ID A0A1X2C4B4_9MYCO Unreviewed; 474 AA.
AC A0A1X2C4B4;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
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:BBX63055.1};
GN Synonyms=aspA {ECO:0000313|EMBL:ORW70654.1};
GN ORFNames=AWC23_16370 {ECO:0000313|EMBL:ORW70654.1}, MSAS_22290
GN {ECO:0000313|EMBL:BBX63055.1};
OS Mycobacterium saskatchewanense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium simiae complex.
OX NCBI_TaxID=220927 {ECO:0000313|EMBL:BBX63055.1, ECO:0000313|Proteomes:UP000467517};
RN [1] {ECO:0000313|EMBL:ORW70654.1, ECO:0000313|Proteomes:UP000193387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44616 {ECO:0000313|EMBL:ORW70654.1,
RC ECO:0000313|Proteomes:UP000193387};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BBX63055.1, ECO:0000313|Proteomes:UP000467517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13016 {ECO:0000313|EMBL:BBX63055.1,
RC ECO:0000313|Proteomes:UP000467517};
RX PubMed=31287781;
RA Matsumoto Y., Kinjo T., Motooka D., Nabeya D., Jung N., Uechi K., Horii T.,
RA Iida T., Fujita J., Nakamura S.;
RT "Comprehensive subspecies identification of 175 nontuberculous mycobacteria
RT species based on 7547 genomic profiles.";
RL Emerg. Microbes Infect. 8:1043-1053(2019).
RN [3] {ECO:0000313|EMBL:BBX63055.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 13016 {ECO:0000313|EMBL:BBX63055.1};
RA Matsumoto Y., Motooka D., Nakamura S.;
RL Submitted (FEB-2020) 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}.
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DR EMBL; AP022573; BBX63055.1; -; Genomic_DNA.
DR EMBL; LQPR01000038; ORW70654.1; -; Genomic_DNA.
DR STRING; 220927.AWC23_16370; -.
DR KEGG; msak:MSAS_22290; -.
DR OrthoDB; 9802809at2; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000193387; Unassembled WGS sequence.
DR Proteomes; UP000467517; 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 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00743};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00743};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT DOMAIN 22..346
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 412..468
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
FT ACT_SITE 191
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT ACT_SITE 322
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 108..110
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 132..135
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 142..144
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 328..330
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT SITE 335
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
SQ SEQUENCE 474 AA; 50325 MW; C1E71DFE746E14EE CRC64;
MADSALQDNT DTEYRIEHDT MGEVRVPAKA LWRAQTQRAV ENFPISGRGL ERTQIRALGL
LKGACAQVNK DLGLLAPEKA DAIIAAAAEI ADGQHDDQFP IDVFQTGSGT SSNMNTNEVI
ASIAAANGVT VHPNDDVNMS QSSNDTFPTA THIAATEAAV RHLIPALEVL HDALAGKARE
WHTVVKSGRT HLMDAVPVTL GQEFSGYARQ IEAGIERVRA TLPRLGELAI GGTAVGTGLN
APDGFGARVV ETLIVSTGLN ELRPAKNSFE AQAARDGLVE ASGALRTIAV SLTKIANDIR
WMGSGPLTGL AEIRLPDLQP GSSIMPGKVN PVLPEAVTQV AAQVIGNDAA VTVGGLSGAF
ELNVYIPMMA RNILESFKLL TNVSRLFAER CIVGLAANVE HLRELAESSP SIVTPLNSAI
GYEEAAAVAK QALKERKTIR QTVIDRGLIG DKLSEEELDR RLDVLAMAKV KPED
//
