ID Q9JYR9_NEIMB Unreviewed; 462 AA.
AC Q9JYR9;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 134.
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:AAF41817.1};
GN OrderedLocusNames=NMB1458 {ECO:0000313|EMBL:AAF41817.1};
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41817.1, ECO:0000313|Proteomes:UP000000425};
RN [1] {ECO:0000313|EMBL:AAF41817.1, ECO:0000313|Proteomes:UP000000425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41817.1,
RC ECO:0000313|Proteomes:UP000000425};
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L.,
RA White O., Fleischmann R.D., Dougherty B.A., Mason T., Ciecko A.,
RA Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H., Qin H., Vamathevan J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
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; AE002098; AAF41817.1; -; Genomic_DNA.
DR PIR; C81082; C81082.
DR RefSeq; NP_274469.1; NC_003112.2.
DR RefSeq; WP_002225106.1; NC_003112.2.
DR AlphaFoldDB; Q9JYR9; -.
DR STRING; 122586.NMB1458; -.
DR PaxDb; 122586-NMB1458; -.
DR KEGG; nme:NMB1458; -.
DR PATRIC; fig|122586.8.peg.1839; -.
DR HOGENOM; CLU_021594_4_1_4; -.
DR InParanoid; Q9JYR9; -.
DR OrthoDB; 9802809at2; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro.
DR GO; GO:0004333; F:fumarate hydratase activity; IBA:GO_Central.
DR GO; GO:0006106; P:fumarate metabolic process; IBA:GO_Central.
DR GO; GO:0006108; P:malate metabolic process; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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; 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:AAF41817.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000425};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT DOMAIN 11..341
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 407..460
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
FT ACT_SITE 187
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT ACT_SITE 317
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 128..131
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 138..140
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 323..325
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT SITE 330
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
SQ SEQUENCE 462 AA; 49332 MW; 4E44AD0D3489F250 CRC64;
MSTRTEHDTM GNVEVPSEAY WGAQTQRSRN NFKIGGETLP QPLIYALALV KKAAAATNVS
LGRIKPEQAD LITQAADDVL SGKLDGQFPL VVWQTGSGTQ SNMNMNEVLA NRANEIAGTG
LAAYQPVHPN DHVNHAQSTN DAFPTAIHVA AAIEINRHLI PAVKALRDTL DKKAQAFAPI
VKIGRTHLQD ATPLTLGQEF SGYVSQLDHG LGRLNDALKD LYELALGGTA VGTGLNSHPE
YAEKAAAKLA ELSGLPFVSA PNKFEALGGR DAAVAASGAL KTLAASLNKI ANDIRWLASG
PRCGLGEIKI PENEPGSSIM PGKVNPTQCE AMTMVCCQVF GNDVTIGMAG ASGNFELNVY
MPVIAYNLLQ SIHLLGDACN SFNEHCAIGI EPVPEKIDYF LHHSLMLVTA LNRKIGYENA
AKVAKTAYKN NKSLRETAVE LGLLTGEEFD ELVVPADMVH PR
//
