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LDHB_FUNHE
ID   LDHB_FUNHE              Reviewed;         334 AA.
AC   P20373;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=L-lactate dehydrogenase B chain;
DE            Short=LDH-B;
DE            EC=1.1.1.27 {ECO:0000250|UniProtKB:P07195};
GN   Name=ldhb;
OS   Fundulus heteroclitus (Killifish) (Mummichog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Fundulidae; Fundulus.
OX   NCBI_TaxID=8078;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=2615640; DOI=10.1093/oxfordjournals.molbev.a040559;
RA   Crawford D.L., Constantino H.R., Powers D.A.;
RT   "Lactate dehydrogenase-B cDNA from the teleost Fundulus heteroclitus:
RT   evolutionary implications.";
RL   Mol. Biol. Evol. 6:369-383(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8105474; DOI=10.1073/pnas.90.20.9271;
RA   Bernardi G., Sordino P., Powers D.A.;
RT   "Concordant mitochondrial and nuclear DNA phylogenies for populations of
RT   the teleost fish Fundulus heteroclitus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:9271-9274(1993).
CC   -!- FUNCTION: Interconverts simultaneously and stereospecifically pyruvate
CC       and lactate with concomitant interconversion of NADH and NAD(+).
CC       {ECO:0000250|UniProtKB:P07195}.
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:0000250|UniProtKB:P07195};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23445;
CC         Evidence={ECO:0000250|UniProtKB:P07195};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23446;
CC         Evidence={ECO:0000250|UniProtKB:P07195};
CC   -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC       from pyruvate: step 1/1. {ECO:0000250|UniProtKB:P07195}.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- POLYMORPHISM: Isolates from various regions of the US and Canada show
CC       some variations. PubMed:8105474 has sequenced LDH-B isolates called
CC       Florida 1A, 1B, 2A and 2B; Georgia 2A and 2B; Maine 2A; New Jersey
CC       121A, 121B, 137A, 137B and 197B; Nova Scotia 1A, 1B, 2A and 2B.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000305}.
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DR   EMBL; L23792; AAA49298.1; -; Genomic_DNA.
DR   EMBL; M33969; AAA49306.1; -; mRNA.
DR   EMBL; L23781; AAA49291.1; -; Genomic_DNA.
DR   EMBL; L23782; AAA49289.1; -; Genomic_DNA.
DR   EMBL; L23783; AAA49292.1; -; Genomic_DNA.
DR   EMBL; L23784; AAA49288.1; -; Genomic_DNA.
DR   EMBL; L23785; AAA49304.1; -; Genomic_DNA.
DR   EMBL; L23786; AAA49305.1; -; Genomic_DNA.
DR   EMBL; L23787; AAA49293.1; -; Genomic_DNA.
DR   EMBL; L23788; AAA49294.1; -; Genomic_DNA.
DR   EMBL; L23789; AAA49295.1; -; Genomic_DNA.
DR   EMBL; L23790; AAA49296.1; -; Genomic_DNA.
DR   EMBL; L23791; AAA49297.1; -; Genomic_DNA.
DR   EMBL; L23793; AAA49299.1; -; Genomic_DNA.
DR   EMBL; L23794; AAA49300.1; -; Genomic_DNA.
DR   EMBL; L23795; AAA49301.1; -; Genomic_DNA.
DR   EMBL; L23796; AAA49302.1; -; Genomic_DNA.
DR   EMBL; L23797; AAA49303.1; -; Genomic_DNA.
DR   PIR; A32430; A32430.
DR   PIR; I50555; I50555.
DR   RefSeq; NP_001296887.1; NM_001309958.1.
DR   AlphaFoldDB; P20373; -.
DR   SMR; P20373; -.
DR   STRING; 8078.ENSFHEP00000012921; -.
DR   GeneID; 105929819; -.
DR   CTD; 30497; -.
DR   OrthoDB; 1204514at2759; -.
DR   UniPathway; UPA00554; UER00611.
DR   Proteomes; UP000265000; Whole Genome Shotgun Assembly.
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   HAMAP; MF_00488; Lactate_dehydrog; 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   2: Evidence at transcript level;
KW   Cytoplasm; NAD; Oxidoreductase.
FT   CHAIN           1..334
FT                   /note="L-lactate dehydrogenase B chain"
FT                   /id="PRO_0000168476"
FT   ACT_SITE        194
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         30..58
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         139
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   VARIANT         10
FT                   /note="T -> P (in strain: Isolate New Jersey 121A)"
FT   VARIANT         45
FT                   /note="L -> P (in strain: Isolate Georgia 2B)"
FT   VARIANT         49
FT                   /note="L -> P (in strain: Isolate Nova Scotia 2B)"
FT   VARIANT         112
FT                   /note="Q -> R (in strain: Isolate New Jersey 137A)"
FT   VARIANT         114
FT                   /note="N -> S (in strain: Isolate New Jersey 137A)"
FT   VARIANT         185
FT                   /note="A -> S (in strain: Isolate Maine 2A, Isolate New
FT                   Jersey 121B, Isolate New Jersey 197B, Isolate Nova Scotia
FT                   1A, Isolate Nova Scotia 1B, Isolate Nova Scotia 2A and
FT                   Isolate Nova Scotia 2B)"
FT   VARIANT         287
FT                   /note="E -> D (in strain: Isolate Nova Scotia 1B and
FT                   Isolate Nova Scotia 2B)"
FT   VARIANT         301
FT                   /note="V -> L (in strain: Isolate New Jersey 197B)"
FT   VARIANT         311
FT                   /note="D -> A (in strain: Isolate Maine 2A, Isolate New
FT                   Jersey 137A, Isolate New Jersey 137B, Isolate New Jersey
FT                   197B, Isolate Nova Scotia 1A, Isolate Nova Scotia 1B,
FT                   Isolate Nova Scotia 2A and Isolate Nova Scotia 2B)"
SQ   SEQUENCE   334 AA;  36224 MW;  CE8CEF79D7C07B97 CRC64;
     MSSVLQKLIT PLASSSAEPP RNKVTVVGVG QVGMACAVSI LLRDLCDELA LVDVMEDRLK
     GEMMDLQHGL LFLKTSKVVA DKDYAVTANS RLVVVTAGVR QQEGESRLNL VQRNVNVFKC
     IIPQIIKYSP NCTILVVSNP VDVLTYVTWK LSGLPKHRVI GSGTNLDSAR FRYMMAERLG
     IHASAFNGWV LGEHGDTSVP VWSGANVAGV SLQKLNPEIG TDGDKEQWKA THKAVVDSAY
     EVIKLKGYTN WAIGFSVADL TESIVKNLSR VHPVSTMVKD MFGIGEEVFL SLPCVLNGSG
     VGSVVNMTLT DAEVAQLKKS ADTLWGIQKD LKDL
 
 
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