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LDH_SELRU
ID   LDH_SELRU               Reviewed;         318 AA.
AC   Q9EVR0;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=L-lactate dehydrogenase;
DE            Short=L-LDH;
DE            EC=1.1.1.27;
GN   Name=ldh; Synonyms=ldhL;
OS   Selenomonas ruminantium.
OC   Bacteria; Firmicutes; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Selenomonas.
OX   NCBI_TaxID=971;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC   STRAIN=HD4;
RX   PubMed=11821921; DOI=10.1007/s00284-001-0082-9;
RA   Evans J.D., Martin S.A.;
RT   "Cloning of the L-lactate dehydrogenase gene from the ruminal bacterium
RT   Selenomonas ruminantium HD4.";
RL   Curr. Microbiol. 44:155-160(2002).
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:0000269|PubMed:11821921};
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; AF287913; AAG01001.1; -; Genomic_DNA.
DR   RefSeq; WP_014423306.1; NZ_FRBC01000007.1.
DR   PDB; 7NAY; X-ray; 1.84 A; A=1-318.
DR   PDBsum; 7NAY; -.
DR   AlphaFoldDB; Q9EVR0; -.
DR   SMR; Q9EVR0; -.
DR   STRING; 1392502.JNIO01000007_gene1117; -.
DR   eggNOG; COG0039; Bacteria.
DR   OMA; AWSHVTI; -.
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; 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.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; NAD; Oxidoreductase; Phosphoprotein.
FT   CHAIN           1..318
FT                   /note="L-lactate dehydrogenase"
FT                   /id="PRO_0000168378"
FT   ACT_SITE        180
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         13..41
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         225
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   STRAND          6..10
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   HELIX           14..25
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   STRAND          30..35
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   HELIX           39..52
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   STRAND          62..65
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   HELIX           68..71
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   STRAND          75..79
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   HELIX           93..96
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   HELIX           97..114
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   STRAND          116..122
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   STRAND          124..126
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   HELIX           127..136
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   HELIX           142..144
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   STRAND          145..147
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   HELIX           151..165
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   HELIX           169..171
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   STRAND          172..178
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   STRAND          184..193
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   HELIX           198..200
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   HELIX           201..204
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   HELIX           213..231
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   HELIX           236..250
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   STRAND          255..265
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   HELIX           266..268
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   STRAND          270..281
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   STRAND          284..288
FT                   /evidence="ECO:0007829|PDB:7NAY"
FT   HELIX           295..314
FT                   /evidence="ECO:0007829|PDB:7NAY"
SQ   SEQUENCE   318 AA;  34975 MW;  04B73C60F3630254 CRC64;
     MNNRRKIVVI GASNVGSAVA NKIADFQLAT EVVLIDLNED KAWGEAKDSS HATSCIYSTN
     IKFHLGDYED CKDANIIVIT AGPSIRPGET PDRLKLAGTN AKIMSSVMGE IVKRTKEAMI
     IMITNPLDVA TYVVSTQFDY PRNLILGTGT MLETYRFRRI LADKYQVDPK NINGYVLGEH
     GNAAFVAWST TGCAGFPIDD LDEYFHRTEK LSHEAVEQEL VQVAYDVINK KGFTNTGIAM
     AACRFIKSVL YDEHTILPCS AVLEGEYGIK DVALSIPRMV CADGIMRSFE VHLTDDELEK
     MHKAAQSVRS ALDGAGIK
 
 
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