ID   B2HT54_MYCMM            Unreviewed;       476 AA.
AC   B2HT54;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 92.
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=fum {ECO:0000313|EMBL:ACC42775.1};
GN   Synonyms=fumC {ECO:0000256|HAMAP-Rule:MF_00743};
GN   OrderedLocusNames=MMAR_4368 {ECO:0000313|EMBL:ACC42775.1};
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC42775.1, ECO:0000313|Proteomes:UP000001190};
RN   [1] {ECO:0000313|EMBL:ACC42775.1, ECO:0000313|Proteomes:UP000001190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
RN   [2] {ECO:0007829|PDB:3QBP}
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-474.
RX   PubMed=25613812; DOI=10.1016/j.tube.2014.12.003;
RA   Baugh L., Phan I., Begley D.W., Clifton M.C., Armour B., Dranow D.M.,
RA   Taylor B.M., Muruthi M.M., Abendroth J., Fairman J.W., Fox D.,
RA   Dieterich S.H., Staker B.L., Gardberg A.S., Choi R., Hewitt S.N.,
RA   Napuli A.J., Myers J., Barrett L.K., Zhang Y., Ferrell M., Mundt E.,
RA   Thompkins K., Tran N., Lyons-Abbott S., Abramov A., Sekar A.,
RA   Serbzhinskiy D., Lorimer D., Buchko G.W., Stacy R., Stewart L.J.,
RA   Edwards T.E., Van Voorhis W.C., Myler P.J.;
RT   "Increasing the structural coverage of tuberculosis drug targets.";
RL   Tuberculosis 95:142-148(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}.
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DR   EMBL; CP000854; ACC42775.1; -; Genomic_DNA.
DR   RefSeq; WP_012395931.1; NC_010612.1.
DR   PDB; 3QBP; X-ray; 1.85 A; A/B/C/D=1-474.
DR   PDBsum; 3QBP; -.
DR   AlphaFoldDB; B2HT54; -.
DR   SMR; B2HT54; -.
DR   STRING; 216594.MMAR_4368; -.
DR   GeneID; 34341026; -.
DR   KEGG; mmi:MMAR_4368; -.
DR   eggNOG; COG0114; Bacteria.
DR   HOGENOM; CLU_021594_4_1_11; -.
DR   OrthoDB; 9802809at2; -.
DR   UniPathway; UPA00223; UER01007.
DR   EvolutionaryTrace; B2HT54; -.
DR   Proteomes; UP000001190; 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   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; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3QBP};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00743};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00743};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001190};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT   DOMAIN          23..347
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          413..469
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
FT   ACT_SITE        192
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   ACT_SITE        323
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         109..111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         133..136
FT                   /ligand="substrate"
FT                   /note="in site B"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         143..145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         329..331
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   SITE            336
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
SQ   SEQUENCE   476 AA;  50192 MW;  EA3DEA92B5FFD49F CRC64;
     MAHSAHDDAD NDTEYRIEHD TMGEVRVPAK ALWRAQTQRA VENFPISGRG LERAQIRALG
     LLKGACAQVN MDLGLLAPEK AEAIIAAAAE IADGQHDDQF PIDVFQTGSG TSSNMNTNEV
     IASIAGANGV AVHPNDDVNM SQSSNDTFPT ATHIAATEAA VSHLIPALEI LQDALATKAL
     EWQSVVKSGR THLMDAVPVT LGQEFSGYAR QIEAGIERVR ATLPRLGELA IGGTAVGTGL
     NAPEGFGVKV VSVLVSQTGL PQLRTAANSF EAQAARDGLV EASGALRTIA VSLTKIANDI
     RWMGSGPLTG LAEIQLPDLQ PGSSIMPGKV NPVLPEAVTQ VAAQVIGNDA AVAWGGANGA
     FELNVYIPMM ARNILESFTL LTNVSKLFAQ RCIAGLTANA EHLRELAESS PSIVTPLNSA
     IGYEEAAAVA KQALKERKTI RQTVIDRGLI GDKLSLEELD RRLDVLAMAK VEATDD
//