O53446 (FUMC_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fumarate hydratase class II
Short name=Fumarase C
EC=4.2.1.2

Gene names

Name:	fumC
Synonyms:	fum
Ordered Locus Names:	Rv1098c, MT1130
ORF Names:	MTV017.51c

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	474 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reversible addition of water to fumarate to give L-malate. HAMAP-Rule MF_00743
Catalytic activity	(S)-malate = fumarate + H2O. Ref.4
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. HAMAP-Rule MF_00743
Subunit structure	Homotetramer. Ref.3 Ref.4
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Cytoplasm
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fumarate metabolic process Inferred from electronic annotation. Source: InterPro growth Inferred from mutant phenotype PubMed 12657046. Source: MTBBASE tricarboxylic acid cycle Inferred from electronic annotation. Source: HAMAP
Cellular_component	cell wall Inferred from direct assay PubMed 20825248. Source: MTBBASE cytosol Inferred from direct assay PubMed 15525680. Source: MTBBASE extracellular region Inferred from direct assay PubMed 17443846. Source: MTBBASE plasma membrane Inferred from direct assay PubMed 14532352PubMed 15525680. Source: MTBBASE tricarboxylic acid cycle enzyme complex Inferred from electronic annotation. Source: InterPro
Molecular_function	fumarate hydratase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 474

474

Fumarate hydratase class II HAMAP-Rule MF_00743

PRO_0000161289

Regions

Region

104 – 106

3

Substrate binding HAMAP-Rule MF_00743

Region

138 – 140

3

Substrate binding HAMAP-Rule MF_00743

Region

186 – 187

2

Substrate binding HAMAP-Rule MF_00743

Region

324 – 326

3

Substrate binding HAMAP-Rule MF_00743

Sites

Active site

187

1

Proton donor/acceptor Probable

Active site

318

1

Probable

Binding site

319

1

Substrate

Site

331

1

Important for catalytic activity By similarity

Experimental info

Mutagenesis

318

1

S → A: Absence of fumarate hydratase activity. Ref.4

Secondary structure

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474

Helix Strand Turn

Details...

Beta strand

10 – 15

6

Beta strand

18 – 23

6

Helix

30 – 38

9

Beta strand

41 – 43

3

Helix

48 – 67

20

Helix

73 – 87

15

Turn

89 – 91

3

Helix

92 – 94

3

Beta strand

98 – 101

4

Helix

106 – 122

17

Turn

129 – 136

8

Helix

139 – 157

19

Helix

159 – 176

18

Turn

177 – 179

3

Beta strand

181 – 186

6

Beta strand

189 – 195

7

Helix

196 – 221

26

Turn

229 – 231

3

Helix

241 – 253

13

Helix

266 – 269

4

Helix

272 – 298

27

Turn

302 – 304

3

Beta strand

319 – 323

5

Helix

328 – 352

25

Helix

362 – 386

25

Helix

388 – 390

3

Helix

395 – 404

10

Helix

406 – 412

7

Helix

413 – 416

4

Helix

418 – 431

14

Helix

435 – 441

7

Beta strand

446 – 448

3

Helix

451 – 457

7

Helix

460 – 463

4

Sequences

	Sequence		Length	Mass (Da)
	O53446 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 4052F93F963D3DBB	FASTA	474	50,141
	10 20 30 40 50 60 MAVDADSANY RIEHDTMGEV RVPAKALWRA QTQRAVENFP ISGRGLERTQ IRALGLLKGA 70 80 90 100 110 120 CAQVNSDLGL LAPEKADAII AAAAEIADGQ HDDQFPIDVF QTGSGTSSNM NTNEVIASIA 130 140 150 160 170 180 AKGGVTLHPN DDVNMSQSSN DTFPTATHIA ATEAAVAHLI PALQQLHDAL AAKALDWHTV 190 200 210 220 230 240 VKSGRTHLMD AVPVTLGQEF SGYARQIEAG IERVRACLPR LGELAIGGTA VGTGLNAPDD 250 260 270 280 290 300 FGVRVVAVLV AQTGLSELRT AANSFEAQAA RDGLVEASGA LRTIAVSLTK IANDIRWMGS 310 320 330 340 350 360 GPLTGLAEIQ LPDLQPGSSI MPGKVNPVLP EAVTQVAAQV IGNDAAIAWG GANGAFELNV 370 380 390 400 410 420 YIPMMARNIL ESFKLLTNVS RLFAQRCIAG LTANVEHLRR LAESSPSIVT PLNSAIGYEE 430 440 450 460 470 AAAVAKQALK ERKTIRQTVI DRGLIGDRLS IEDLDRRLDV LAMAKAEQLD SDRL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"Crystal structure of apo fumarate hydratase from Mycobacterium tuberculosis." Mycobacterium tuberculosis structural genomics consortium (TB) Submitted (JUL-2010) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS), SUBUNIT.
[4]	"Conformational changes upon ligand binding in the essential class II fumarase Rv1098c from Mycobacterium tuberculosis." Mechaly A.E., Haouz A., Miras I., Barilone N., Weber P., Shepard W., Alzari P.M., Bellinzoni M. FEBS Lett. 586:1606-1611(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF MUTANTS ALA-318 AND CYS-318 IN COMPLEX WITH SUBSTRATES AND SUBSTRATE ANALOGS, MUTAGENESIS OF SER-318, CATALYTIC ACTIVITY, ACTIVE SITE, REACTION MECHANISM, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BX842575 Genomic DNA. Translation: CAA17214.1.
AE000516 Genomic DNA. Translation: AAK45388.1.
AL123456 Genomic DNA. Translation: CCP43851.1.

PIR

H70896.

RefSeq

NP_215614.1. NC_000962.3.
NP_335574.1. NC_002755.2.
YP_006514467.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3NO9	X-ray	2.48	A/B/C/D	1-474	[»]
4ADL	X-ray	2.20	A/B/C/D	1-473	[»]
4ADM	X-ray	1.65	A/B/C/D	1-473	[»]
4APA	X-ray	2.04	A/B/C/D	2-474	[»]
4APB	X-ray	1.94	A/B/C/D	2-474	[»]

ProteinModelPortal

O53446.

SMR

O53446. Positions 10-465.

ModBase

Search...

Protein-protein interaction databases

STRING

83332.Rv1098c.

Proteomic databases

PaxDb

O53446.

PRIDE

O53446.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAK45388; AAK45388; MT1130.

GeneID

13319670.
885651.
924972.

KEGG

mtc:MT1130.
mtu:Rv1098c.
mtv:RVBD_1098c.

PATRIC

18124246. VBIMycTub22151_1243.

Organism-specific databases

TubercuList

Rv1098c.

Phylogenomic databases

eggNOG

COG0114.

HOGENOM

HOG000061736.

KO

K01679.

OMA

IIPTTIH.

ProtClustDB

PRK00485.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-11948.

UniPathway

UPA00223; UER01007.

Family and domain databases

Gene3D

1.10.275.10. 1 hit.

HAMAP

MF_00743. FumaraseC.

InterPro

IPR005677. Fum_hydII.
IPR024083. Fumarase/histidase_N.
IPR018951. Fumarase_C_C.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]

Pfam

PF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]

PRINTS

PR00149. FUMRATELYASE.

SUPFAM

SSF48557. L-Aspartase-like. 1 hit.

PROSITE

PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O53446.

Entry information

Entry name

FUMC_MYCTU

Accession

Primary (citable) accession number: O53446
Secondary accession number(s): L0T5U4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program