ID   FUMC_MYCTU              Reviewed;         474 AA.
AC   P9WN93; L0T5U4; O53446;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   16-APR-2014, entry version 1.
DE   RecName: Full=Fumarate hydratase class II;
DE            Short=Fumarase C;
DE            EC=4.2.1.2;
GN   Name=fumC; Synonyms=fum; OrderedLocusNames=Rv1098c;
GN   ORFNames=MTV017.51c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
RA   Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA   Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA   Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA   Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA   Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA   Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the
RT   complete genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS), AND SUBUNIT.
RG   Mycobacterium tuberculosis structural genomics consortium (TB);
RT   "Crystal structure of apo fumarate hydratase from Mycobacterium
RT   tuberculosis.";
RL   Submitted (JUL-2010) to the PDB data bank.
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF MUTANTS ALA-318 AND CYS-318
RP   IN COMPLEX WITH SUBSTRATES AND SUBSTRATE ANALOGS, MUTAGENESIS OF
RP   SER-318, CATALYTIC ACTIVITY, ACTIVE SITE, REACTION MECHANISM, AND
RP   SUBUNIT.
RX   PubMed=22561013; DOI=10.1016/j.febslet.2012.04.034;
RA   Mechaly A.E., Haouz A., Miras I., Barilone N., Weber P., Shepard W.,
RA   Alzari P.M., Bellinzoni M.;
RT   "Conformational changes upon ligand binding in the essential class II
RT   fumarase Rv1098c from Mycobacterium tuberculosis.";
RL   FEBS Lett. 586:1606-1611(2012).
CC   -!- FUNCTION: Catalyzes the reversible addition of water to fumarate
CC       to give L-malate.
CC   -!- CATALYTIC ACTIVITY: (S)-malate = fumarate + H(2)O.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-
CC       malate from fumarate: step 1/1.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC       Fumarase subfamily.
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DR   EMBL; AL123456; CCP43851.1; -; Genomic_DNA.
DR   PIR; H70896; H70896.
DR   PDB; 3NO9; X-ray; 2.48 A; A/B/C/D=1-474.
DR   PDB; 4ADL; X-ray; 2.20 A; A/B/C/D=1-473.
DR   PDB; 4ADM; X-ray; 1.65 A; A/B/C/D=1-473.
DR   PDB; 4APA; X-ray; 2.04 A; A/B/C/D=2-474.
DR   PDB; 4APB; X-ray; 1.94 A; A/B/C/D=2-474.
DR   PDBsum; 3NO9; -.
DR   PDBsum; 4ADL; -.
DR   PDBsum; 4ADM; -.
DR   PDBsum; 4APA; -.
DR   PDBsum; 4APB; -.
DR   TubercuList; Rv1098c; -.
DR   UniPathway; UPA00223; UER01007.
DR   HAMAP; MF_00743; FumaraseC; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Cytoplasm; Lyase; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    474       Fumarate hydratase class II.
FT                                /FTId=PRO_0000161289.
FT   REGION      104    106       Substrate binding.
FT   REGION      138    140       Substrate binding.
FT   REGION      186    187       Substrate binding.
FT   REGION      324    326       Substrate binding.
FT   ACT_SITE    187    187       Proton donor/acceptor (Probable).
FT   ACT_SITE    318    318       Probable.
FT   BINDING     319    319       Substrate.
FT   SITE        331    331       Important for catalytic activity (By
FT                                similarity).
FT   MUTAGEN     318    318       S->A: Absence of fumarate hydratase
FT                                activity.
FT   STRAND       10     15
FT   STRAND       18     23
FT   HELIX        30     38
FT   STRAND       41     43
FT   HELIX        48     67
FT   HELIX        73     87
FT   TURN         89     91
FT   HELIX        92     94
FT   STRAND       98    101
FT   HELIX       106    122
FT   TURN        129    136
FT   HELIX       139    157
FT   HELIX       159    176
FT   TURN        177    179
FT   STRAND      181    186
FT   STRAND      189    195
FT   HELIX       196    221
FT   TURN        229    231
FT   HELIX       241    253
FT   HELIX       266    269
FT   HELIX       272    298
FT   TURN        302    304
FT   STRAND      319    323
FT   HELIX       328    352
FT   HELIX       362    386
FT   HELIX       388    390
FT   HELIX       395    404
FT   HELIX       406    412
FT   HELIX       413    416
FT   HELIX       418    431
FT   HELIX       435    441
FT   STRAND      446    448
FT   HELIX       451    457
FT   HELIX       460    463
SQ   SEQUENCE   474 AA;  50141 MW;  4052F93F963D3DBB CRC64;
     MAVDADSANY RIEHDTMGEV RVPAKALWRA QTQRAVENFP ISGRGLERTQ IRALGLLKGA
     CAQVNSDLGL LAPEKADAII AAAAEIADGQ HDDQFPIDVF QTGSGTSSNM NTNEVIASIA
     AKGGVTLHPN DDVNMSQSSN DTFPTATHIA ATEAAVAHLI PALQQLHDAL AAKALDWHTV
     VKSGRTHLMD AVPVTLGQEF SGYARQIEAG IERVRACLPR LGELAIGGTA VGTGLNAPDD
     FGVRVVAVLV AQTGLSELRT AANSFEAQAA RDGLVEASGA LRTIAVSLTK IANDIRWMGS
     GPLTGLAEIQ LPDLQPGSSI MPGKVNPVLP EAVTQVAAQV IGNDAAIAWG GANGAFELNV
     YIPMMARNIL ESFKLLTNVS RLFAQRCIAG LTANVEHLRR LAESSPSIVT PLNSAIGYEE
     AAAVAKQALK ERKTIRQTVI DRGLIGDRLS IEDLDRRLDV LAMAKAEQLD SDRL
//