ID   LDHA_CHAGU              Reviewed;         331 AA.
AC   O93541;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=L-lactate dehydrogenase A chain;
DE            Short=LDH-A;
DE            EC=1.1.1.27;
GN   Name=ldha;
OS   Champsocephalus gunnari (Mackerel icefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes;
OC   Notothenioidei; Channichthyidae; Champsocephalus.
OX   NCBI_TaxID=52237;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RX   MEDLINE=98409683; PubMed=9736762; DOI=10.1073/pnas.95.19.11476;
RA   Fields P.A., Somero G.N.;
RT   "Hot spots in cold adaptation: localized increases in conformational
RT   flexibility in lactate dehydrogenase A4 orthologs of Antarctic
RT   notothenioid fishes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:11476-11481(1998).
CC   -!- CATALYTIC ACTIVITY: (S)-lactate + NAD(+) = pyruvate + NADH.
CC   -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-
CC       lactate from pyruvate: step 1/1.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
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DR   EMBL; AF079824; AAC63282.1; -; mRNA.
DR   PDB; 2V65; X-ray; 2.35 A; A/B=2-330.
DR   PDBsum; 2V65; -.
DR   HOVERGEN; O93541; -.
DR   BRENDA; 1.1.1.27; 305295.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:EC.
DR   GO; GO:0019642; P:anaerobic glycolysis; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR011304; L-lactate_DH.
DR   InterPro; IPR018177; L-lactate_DH_AS.
DR   InterPro; IPR001236; Lactate/malate_DH.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.90.110.10; lact_mal_DH; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 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   TIGRFAMs; TIGR01771; L-LDH-NAD; 1.
DR   PROSITE; PS00064; L_LDH; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Glycolysis; NAD; Oxidoreductase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    331       L-lactate dehydrogenase A chain.
FT                                /FTId=PRO_0000168431.
FT   NP_BIND      29     57       NAD (By similarity).
FT   ACT_SITE    192    192       Proton acceptor (By similarity).
FT   BINDING      98     98       NAD (By similarity).
FT   BINDING     105    105       Substrate (By similarity).
FT   BINDING     137    137       NAD or substrate (By similarity).
FT   BINDING     168    168       Substrate (By similarity).
FT   BINDING     247    247       Substrate (By similarity).
FT   STRAND        3     14
FT   STRAND       17     21
FT   STRAND       24     87
FT   STRAND       89     96
FT   STRAND      103    126
FT   STRAND      131    151
FT   STRAND      154    179
FT   STRAND      181    196
FT   STRAND      199    208
FT   STRAND      215    269
FT   STRAND      272    289
FT   STRAND      292    330
SQ   SEQUENCE   331 AA;  36156 MW;  556546DC3A03237E CRC64;
     MSTKEKLISH VMKEEPVGSR SKVTVVGVGM VGMASAISIL LKDLCDELAM VDVMEDKLKG
     EVMDLQHGSL FLKTKIVGDK DYSVTANSKV VVVTAGARQQ EGESRLNLVQ RNVNIFKFII
     PNIVKYSPNC ILMVVSNPVD ILTYVAWKLS GFPRHRVIGS GTNLDSARFR HLIGEKLHLH
     PSSCHAWIVG EHGDSSVPVW SGVNVAGVSL QGLNPQMGTE GDGENWKAIH KEVVDGAYEV
     IKLKGYTSWA IGMSVADLVE SIIKNMHKVH PVSTLVQGMH GVKDEVFLSV PCVLGNSGLT
     DVIHMTLKAE EEKQLQKSAE TLWGVQKELT L
//