ID G8PH93_PSEUV Unreviewed; 493 AA.
AC G8PH93;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
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:AEV38963.1};
GN OrderedLocusNames=PSE_4461 {ECO:0000313|EMBL:AEV38963.1};
OS Pseudovibrio sp. (strain FO-BEG1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Stappiaceae; Pseudovibrio.
OX NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV38963.1, ECO:0000313|Proteomes:UP000005634};
RN [1] {ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT interacting bacteria.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEV38963.1, ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV38963.1,
RC ECO:0000313|Proteomes:UP000005634};
RX PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT for symbiosis.";
RL Environ. Microbiol. 15:2095-2113(2013).
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 ---------------------------------------------------------------------------
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; CP003147; AEV38963.1; -; Genomic_DNA.
DR AlphaFoldDB; G8PH93; -.
DR STRING; 911045.PSE_4461; -.
DR KEGG; psf:PSE_4461; -.
DR eggNOG; COG0114; Bacteria.
DR HOGENOM; CLU_021594_4_1_5; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000005634; 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; 1.10.40.30; 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, ECO:0000313|EMBL:AEV38963.1};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT DOMAIN 44..372
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 438..490
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
FT ACT_SITE 218
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT ACT_SITE 348
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 128..130
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 159..162
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 169..171
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 354..356
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT SITE 361
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
SQ SEQUENCE 493 AA; 52716 MW; BEE89A03F5F6E04A CRC64;
MSSFVAFFFQ ETARVFGTAL WRRVSMSAQD SDSMRQESDS FGVLDVPVGK YWGAQTARSL
INFPIGREHL PPALIHALGA VKLAAAKVNM EEGRLPEDLG KAICQAATEV ISGKLDAHFP
LVIWQTGSGT QSNMNTNEVI ANRAIELLGG QIGSKSPVHP NDHVNMGQSS NDTFPTAMHI
AAACEINKVL LPALVHLHDT LEAKVAAFSD IVKIGRTHTQ DATPLTLGQE FSGYVAQLEY
SKERIEQSLV GLYRLAQGGT AVGTGLNSTP EFASAFATHV SEVTGLPFVT ATNKFEALAT
HDAAVFAHGA LNTLACSLMK IANDIRFLAS GPRSGLGEIS LPANEPGSSI MPGKVNPTQC
EAVTMVCAQV MGNQTAVSVA GATGHFELNV FKPVIANSLL QSIELLADCM VSFADRCVVG
IEPNLDRIEE LMERSLMLVT ALAPTIGYDK ATEIAKSAHK NGTTLKEEAL RLGYVTAEEF
DRVVRPEKMV RPG
//
