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Database: UniProt
Entry: F5Z3R1_MYCSD
LinkDB: F5Z3R1_MYCSD
Original site: F5Z3R1_MYCSD 
ID   F5Z3R1_MYCSD            Unreviewed;       415 AA.
AC   F5Z3R1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=L-lactate dehydrogenase (Cytochrome) LldD2 {ECO:0000313|EMBL:AEF35961.1};
GN   Name=lldD2 {ECO:0000313|EMBL:AEF35961.1};
GN   OrderedLocusNames=JDM601_1961 {ECO:0000313|EMBL:AEF35961.1};
OS   Mycolicibacter sinensis (strain JDM601) (Mycobacterium sinense).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacter.
OX   NCBI_TaxID=875328 {ECO:0000313|EMBL:AEF35961.1, ECO:0000313|Proteomes:UP000009224};
RN   [1] {ECO:0000313|EMBL:AEF35961.1, ECO:0000313|Proteomes:UP000009224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JDM601 {ECO:0000313|EMBL:AEF35961.1,
RC   ECO:0000313|Proteomes:UP000009224};
RX   PubMed=21685274; DOI=10.1128/JB.05291-11;
RA   Zhang Z.Y., Sun Z.Q., Wang Z.L., Wen Z.L., Sun Q.W., Zhu Z.Q., Song Y.Z.,
RA   Zhao J.W., Wang H.H., Zhang S.L., Guo X.K.;
RT   "Complete genome sequence of a novel clinical isolate, the nontuberculous
RT   Mycobacterium strain JDM601.";
RL   J. Bacteriol. 193:4300-4301(2011).
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; CP002329; AEF35961.1; -; Genomic_DNA.
DR   AlphaFoldDB; F5Z3R1; -.
DR   STRING; 875328.JDM601_1961; -.
DR   KEGG; mjd:JDM601_1961; -.
DR   eggNOG; COG1304; Bacteria.
DR   HOGENOM; CLU_020639_6_1_11; -.
DR   Proteomes; UP000009224; Chromosome.
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   PIRSF; PIRSF000138; Al-hdrx_acd_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   Flavoprotein {ECO:0000256|PIRSR:PIRSR000138-2};
KW   FMN {ECO:0000256|PIRSR:PIRSR000138-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009224}.
FT   DOMAIN          34..411
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   ACT_SITE        306
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT   BINDING         60
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         113..115
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         142
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         164
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         166
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         192
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         201
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         282
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         304
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         306
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         309
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         360..361
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ   SEQUENCE   415 AA;  45696 MW;  EB5161F3CA5BD752 CRC64;
     MEQAMPVTQR RFPRVHELAP LIRFRRPRLN RRAQRLAAAL TVEDLRRIAQ RRTPRAAFDY
     TDGAAEDEIS LERARQAFRD IEFHPAILRD VTDVDTSRDV LGASVALPFA IAPTGFTRLM
     HTAGELAGAR AAEAAGIPFS LSTLGTASIE EVAAAAPGAR RWFQLYIWRD RERSMALLRR
     AADAGYDTLL ATVDAPVPGA RRRDTRNGMT IPPALTLRTV ADAIVHPAWW FDLFTTEPLA
     FASLDRWSGT VAQYMDNMFD PSMTFDDLAW VRSQWPGRFV VKGIQTLADA RAVVDLGADG
     IVLSNHGGRQ LDRAPVPFAL LPHVAREVGA DTEILLDTGI MSGADIVAAV ALGARCTLIG
     RAYLYGLMAG GQAGVQRVID ILAEQIRRTM RLLGVSELAE LSPQHVTQLR RHVPR
//
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