ID I2N5I4_STRT9 Unreviewed; 486 AA.
AC I2N5I4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=aspA {ECO:0000313|EMBL:QKM67702.1};
GN Synonyms=fumC {ECO:0000256|HAMAP-Rule:MF_00743};
GN ORFNames=STSU_011530 {ECO:0000313|EMBL:QKM67702.1};
OS Streptomyces tsukubensis (strain DSM 42081 / NBRC 108919 / NRRL 18488 /
OS 9993).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1114943 {ECO:0000313|EMBL:QKM67702.1, ECO:0000313|Proteomes:UP000005940};
RN [1] {ECO:0000313|EMBL:QKM67702.1, ECO:0000313|Proteomes:UP000005940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 42081 / NBRC 108919 / NRRL 18488 / 9993
RC {ECO:0000313|Proteomes:UP000005940};
RX PubMed=22740677; DOI=10.1128/JB.00692-12;
RA Barreiro C., Prieto C., Sola-Landa A., Solera E., Martinez-Castro M.,
RA Perez-Redondo R., Garcia-Estrada C., Aparicio J.F.,
RA Fernandez-Martinez L.T., Santos-Aberturas J., Salehi-Najafabadi Z.,
RA Rodriguez-Garcia A., Tauch A., Martin J.F.;
RT "Draft genome of Streptomyces tsukubaensis NRRL 18488, the producer of the
RT clinically important immunosuppressant tacrolimus (FK506).";
RL J. Bacteriol. 194:3756-3757(2012).
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}.
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DR EMBL; CP029159; QKM67702.1; -; Genomic_DNA.
DR AlphaFoldDB; I2N5I4; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000005940; 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 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 PANTHER; PTHR11444; ASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE; 1.
DR PANTHER; PTHR11444:SF22; FUMARATE HYDRATASE CLASS II; 1.
DR Pfam; PF10415; FumaraseC_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
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, ECO:0000313|EMBL:QKM67702.1};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT DOMAIN 37..361
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 428..485
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
FT ACT_SITE 207
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT ACT_SITE 337
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 123..125
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 148..151
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 158..160
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 338
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 343..345
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT SITE 350
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
SQ SEQUENCE 486 AA; 50793 MW; 9191F16E7525806D CRC64;
MSAADGTDGT GTNTPTTTGS GGAGGDGRYR VEHDSMGEVR VPADAKWRAQ TQRAVANFPV
SGQRLEPSHI AALARVKAAA AVVNARLGVL EEDVAGAIAA AAAEVAAGRW DDQFPVDVFQ
TGSGTSSNMN MNEVLATLAE ERLGRPVHPN DQVNASQSSN DVFPSSIHIA ATAAVTGELI
PALEQLAGSL ERKAGEFARV VKSGRTHLMD ATPVTLGQEF GGYAAQVRYG VERLRSSLPR
LAELPLGGTA VGTGINTPPG FPAAVIAEVA RATGLPLTEA RDHFEAQGAR DGLVETSGQL
RTIAVSLTKI ANDLRWMASG PRTGLAEINL PDLQPGSSIM PGKVNPVVPE AVLMVAAQVT
GNDTTVAVAG AAGNFELNVM LPVMAKNLLE SVRLLAAASR LLADRTVDGI TANAERAREY
AESSPSVVTP LNKYLGYEEA AKIVKKSLAE RKTIRQVVLE SGHVERGALT VEQLDEALDV
LRMTRP
//
