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Database: UniProt
Entry: A0A0A0EEU3_9RHOB
LinkDB: A0A0A0EEU3_9RHOB
Original site: A0A0A0EEU3_9RHOB 
ID   A0A0A0EEU3_9RHOB        Unreviewed;       463 AA.
AC   A0A0A0EEU3;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=ATO9_16870 {ECO:0000313|EMBL:KGM47737.1};
OS   Pseudooceanicola atlanticus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pseudooceanicola.
OX   NCBI_TaxID=1461694 {ECO:0000313|EMBL:KGM47737.1, ECO:0000313|Proteomes:UP000030004};
RN   [1] {ECO:0000313|EMBL:KGM47737.1, ECO:0000313|Proteomes:UP000030004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II-s11g {ECO:0000313|EMBL:KGM47737.1,
RC   ECO:0000313|Proteomes:UP000030004};
RX   PubMed=25663028; DOI=10.1007/s10482-015-0398-2;
RA   Lai Q., Li G., Liu X., Du Y., Sun F., Shao Z.;
RT   "Pseudooceanicola atlanticus gen. nov. sp. nov., isolated from surface
RT   seawater of the Atlantic Ocean and reclassification of Oceanicola
RT   batsensis, Oceanicola marinus, Oceanicola nitratireducens, Oceanicola
RT   nanhaiensis, Oceanicola antarcticus and Oceanicola flagellatus, as
RT   Pseudooceanicola batsensis comb. nov., Pseudooceanicola marinus comb. nov.,
RT   Pseudooceanicola nitratireducens comb. nov., Pseudooceanicola nanhaiensis
RT   comb. nov., Pseudooceanicola antarcticus comb. nov., and Pseudooceanicola
RT   flagellatus comb. nov.";
RL   Antonie Van Leeuwenhoek 107:1065-1074(2015).
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:KGM47737.1}.
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DR   EMBL; AQQX01000008; KGM47737.1; -; Genomic_DNA.
DR   RefSeq; WP_043751779.1; NZ_CP051248.1.
DR   AlphaFoldDB; A0A0A0EEU3; -.
DR   STRING; 1461694.ATO9_16870; -.
DR   eggNOG; COG0114; Bacteria.
DR   OrthoDB; 9802809at2; -.
DR   UniPathway; UPA00223; UER01007.
DR   Proteomes; UP000030004; 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|HAMAP-Rule:MF_00743};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030004};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT   DOMAIN          13..342
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          408..460
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
FT   ACT_SITE        188
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   ACT_SITE        318
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         98..100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         129..132
FT                   /ligand="substrate"
FT                   /note="in site B"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         139..141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         319
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         324..326
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   SITE            331
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
SQ   SEQUENCE   463 AA;  49488 MW;  1D9F844C4549C2A8 CRC64;
     MTQTRTESDS FGPLEVPSDK YWGAQTQRSI MNFPIGWEKQ PVAIVRALGV IKKACAMANK
     DNGALDPKLA DAIIQAAGEV VEGKFDDNFP LVVWQTGSGT QSNMNSNEVI ANRAIEILGG
     EIGSKDPVHP NDHCNMGQSS NDTFPTAMHI AAAMTARDVL LPGLEKLLAS LDAKAEEFKD
     IIKIGRTHTQ DATPLTLGQE FSGYAHQIRQ GIARINAALP GIYELAQGGT AVGTGLNTKK
     GWGEQVAANM AEITGLPFVT APNKFESLAA HDAMVFMSGA LATVAGSCYK IANDIRFLGS
     GPRSGLGELI LPENEPGSSI MPGKVNPTQA EAMTQVAAHV MGNDAAIKFA GSQGHFELNV
     YNPMMSYNLL QSMQLLGDVA DSFTERMLNG IQANEPRIEK LMKESLMLVT ALAPTIGYDN
     ATKVAKTAHK NGTTLKEEAI ALGFVDEETF DKVVRPEDMI GPK
//
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