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Database: UniProt
Entry: A0A3P2A8A0_9NEIS
LinkDB: A0A3P2A8A0_9NEIS
Original site: A0A3P2A8A0_9NEIS 
ID   A0A3P2A8A0_9NEIS        Unreviewed;       251 AA.
AC   A0A3P2A8A0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=L-lactate dehydrogenase {ECO:0000313|EMBL:RRD91036.1};
DE   Flags: Fragment;
GN   ORFNames=EII21_03565 {ECO:0000313|EMBL:RRD91036.1};
OS   Conchiformibius steedae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Conchiformibius.
OX   NCBI_TaxID=153493 {ECO:0000313|EMBL:RRD91036.1, ECO:0000313|Proteomes:UP000269923};
RN   [1] {ECO:0000313|EMBL:RRD91036.1, ECO:0000313|Proteomes:UP000269923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COT-280 {ECO:0000313|EMBL:RRD91036.1,
RC   ECO:0000313|Proteomes:UP000269923};
RA   Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA   Eisen J.A., Holcombe L.J., O'Flynn C.;
RT   "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT   for Automated Genome-Based Taxonomic Assignment.";
RL   Submitted (NOV-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RRD91036.1}.
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DR   EMBL; RQYC01000003; RRD91036.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P2A8A0; -.
DR   STRING; 1121352.GCA_000620925_00775; -.
DR   OrthoDB; 9770452at2; -.
DR   Proteomes; UP000269923; Unassembled WGS sequence.
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   InterPro; IPR008259; FMN_hydac_DH_AS.
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; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR   PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000269923}.
FT   DOMAIN          1..215
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:RRD91036.1"
SQ   SEQUENCE   251 AA;  27894 MW;  AC83A3A76E5E65C4 CRC64;
     KDIKNGLSAP PKPTLPNLLN LALKPEWCLK MLNTERHTFR NIVGHAQNVG DLSSLSSWTA
     EQFDPSLSWD DVARIKDLWG GKLIIKGIMD PEDAEMAVKH GADAIVVSNH GGRQLDGALS
     SILALPDIVS AVSGQTEIWL DSGIRSGQDI LKAWALGARG VMIGRAFLYG LGAYGQEGVT
     RALEILYKEM DVTMAFTGHR DIQNVGREIL IKGTYPISEY ERTESELQKR RRIYDELYGW
     PRASLRFGTM W
//
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