ID   LDHB_RHIOR              Reviewed;         302 AA.
AC   Q9P4B5;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=L-lactate dehydrogenase B;
DE            Short=L-LDH B;
DE            EC=1.1.1.27;
GN   Name=LDHB;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9363 / NRRL 395;
RX   PubMed=10831409; DOI=10.1128/aem.66.6.2343-2348.2000;
RA   Skory C.D.;
RT   "Isolation and expression of lactate dehydrogenase genes from Rhizopus
RT   oryzae.";
RL   Appl. Environ. Microbiol. 66:2343-2348(2000).
CC   -!- FUNCTION: Converts L-lactate to pyruvate.
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:0000255|PROSITE-ProRule:PRU10002};
CC   -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC       from pyruvate: step 1/1.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000305}.
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DR   EMBL; AF226155; AAF61914.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9P4B5; -.
DR   SMR; Q9P4B5; -.
DR   UniPathway; UPA00554; UER00611.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.110.10; -; 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   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; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01771; L-LDH-NAD; 1.
DR   PROSITE; PS00064; L_LDH; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NAD; Oxidoreductase.
FT   CHAIN           1..302
FT                   /note="L-lactate dehydrogenase B"
FT                   /id="PRO_0000168499"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10002"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   302 AA;  32388 MW;  348C79DF8ABDE695 CRC64;
     MVLHSKVAII GAGAVGASTA YALMFKNICT EIIIVDINPD IVQAQVLDLA DAASVSNTPI
     RAGSAEEAGQ SDIIVITAGA KQKEGEPRTK LIERNYRVLK NIIGGMQPIR SDAIILVVVN
     PVDILTHIAQ TLSGLAPNQV IGSGTYLDTT RLRVHLGDIF DVNPQSIHAF VLGEHGDSQM
     IAWEAASIGG QPLTSFPEFA ELDKKAISKA ISGKAMEIIR LKGATFYGIG ACAADLVHTI
     MLNRKSVHPV SVYVEKYGVT FSMPAKLGWR GVEKIYEVPL TEEEEALLLK SVEALKAVEY
     LS