ID A0A161W7N6_STAPS Unreviewed; 461 AA.
AC A0A161W7N6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 44.
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 ECO:0000313|EMBL:REA82445.1};
GN ORFNames=DD902_07540 {ECO:0000313|EMBL:PWZ74649.1}, DV961_05080
GN {ECO:0000313|EMBL:REA82445.1};
OS Staphylococcus pseudintermedius.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus; Staphylococcus intermedius group.
OX NCBI_TaxID=283734 {ECO:0000313|EMBL:REA82445.1, ECO:0000313|Proteomes:UP000256409};
RN [1] {ECO:0000313|EMBL:PWZ74649.1, ECO:0000313|Proteomes:UP000246800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST525 1 {ECO:0000313|EMBL:PWZ74649.1,
RC ECO:0000313|Proteomes:UP000246800};
RX PubMed=29292005; DOI=10.1016/j.vetmic.2017.11.018;
RA Worthing K.A., Abraham S., Coombs G.W., Pang S., Saputra S., Jordan D.,
RA Trott D.J., Norris J.M.;
RT "Clonal diversity and geographic distribution of methicillin-resistant
RT Staphylococcus pseudintermedius from Australian animals: Discovery of novel
RT sequence types.";
RL Vet. Microbiol. 213:58-65(2018).
RN [2] {ECO:0000313|EMBL:REA82445.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ST496-2 {ECO:0000313|EMBL:REA82445.1};
RX PubMed=30173756; DOI=10.1016/j.vetmic.2018.07.021;
RA Worthing K.A., Brown J., Gerber L., Abraham S., Trott D., Norris J.M.;
RT "Methicillin-resistant staphylococci amongst veterinary personnel,
RT personnel-owned pets, patients and the hospital environment of two small
RT animal veterinary hospitals.";
RL Vet. Microbiol. 223:79-85(2018).
RN [3] {ECO:0000313|Proteomes:UP000256409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST496-2 {ECO:0000313|Proteomes:UP000256409};
RA Worthing K.A., Brown J., Gerber L., Abraham S., Trott D., Norris J.M.;
RT "Molecular epidemiology of methicillin-resistant staphylococci amongst
RT veterinary personnel, personnel-owned pets, patients and the hospital
RT environment of two companion animal veterinary hospitals.";
RL Vet. Microbiol. 0:0-0(2018).
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:REA82445.1}.
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DR EMBL; QEIT01000034; PWZ74649.1; -; Genomic_DNA.
DR EMBL; QQPC01000028; REA82445.1; -; Genomic_DNA.
DR RefSeq; WP_014613534.1; NZ_WWPO01000015.1.
DR AlphaFoldDB; A0A161W7N6; -.
DR GeneID; 66876217; -.
DR eggNOG; COG0114; Bacteria.
DR OrthoDB; 9802809at2; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000246800; Unassembled WGS sequence.
DR Proteomes; UP000256409; 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; 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|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00743};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT DOMAIN 11..340
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 406..459
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
FT ACT_SITE 186
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT ACT_SITE 316
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 127..130
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 137..139
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 322..324
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT SITE 329
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
SQ SEQUENCE 461 AA; 50853 MW; D6B88582A96924E6 CRC64;
MSVRIEHDTF GQIEVPADKY WGAQTQRSKQ NFPVGKEKMP IEVVYGFAQL KRAAALANNE
LGKLSDAKKD AIVYACDRIL AGELDEHFPL VVWQTGSGTQ SNMNVNEVVS YVANEYLKEK
GSDETIHPND DVNKSQSSND TFPTAMHVAL YHEVEKRLEP ALKGLRETFY KKENEFKDII
KIGRTHLQDA TPITLGQEIS GWRYMLDVCE NLLAESKKHI LNLAIGGTAV GTGINAHPEF
GTKVAGYIAE NTGYPFVSSE NKFHALTAHD EVVQLHGSLK ALAGDLMKIA NDVRWLASGP
RAGLAEISIP ENEPGSSIMP GKVNPTQCEM LTMVAVQVMG NDTVVGFSSA QGNFELNVFK
PVILHNTLQS IYLLADGMET FNQNCAVGIE PIPENIDNYL NRSLMLVTAL NPHIGYEKAA
AIAKKAHKEG ITLKESAIQS GYVTEEQFEE WIKPENMVHP K
//
