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Database: UniProt
Entry: M3NEJ7_HELPX
LinkDB: M3NEJ7_HELPX
Original site: M3NEJ7_HELPX 
ID   M3NEJ7_HELPX            Unreviewed;       463 AA.
AC   M3NEJ7;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   08-NOV-2023, entry version 43.
DE   RecName: Full=Fumarate hydratase class II {ECO:0000256|HAMAP-Rule:MF_00743};
DE            Short=Fumarase C {ECO:0000256|HAMAP-Rule:MF_00743};
DE            EC=4.2.1.2 {ECO:0000256|HAMAP-Rule:MF_00743};
DE   AltName: Full=Aerobic fumarase {ECO:0000256|HAMAP-Rule:MF_00743};
DE   AltName: Full=Iron-independent fumarase {ECO:0000256|HAMAP-Rule:MF_00743};
GN   Name=fumC {ECO:0000256|HAMAP-Rule:MF_00743};
GN   ORFNames=HMPREF1408_01050 {ECO:0000313|EMBL:EMH05120.1};
OS   Helicobacter pylori GAM245Ai.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1159036 {ECO:0000313|EMBL:EMH05120.1, ECO:0000313|Proteomes:UP000011920};
RN   [1] {ECO:0000313|EMBL:EMH05120.1, ECO:0000313|Proteomes:UP000011920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GAM245Ai {ECO:0000313|EMBL:EMH05120.1,
RC   ECO:0000313|Proteomes:UP000011920};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Antonio M., Secka O.,
RA   Thomas J., Warren W., Mitreva M., Mardis E.R., Wilson R.K.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the TCA cycle. Catalyzes the stereospecific
CC       interconversion of fumarate to L-malate. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00743};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate
CC       from fumarate: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00743}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00743}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00743}.
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase
CC       subfamily. {ECO:0000256|ARBA:ARBA00009084, ECO:0000256|HAMAP-
CC       Rule:MF_00743}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMH05120.1}.
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DR   EMBL; APDL01000044; EMH05120.1; -; Genomic_DNA.
DR   RefSeq; WP_001945399.1; NZ_KB636505.1.
DR   AlphaFoldDB; M3NEJ7; -.
DR   PATRIC; fig|1159036.3.peg.995; -.
DR   HOGENOM; CLU_021594_4_1_7; -.
DR   UniPathway; UPA00223; UER01007.
DR   Proteomes; UP000011920; Unassembled WGS sequence.
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; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR   Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR   Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 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   NCBIfam; TIGR00979; fumC_II; 1.
DR   PANTHER; PTHR11444; ASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE; 1.
DR   PANTHER; PTHR11444:SF1; FUMARATE HYDRATASE, MITOCHONDRIAL; 1.
DR   Pfam; PF10415; FumaraseC_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00743};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00743};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT   DOMAIN          11..341
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          407..459
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
FT   ACT_SITE        187
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   ACT_SITE        317
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         97..99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         128..131
FT                   /ligand="substrate"
FT                   /note="in site B"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         138..140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         318
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         323..325
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   SITE            330
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
SQ   SEQUENCE   463 AA;  50892 MW;  7D400949E246FCD6 CRC64;
     MQFRIEHDTM GEIKVDDSQY WGAQTQRSLE NFKIGTEKMP KELIGAFAKL KRSLAVVNHK
     LGKLSLEKSQ AIIKACDCIL KGELCGEFPL AIWQTGSGTQ TNMNLNEVIA NKATEILGGN
     FREKKLIHPN DDVNMSQSSN DTFPTAMHVV SALEITHKLL PSLENLLKTF KEKSQQFKEI
     VKIGRTHLQD ATPLTLGQEF SGYASMLEHS KQQILESLEH LRELAIGGTA VGTGLNAHKE
     LSEKVAEELS QFSGVKFVSA PNKFHALTSH DAIAYAHGAF KALAANLMKI ANDIRWLASG
     PRCGLGELNI PENEPGSSIM PGKVNPTQCE AMTMVAVQVM GNDTAIGIAA SQGNFELNVF
     KPVIIYNFLQ SLRLLSDSME SFNIHCASGI EPNREKIDYY LHHSLMLVTA LNPHVGYENA
     AKIAKNAHKK GISLKESAVE LKLLSAEDFD KFVVPEKMIG PKA
//
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