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Database: UniProt
Entry: Q68BR5_RHIOR
LinkDB: Q68BR5_RHIOR
Original site: Q68BR5_RHIOR 
ID   Q68BR5_RHIOR            Unreviewed;       302 AA.
AC   Q68BR5;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   24-JAN-2024, entry version 114.
DE   RecName: Full=L-lactate dehydrogenase {ECO:0000256|ARBA:ARBA00012967, ECO:0000256|RuleBase:RU000496};
DE            EC=1.1.1.27 {ECO:0000256|ARBA:ARBA00012967, ECO:0000256|RuleBase:RU000496};
GN   Name=ldh B {ECO:0000313|EMBL:BAD38932.1};
OS   Rhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=64495 {ECO:0000313|EMBL:BAD38932.1};
RN   [1] {ECO:0000313|EMBL:BAD38932.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NBRC4744 {ECO:0000313|EMBL:BAD38930.1}, and NBRC4780
RC   {ECO:0000313|EMBL:BAD38932.1};
RX   PubMed=15278242; DOI=10.1007/s00203-004-0691-3;
RA   Saito K., Saito A., Ohnishi M., Oda Y.;
RT   "Genetic diversity in Rhizopus oryzae strains as revealed by the sequence
RT   of lactate dehydrogenase genes.";
RL   Arch. Microbiol. 182:30-36(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate;
CC         Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27;
CC         Evidence={ECO:0000256|ARBA:ARBA00001763,
CC         ECO:0000256|RuleBase:RU000496};
CC   -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC       from pyruvate: step 1/1. {ECO:0000256|ARBA:ARBA00004843,
CC       ECO:0000256|RuleBase:RU000496}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000256|ARBA:ARBA00006054}.
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DR   EMBL; AB111559; BAD38930.1; -; Genomic_DNA.
DR   EMBL; AB111561; BAD38932.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q68BR5; -.
DR   SMR; Q68BR5; -.
DR   UniPathway; UPA00554; UER00611.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   CDD; cd00300; LDH_like; 1.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR011304; L-lactate_DH.
DR   InterPro; IPR018177; L-lactate_DH_AS.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01771; L-LDH-NAD; 1.
DR   PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR   PANTHER; PTHR43128:SF16; L-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   PRINTS; PR00086; LLDHDRGNASE.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00064; L_LDH; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000496}.
FT   DOMAIN          6..142
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          145..297
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         11..16
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         36
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         95
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         118..120
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ   SEQUENCE   302 AA;  32343 MW;  9F26D2D8906A5BE9 CRC64;
     MVLHSKVAII GAGAVGASTA YALMFKNICT EIIIVDINPD IVQAQVLDLA DAASVSNTPI
     RAGSAEEAGQ SDIIVIAAGA KQKEGEPRTK LIERNYRVLK NIIGGMQPIR SDAIILVVVN
     PVDILTHIAQ TLSGLAPNQV IGSGTYLDTT RLRVHLGDIF DVNPQSIHAF VLGEHGDSQM
     IAWEAASIGG QPLTSFPEFA ELDKNAISKA ISGKAMEIIR LKGATFYGIG ACAADLVHTI
     MLNRKSVHPV SVYVEKYGVT FSMPAKLGWR GVEKIYEVPL TEEEEALLLK SVEALKAVEY
     LS
//
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