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