(data stored in SCRATCH zone)

SWISSPROT: Q5LVU7_RUEPO

ID   Q5LVU7_RUEPO            Unreviewed;       371 AA.
AC   Q5LVU7;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 91.
DE   SubName: Full=Membrane-bound sulfolactate dehydrogenase {ECO:0000313|EMBL:AAV93913.1};
GN   Name=slcD {ECO:0000313|EMBL:AAV93913.1};
GN   OrderedLocusNames=SPO0598 {ECO:0000313|EMBL:AAV93913.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93913.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93913.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93913.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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; CP000031; AAV93913.1; -; Genomic_DNA.
DR   RefSeq; WP_011046354.1; NC_003911.12.
DR   STRING; 246200.SPO0598; -.
DR   EnsemblBacteria; AAV93913; AAV93913; SPO0598.
DR   KEGG; sil:SPO0598; -.
DR   eggNOG; ENOG4105DMF; Bacteria.
DR   eggNOG; COG1304; LUCA.
DR   HOGENOM; HOG000217464; -.
DR   KO; K00101; -.
DR   OMA; WHGRAWS; -.
DR   OrthoDB; 1186741at2; -.
DR   BioCyc; RPOM246200:G1G48-606-MONOMER; -.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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   Pfam; PF01070; FMN_dh; 1.
DR   PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
DR   PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5LVU7.
DR   SWISS-2DPAGE; Q5LVU7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   Flavoprotein {ECO:0000256|PROSITE-ProRule:PRU00683};
KW   FMN {ECO:0000256|PIRSR:PIRSR000138-2, ECO:0000256|PROSITE-
KW   ProRule:PRU00683};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023}.
FT   DOMAIN        2    371       FMN hydroxy acid dehydrogenase.
FT                                {ECO:0000259|PROSITE:PS51349}.
FT   NP_BIND     301    325       FMN. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00683}.
FT   NP_BIND     301    305       FMN. {ECO:0000256|PIRSR:PIRSR000138-2}.
FT   ACT_SITE    270    270       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000138-1, ECO:0000256|PROSITE-
FT                                ProRule:PRU00683}.
FT   BINDING      28     28       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000138-2, ECO:0000256|PROSITE-
FT                                ProRule:PRU00683}.
FT   BINDING     110    110       FMN. {ECO:0000256|PIRSR:PIRSR000138-2,
FT                                ECO:0000256|PROSITE-ProRule:PRU00683}.
FT   BINDING     131    131       FMN. {ECO:0000256|PIRSR:PIRSR000138-2,
FT                                ECO:0000256|PROSITE-ProRule:PRU00683}.
FT   BINDING     133    133       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000138-2, ECO:0000256|PROSITE-
FT                                ProRule:PRU00683}.
FT   BINDING     159    159       FMN. {ECO:0000256|PIRSR:PIRSR000138-2,
FT                                ECO:0000256|PROSITE-ProRule:PRU00683}.
FT   BINDING     168    168       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000138-2, ECO:0000256|PROSITE-
FT                                ProRule:PRU00683}.
FT   BINDING     246    246       FMN. {ECO:0000256|PIRSR:PIRSR000138-2,
FT                                ECO:0000256|PROSITE-ProRule:PRU00683}.
FT   BINDING     268    268       FMN. {ECO:0000256|PIRSR:PIRSR000138-2}.
FT   BINDING     273    273       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000138-2, ECO:0000256|PROSITE-
FT                                ProRule:PRU00683}.
FT   BINDING     325    325       FMN. {ECO:0000256|PIRSR:PIRSR000138-2}.
SQ   SEQUENCE   371 AA;  40754 MW;  627038AAFF72E8F3 CRC64;
     MLRQTGIHSS EDARRLARKR LPWMVFDYVD GAAGEEHGAM LARRAIQDIR LTPRVLRNVS
     RRELRVQLFD KLAVRPFGIS PMGMCNLSAP DADLMLARLA ARDRVPHGVS TVASTDMETL
     LKASGGMAWF QLYFSGDGSG TMKLVERARA AGYGTLVLTV DVPEVGRRPR ELRHGFKMPF
     RIGPRQFVDF ALHPRWSLST LIRGRPQMAN FDGRNYVFDR TESRAAADWT TFETLRATWP
     GKLVVKGVLH PGDALRLKAL GADAIQVSSH GCRQLDAAPP AIEALAAIRQ AVGPSYPLFY
     DSGIRSGEDV VKAYAMGADF VFLGRPLLYA MAAGGEAGLH QLWEVLAQEV SLTLAQLGLT
     EMAALREGAA R
//

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