ID A0A0J1GKT6_9GAMM Unreviewed; 462 AA.
AC A0A0J1GKT6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
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:KLV00313.1};
GN Synonyms=fumC {ECO:0000256|HAMAP-Rule:MF_00743};
GN ORFNames=ABT58_13185 {ECO:0000313|EMBL:KLV00313.1};
OS Photobacterium aphoticum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=754436 {ECO:0000313|EMBL:KLV00313.1, ECO:0000313|Proteomes:UP000036426};
RN [1] {ECO:0000313|EMBL:KLV00313.1, ECO:0000313|Proteomes:UP000036426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25995 {ECO:0000313|EMBL:KLV00313.1,
RC ECO:0000313|Proteomes:UP000036426};
RA Machado H., Gram L.;
RT "Photobacterium galathea sp. nov.";
RL Submitted (MAY-2015) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-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:KLV00313.1}.
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DR EMBL; LDOV01000023; KLV00313.1; -; Genomic_DNA.
DR RefSeq; WP_047874887.1; NZ_PYMF01000003.1.
DR AlphaFoldDB; A0A0J1GKT6; -.
DR PATRIC; fig|754436.4.peg.2804; -.
DR OrthoDB; 9802809at2; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000036426; 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 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:KLV00313.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036426};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT DOMAIN 13..337
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 403..455
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
FT ACT_SITE 183
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT ACT_SITE 313
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 134..136
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 319..321
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT SITE 326
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
SQ SEQUENCE 462 AA; 49263 MW; E11DDC9A0161148F CRC64;
MTHEYRIETD SMGDVQVPKN ALYRAQTQRA INNFPLSGIP LPPLFIQTLA YIKQAAARSN
LELGLLEHDK AHAIIDSCQL IIDGQHLDQF PIDTFQTGSG TSSNMNANEV IATLASIRLG
HSVDANDDVN MGQSSNDVIP TAIQVSSALA CHSLLFPAID HAIETLAERI AAIGDTVKTG
RTHLMDAMPI TLGQELAGWQ TQLLKARKGI EHALEEVTAL AQGGTAVGTG INTAPEFAVI
FANNISVSTE VEFTVSDNFF YNLSSQDAIV ALSGQIKTAA VALMKMSNDL RWMNSGPLAG
LREIELEGLQ PGSSIMPGKV NPVIPESTAM IAAQVIGNDT TITVAGQSGN FQLNVMLPLI
AHNILQSIEL LANGLTVLAD KALATFTVND ATLQQALAKN PILVTALNPI IGYAKAAAIA
KKAYAEQREI IDVAAEETEM SREQLTTLLN PYHLTQGGVA DQ
//
