(data stored in SCRATCH zone)

SWISSPROT: A4ATW3_MARSH

ID   A4ATW3_MARSH            Unreviewed;       387 AA.
AC   A4ATW3;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 65.
DE   SubName: Full=L-lactate dehydrogenase and related alpha-hydroxy acid dehydrogenase {ECO:0000313|EMBL:EAR00883.1};
GN   OrderedLocusNames=FB2170_17401 {ECO:0000313|EMBL:EAR00883.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00883.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00883.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00683}.
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DR   EMBL; CP002157; EAR00883.1; -; Genomic_DNA.
DR   RefSeq; WP_013304686.1; NC_014472.1.
DR   STRING; 313603.FB2170_17401; -.
DR   EnsemblBacteria; EAR00883; EAR00883; FB2170_17401.
DR   KEGG; fbc:FB2170_17401; -.
DR   eggNOG; ENOG4105DMF; Bacteria.
DR   eggNOG; COG1304; LUCA.
DR   HOGENOM; HOG000217464; -.
DR   KO; K00101; -.
DR   OMA; LIVTTDW; -.
DR   OrthoDB; 1186741at2; -.
DR   BioCyc; MSP313603:G1GNS-255-MONOMER; -.
DR   Proteomes; UP000001602; 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   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; A4ATW3.
DR   SWISS-2DPAGE; A4ATW3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
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:UP000001602}.
FT   DOMAIN        9    387       FMN hydroxy acid dehydrogenase.
FT                                {ECO:0000259|PROSITE:PS51349}.
FT   NP_BIND     317    341       FMN. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00683}.
FT   NP_BIND     317    321       FMN. {ECO:0000256|PIRSR:PIRSR000138-2}.
FT   ACT_SITE    286    286       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000138-1, ECO:0000256|PROSITE-
FT                                ProRule:PRU00683}.
FT   BINDING      35     35       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000138-2, ECO:0000256|PROSITE-
FT                                ProRule:PRU00683}.
FT   BINDING     117    117       FMN. {ECO:0000256|PIRSR:PIRSR000138-2,
FT                                ECO:0000256|PROSITE-ProRule:PRU00683}.
FT   BINDING     138    138       FMN. {ECO:0000256|PIRSR:PIRSR000138-2,
FT                                ECO:0000256|PROSITE-ProRule:PRU00683}.
FT   BINDING     140    140       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000138-2, ECO:0000256|PROSITE-
FT                                ProRule:PRU00683}.
FT   BINDING     175    175       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000138-2, ECO:0000256|PROSITE-
FT                                ProRule:PRU00683}.
FT   BINDING     262    262       FMN. {ECO:0000256|PIRSR:PIRSR000138-2,
FT                                ECO:0000256|PROSITE-ProRule:PRU00683}.
FT   BINDING     284    284       FMN. {ECO:0000256|PIRSR:PIRSR000138-2}.
FT   BINDING     289    289       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000138-2, ECO:0000256|PROSITE-
FT                                ProRule:PRU00683}.
FT   BINDING     341    341       FMN. {ECO:0000256|PIRSR:PIRSR000138-2}.
SQ   SEQUENCE   387 AA;  43229 MW;  16D7CAEE0EEDFA14 CRC64;
     MSRNTIAKHF DSRYPSVEDL RNKAQKRIPK FAFEYLDSGC NEEVNLRRNT REIREVQLVP
     NYLDNFGQAS LKTELFGHVY DAPFGIAPVG LQGLMWPNAS EILAKAAFEN NIPFVLSTVS
     TSSIERISEL TEGKAWFQLY HPTEDSIRND MLKRAEAAEC PVLVLLCDTP AFGFRPKEIK
     NGLSMPPKMS INNILQVFGK PNWAFNTLKY GQPNFEVLKP YMPKGLDLGQ LGNFMDQTFS
     KRMSMEKIAP IRDLWKGKIV LKGVSTEADT EKAIQLGLDG IIVSNHGGRQ LDAGESTIKP
     MTRISKKYGS QIKVLMDSGL RSGPDIARTL ASGAEFSFLG RSFMYGVAAL GKKGGEHTIS
     LLKTQLQQVM EQIGCEEIKD FPKHLIS
//

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