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 07-JAN-2015, entry version 9. 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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS]. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=21969609; DOI=10.1074/mcp.M111.011627; RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., RA Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H., RA Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., RA Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S., RA Dash D., Pandey A.; RT "Proteogenomic analysis of Mycobacterium tuberculosis by high RT resolution mass spectrometry."; RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011). RN [3] 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 [4] 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 {ECO:0000269|PubMed:22561013}. CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)- CC malate from fumarate: step 1/1. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:22561013, CC ECO:0000269|Ref.3}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. CC Fumarase subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL123456; CCP43851.1; -; Genomic_DNA. DR PIR; H70896; H70896. DR RefSeq; NP_215614.1; NC_000962.3. DR RefSeq; YP_006514467.1; NC_018143.2. 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 ProteinModelPortal; P9WN93; -. DR SMR; P9WN93; 10-465. DR GeneID; 13319670; -. DR GeneID; 885651; -. DR KEGG; mtu:Rv1098c; -. DR KEGG; mtv:RVBD_1098c; -. DR TubercuList; Rv1098c; -. DR KO; K01679; -. DR OMA; NTPKGYD; -. DR PhylomeDB; P9WN93; -. DR UniPathway; UPA00223; UER01007. DR Proteomes; UP000001584; Chromosome. DR GO; GO:0005618; C:cell wall; IDA:MTBBASE. DR GO; GO:0005829; C:cytosol; IDA:MTBBASE. DR GO; GO:0005576; C:extracellular region; IDA:MTBBASE. DR GO; GO:0005886; C:plasma membrane; IDA:MTBBASE. DR GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro. DR GO; GO:0004333; F:fumarate hydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006106; P:fumarate metabolic process; IEA:InterPro. DR GO; GO:0040007; P:growth; IMP:MTBBASE. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.275.10; -; 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; PTHR11444; 1. DR Pfam; PF10415; FumaraseC_C; 1. DR Pfam; PF00206; Lyase_1; 1. DR PRINTS; PR00149; FUMRATELYASE. DR SUPFAM; SSF48557; SSF48557; 1. DR PROSITE; PS00163; FUMARATE_LYASES; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; Lyase; KW Reference proteome; Tricarboxylic acid cycle. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:21969609}. FT CHAIN 2 474 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. FT {ECO:0000305|PubMed:22561013}. FT ACT_SITE 318 318 {ECO:0000305|PubMed:22561013}. FT BINDING 319 319 Substrate. FT SITE 331 331 Important for catalytic activity. FT {ECO:0000250}. FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000269|PubMed:21969609}. FT MUTAGEN 318 318 S->A: Absence of fumarate hydratase FT activity. {ECO:0000269|PubMed:22561013}. FT STRAND 10 15 {ECO:0000244|PDB:4ADM}. FT STRAND 18 23 {ECO:0000244|PDB:4ADM}. FT HELIX 30 38 {ECO:0000244|PDB:4ADM}. FT STRAND 41 43 {ECO:0000244|PDB:4ADM}. FT HELIX 48 67 {ECO:0000244|PDB:4ADM}. FT HELIX 73 87 {ECO:0000244|PDB:4ADM}. FT TURN 89 91 {ECO:0000244|PDB:4APB}. FT HELIX 92 94 {ECO:0000244|PDB:4ADM}. FT STRAND 98 101 {ECO:0000244|PDB:4ADM}. FT HELIX 106 122 {ECO:0000244|PDB:4ADM}. FT TURN 129 136 {ECO:0000244|PDB:4ADM}. FT HELIX 139 157 {ECO:0000244|PDB:4ADM}. FT HELIX 159 176 {ECO:0000244|PDB:4ADM}. FT TURN 177 179 {ECO:0000244|PDB:4ADM}. FT STRAND 181 186 {ECO:0000244|PDB:4ADM}. FT STRAND 189 195 {ECO:0000244|PDB:4ADM}. FT HELIX 196 221 {ECO:0000244|PDB:4ADM}. FT TURN 229 231 {ECO:0000244|PDB:4ADM}. FT HELIX 241 253 {ECO:0000244|PDB:4ADM}. FT HELIX 266 269 {ECO:0000244|PDB:4ADM}. FT HELIX 272 298 {ECO:0000244|PDB:4ADM}. FT TURN 302 304 {ECO:0000244|PDB:3NO9}. FT STRAND 319 323 {ECO:0000244|PDB:4APB}. FT HELIX 328 352 {ECO:0000244|PDB:4ADM}. FT HELIX 362 386 {ECO:0000244|PDB:4ADM}. FT HELIX 388 390 {ECO:0000244|PDB:4ADM}. FT HELIX 395 404 {ECO:0000244|PDB:4ADM}. FT HELIX 406 412 {ECO:0000244|PDB:4ADM}. FT HELIX 413 416 {ECO:0000244|PDB:4ADM}. FT HELIX 418 431 {ECO:0000244|PDB:4ADM}. FT HELIX 435 441 {ECO:0000244|PDB:4ADM}. FT STRAND 446 448 {ECO:0000244|PDB:4APB}. FT HELIX 451 457 {ECO:0000244|PDB:4ADM}. FT HELIX 460 463 {ECO:0000244|PDB:4ADM}. 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 //