ID B8DKJ3_DESVM Unreviewed; 339 AA.
AC B8DKJ3;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=FMN-dependent alpha-hydroxy acid dehydrogenase {ECO:0000313|EMBL:ACL08155.1};
GN OrderedLocusNames=DvMF_1204 {ECO:0000313|EMBL:ACL08155.1};
OS Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Nitratidesulfovibrio.
OX NCBI_TaxID=883 {ECO:0000313|EMBL:ACL08155.1};
RN [1] {ECO:0000313|EMBL:ACL08155.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Miyazaki F {ECO:0000313|EMBL:ACL08155.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C.,
RA Richardson P.;
RT "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00024042}.
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DR EMBL; CP001197; ACL08155.1; -; Genomic_DNA.
DR AlphaFoldDB; B8DKJ3; -.
DR STRING; 883.DvMF_1204; -.
DR KEGG; dvm:DvMF_1204; -.
DR eggNOG; COG1304; Bacteria.
DR HOGENOM; CLU_020639_6_0_7; -.
DR OrthoDB; 9770452at2; -.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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 PANTHER; PTHR10578:SF107; FMN HYDROXY ACID DEHYDROGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1.
DR Pfam; PF01070; FMN_dh; 2.
DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 2.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000138-2};
KW FMN {ECO:0000256|PIRSR:PIRSR000138-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 35..339
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT ACT_SITE 237
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 213
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 235
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 237
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 240
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 268..272
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 291..292
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 339 AA; 34497 MW; 1128B81CF850E526 CRC64;
MKEVRDKARQ LMKGYCRVCP VCNGKACSGE VPGMGGLGTG ATFAANLDAL AAVRLNMRLV
HDVKEPETTT TVCGIALDMP VLAAPIGGVS FNMGGGVSEE DYAAAVVGGC AERGIIGCTG
DGVPPFIIDA GFAAITGAGG RGIPFIKPWD GAELGEKLDR ALELGCPAIG MDIDAAGLVT
LRKMGRPVGP KTPAELSRIV DKVKARGMAF ILKGIMTTID ASLAVEVGAD GIVVSNHGGR
VLDHAPGTAE VLPEIADAVK GRIAILADGG VRDGVDVFKM LALGADAVML GRPFSIAAVG
GLKDGVTMLV DSIKGQLVQA MVLTGSANVA SIGRHALRM
//
