL:ABL79825.1};
DE            EC=1.1.3.15 {ECO:0000313|EMBL:ABL79825.1};
GN   OrderedLocusNames=Noca_0280 {ECO:0000313|EMBL:ABL79825.1};
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL79825.1, ECO:0000313|Proteomes:UP000000640};
RN   [1] {ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Mattes T., Gossett J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABL79825.1, ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RX   PubMed=21551312; DOI=10.1128/JB.05109-11;
RA   Coleman N.V., Wilson N.L., Barry K., Brettin T.S., Bruce D.C.,
RA   Copeland A., Dalin E., Detter J.C., Del Rio T.G., Goodwin L.A.,
RA   Hammon N.M., Han S., Hauser L.J., Israni S., Kim E., Kyrpides N.,
RA   Land M.L., Lapidus A., Larimer F.W., Lucas S., Pitluck S.,
RA   Richardson P., Schmutz J., Tapia R., Thompson S., Tice H.N.,
RA   Spain J.C., Gossett J.G., Mattes T.E.;
RT   "Genome Sequence of the ethene- and vinyl chloride-oxidizing
RT   actinomycete Nocardioides sp. strain JS614.";
RL   J. Bacteriol. 193:3399-3400(2011).
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000138-2, ECO:0000256|PROSITE-
CC         ProRule:PRU00683};
CC   -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC       dehydrogenase family. {ECO:0000256|PROSITE-ProRule:PRU00683}.
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DR   EMBL; CP000509; ABL79825.1; -; Genomic_DNA.
DR   RefSeq; WP_011753776.1; NC_008699.1.
DR   STRING; 196162.Noca_0280; -.
DR   EnsemblBacteria; ABL79825; ABL79825; Noca_0280.
DR   KEGG; nca:Noca_0280; -.
DR   eggNOG; ENOG4105DMF; Bacteria.
DR   eggNOG; COG1304; LUCA.
DR   HOGENOM; HOG000217464; -.
DR   KO; K00104; -.
DR   OMA; KSVYDYY; -.
DR   OrthoDB; 1186741at2; -.
DR   BioCyc; NSP196162:GH4V-282-MONOMER; -.
DR   Proteomes; UP000000640; Chromosome.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0052853; F:long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052854; F:medium-chain-(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052852; F:very-long-chain-(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
DR   CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN.
DR   InterPro; IPR000262; FMN-dep_DH.
DR   InterPro; IPR037396; FMN_HAD.
DR   InterPro; IPR008259; FMN_hydac_DH_AS.
DR   Pfam; PF01070; FMN_dh; 1.
DR   PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
DR   PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR   PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1SDE0.
DR   SWISS-2DPAGE; A1SDE0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000640};
KW   Flavoprotein {ECO:0000256|PROSITE-ProRule:PRU00683};
KW   FMN {ECO:0000256|PIRSR:PIRSR000138-2, ECO:0000256|PROSITE-
KW   ProRule:PRU00683}; Oxidoreductase {ECO:0000313|EMBL:ABL79825.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000640}.
FT   DOMAIN       27    404       FMN hydroxy acid dehydrogenase.
FT                                {ECO:0000259|PROSITE:PS51349}.
FT   NP_BIND     330    354       FMN. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00683}.
FT   ACT_SITE    299    299       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000138-1, ECO:0000256|PROSITE-
FT                                ProRule:PRU00683}.
FT   BINDING      53     53       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000138-2, ECO:0000256|PROSITE-
FT                                ProRule:PRU00683}.
FT   BINDING     135    135       FMN. {ECO:0000256|PIRSR:PIRSR000138-2,
FT                                ECO:0000256|PROSITE-ProRule:PRU00683}.
FT   BINDING     157    157       FMN. {ECO:0000256|PIRSR:PIRSR000138-2,
FT                                ECO:0000256|PROSITE-ProRule:PRU00683}.
FT   BINDING     159    159       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000138-2, ECO:0000256|PROSITE-
FT                                ProRule:PRU00683}.
FT   BINDING     185    185       FMN. {ECO:0000256|PIRSR:PIRSR000138-2,
FT                                ECO:0000256|PROSITE-ProRule:PRU00683}.
FT   BINDING     194    194       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000138-2, ECO:0000256|PROSITE-
FT                                ProRule:PRU00683}.
FT   BINDING     275    275       FMN. {ECO:0000256|PIRSR:PIRSR000138-2,
FT                                ECO:0000256|PROSITE-ProRule:PRU00683}.
FT   BINDING     297    297       FMN. {ECO:0000256|PIRSR:PIRSR000138-2}.
FT   BINDING     302    302       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000138-2, ECO:0000256|PROSITE-
FT                                ProRule:PRU00683}.
FT   BINDING     354    354       FMN. {ECO:0000256|PIRSR:PIRSR000138-2}.
SQ   SEQUENCE   410 AA;  45169 MW;  DFD4977272C6A90B CRC64;
     MKRQLPRRRD LAPLVRFRTP VLSPRGRRLR DALTIEDLRR AARRRTPRAA FDYTDGAADD
     EISLARARQA FRDVQFNPGV LRDVSSVDTS REVLGARASL PFGIAPTGFT RLMHTEGEVA
     GATAAAAAGI PFALSTMGTT SIEDVAAAAP SGRHWFQLYM WKDRDRSMAL VERAARAGFD
     ALLVTVDVPV AGARLRDVRN GMTIPPTLTP RTVLDAIPRM RWWFDLLTTE PLAFATLDSW
     SGTVAELLDT MFDPTVTFED LAWIKEQWPG RLVVKGIQTV DDARRVADLG ADAVLLSNHG
     GRQLDRAPIP FRLLPEVVAA VGQDVEVHLD TGIMSGQDIV AALAHGARFT LVGRAYLYGL
     MAGGRDGVDR AVEILRSQVE RTMRLLGVRS LGDLEPGHVT QLDRLEPRRR
//

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