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LDHA_RHIOR
ID   LDHA_RHIOR              Reviewed;         320 AA.
AC   Q9P4B6;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=L-lactate dehydrogenase A;
DE            Short=L-LDH A;
DE            EC=1.1.1.27;
GN   Name=LDHA;
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 pyruvate to lactate.
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; AF226154; AAF74436.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9P4B6; -.
DR   SMR; Q9P4B6; -.
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..320
FT                   /note="L-lactate dehydrogenase A"
FT                   /id="PRO_0000168498"
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   320 AA;  34183 MW;  E447F4857F5C2276 CRC64;
     MVLHSKVAIV GAGAVGASTA YALMFKNICT EIIIVDVNPD IVQAQVLDLA DAASISHTPI
     RAGSAEEAGQ ADIVVITAGA KQREGEPRTK LIERNFRVLQ SIIGGMQPIR PDAVILVVAN
     PVDILTHIAK TLSGLPPNQV IGSGTYLDTT RLRVHLGDVF DVNPQSVHAF VLGEHGDSQM
     IAWEAASIGG QPLTSFPEFA KLDKTAISKA ISGKAMEIIR LKGATFYGIG ACAADLVHTI
     MLNRKSVHPV SVYVEKYGAT FSMPAKLGWR GVEQIYEVPL TEEEEALLVK SVEALKSVEY
     SSTKVPEKKV HATSFSKSSC
 
 
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