位置:首页 > 蛋白库 > FUMC_HELPJ
FUMC_HELPJ
ID   FUMC_HELPJ              Reviewed;         463 AA.
AC   Q9ZJQ9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Fumarate hydratase class II {ECO:0000255|HAMAP-Rule:MF_00743};
DE            Short=Fumarase C {ECO:0000255|HAMAP-Rule:MF_00743};
DE            EC=4.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00743};
DE   AltName: Full=Aerobic fumarase {ECO:0000255|HAMAP-Rule:MF_00743};
DE   AltName: Full=Iron-independent fumarase {ECO:0000255|HAMAP-Rule:MF_00743};
GN   Name=fumC {ECO:0000255|HAMAP-Rule:MF_00743}; OrderedLocusNames=jhp_1245;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
CC   -!- FUNCTION: Involved in the TCA cycle. Catalyzes the stereospecific
CC       interconversion of fumarate to L-malate. {ECO:0000255|HAMAP-
CC       Rule:MF_00743}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:12460,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15589, ChEBI:CHEBI:29806; EC=4.2.1.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00743};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate
CC       from fumarate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00743}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00743}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00743}.
CC   -!- MISCELLANEOUS: There are 2 substrate-binding sites: the catalytic A
CC       site, and the non-catalytic B site that may play a role in the transfer
CC       of substrate or product between the active site and the solvent.
CC       Alternatively, the B site may bind allosteric effectors.
CC       {ECO:0000255|HAMAP-Rule:MF_00743}.
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00743}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE001439; AAD06830.1; -; Genomic_DNA.
DR   PIR; H71830; H71830.
DR   RefSeq; WP_001160501.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZJQ9; -.
DR   SMR; Q9ZJQ9; -.
DR   STRING; 85963.jhp_1245; -.
DR   EnsemblBacteria; AAD06830; AAD06830; jhp_1245.
DR   KEGG; hpj:jhp_1245; -.
DR   PATRIC; fig|85963.30.peg.1326; -.
DR   eggNOG; COG0114; Bacteria.
DR   OMA; HDSMGEV; -.
DR   UniPathway; UPA00223; UER01007.
DR   Proteomes; UP000000804; Chromosome.
DR   GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro.
DR   GO; GO:0004333; F:fumarate hydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006106; P:fumarate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd01362; Fumarase_classII; 1.
DR   Gene3D; 1.10.275.10; -; 1.
DR   HAMAP; MF_00743; FumaraseC; 1.
DR   InterPro; IPR005677; Fum_hydII.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR018951; Fumarase_C_C.
DR   InterPro; IPR020557; Fumarate_lyase_CS.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR022761; Fumarate_lyase_N.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   PANTHER; PTHR11444; PTHR11444; 1.
DR   Pfam; PF10415; FumaraseC_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   TIGRFAMs; TIGR00979; fumC_II; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lyase; Tricarboxylic acid cycle.
FT   CHAIN           1..463
FT                   /note="Fumarate hydratase class II"
FT                   /id="PRO_0000161281"
FT   ACT_SITE        187
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   ACT_SITE        317
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         97..99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         128..131
FT                   /ligand="substrate"
FT                   /note="in site B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         138..140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         318
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         323..325
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   SITE            330
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
SQ   SEQUENCE   463 AA;  50920 MW;  EF8EEF9CABD1D485 CRC64;
     MQFRIEHDTM GEIKVDDSQY WGAQTQRSLE NFKIGTEKMP KELIGAFAKL KRSLAVVNHK
     LGKLSLEKSQ AIIKACDCIL KGELCGEFPL AIWQTGSGTQ TNMNLNEVIA NKATEILGGN
     FREKKLIHPN DDVNMSQSSN DTFPTAMHVV SVLEITHKLL PSLENLLKTF KEKSQQFKEI
     VKIGRTHLQD ATPLTLGQEF SGYASMLEHS KQQILESLEH LRELAIGGTA VGTGLNAHKE
     LSEKVAEELS QFSGVKFISA PNKFHALTSH DAIAYAHGAF KALAANLMKI ANDIRWLASG
     PRCGLGELNI PENEPGSSIM PGKVNPTQCE AMTMVAVQVM GNDTAIGIAA SQGNFELNVF
     KPVIIYNFLQ SLRLLSDSME SFNIHCASGI EPNKEKIDYY LHHSLMLVTA LNPHVGYENA
     AKIAKNAHKK GISLKESALE LKLLSAEDFD QFVVPEKMIG PKA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024