ID A0A160FLW9_9BURK Unreviewed; 466 AA.
AC A0A160FLW9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=AYM40_14865 {ECO:0000313|EMBL:ANB73491.1};
OS Paraburkholderia phytofirmans OLGA172.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1417228 {ECO:0000313|EMBL:ANB73491.1, ECO:0000313|Proteomes:UP000076852};
RN [1] {ECO:0000313|EMBL:ANB73491.1, ECO:0000313|Proteomes:UP000076852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLGA172 {ECO:0000313|EMBL:ANB73491.1,
RC ECO:0000313|Proteomes:UP000076852};
RX PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT chlorocatechol degradative operon in a region of genome plasticity.";
RL Gene 586:239-247(2016).
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; CP014578; ANB73491.1; -; Genomic_DNA.
DR RefSeq; WP_063496873.1; NZ_CP014578.1.
DR AlphaFoldDB; A0A160FLW9; -.
DR STRING; 1804984.AYM40_14865; -.
DR KEGG; buz:AYM40_14865; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000076852; Chromosome 1.
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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000076852};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT DOMAIN 13..343
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 409..461
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
FT ACT_SITE 189
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT ACT_SITE 319
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 99..101
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 130..133
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 140..142
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 325..327
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT SITE 332
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
SQ SEQUENCE 466 AA; 49757 MW; BF57CB7944A0A70C CRC64;
MTEDVRMERD TFGEIAVPNT RLWGAQTQRS LQNFRISSEK QSPELITALA VIKRAAAEVN
LGLGVLDESK AKAIMQAADE IIDGKHPEEF PLAVWQTGSG TQTNMNLNEV IANRASELLG
GERGEARKVH PNDDVNRGQS SNDVFPTAMH VAAAYAAVKH LLPALKTLRD TLDGKAKAFA
DIVKIGRTHL QDATPLTLGQ EFSGYVAQLD HGIRHVESAL PHLYELAQGG TAVGTGLNAH
PQFADKVAAA IGKLTGLPFV SAPNKFEVMA GADALVFAHG ALKTVAASLN KIANDIRWLA
SGPRCGLGEL SIPENEPGSS IMPGKVNPTQ SEALTMLCAQ VFGNDVAVNI GGASGNFELN
VFRPMIAHNV LQSVRLLADG AHSFNDNCAV GIEPNRERID TLLNESLMLV TALNPHIGYD
KAAQIAKKAH KEGTTLKAAA LALGYVTEQQ FDEWVRPKDM VGHSAG
//
