Q92PB6 (FUMC_RHIME) 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
Ordered Locus Names:	R01859
ORF Names:	SMc00149

Organism

Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

266834 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium › Rhizobium meliloti

Protein attributes

Sequence length	463 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	(S)-malate = fumarate + H2O. HAMAP-Rule MF_00743
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. HAMAP-Rule MF_00743
Subunit structure	Homotetramer. Ref.3
Subcellular location	Cytoplasm By similarity.
Miscellaneous	There are 2 substrate binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors By similarity. HAMAP-Rule MF_00743
Sequence similarities	Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.
Sequence caution	The sequence CAC46438.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Cytoplasm
Molecular function	Lyase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	fumarate metabolic process Inferred from electronic annotation. Source: InterPro tricarboxylic acid cycle Inferred from electronic annotation. Source: HAMAP
Cellular_component	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 – 463

463

Fumarate hydratase class II HAMAP-Rule MF_00743

PRO_0000161305

Regions

Region

98 – 100

3

Substrate binding By similarity

Region

129 – 132

4

B site By similarity

Region

139 – 141

3

Substrate binding By similarity

Region

187 – 188

2

Substrate binding By similarity

Region

324 – 326

3

Substrate binding By similarity

Sites

Active site

188

1

Proton donor/acceptor By similarity

Active site

318

1

By similarity

Binding site

319

1

Substrate By similarity

Site

331

1

Important for catalytic activity By similarity

Secondary structure

1

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463

Helix Strand Turn

Details...

Beta strand

4 – 9

6

Beta strand

12 – 17

6

Helix

24 – 32

9

Helix

42 – 61

20

Helix

67 – 81

15

Helix

86 – 88

3

Beta strand

92 – 95

4

Helix

100 – 117

18

Turn

122 – 125

4

Helix

130 – 134

5

Turn

135 – 137

3

Helix

140 – 158

19

Helix

160 – 178

19

Beta strand

182 – 187

6

Beta strand

190 – 196

7

Helix

197 – 217

21

Helix

219 – 222

4

Turn

230 – 232

3

Helix

242 – 254

13

Helix

264 – 269

6

Helix

272 – 298

27

Beta strand

302 – 305

4

Helix

328 – 352

25

Helix

362 – 386

25

Helix

388 – 390

3

Helix

395 – 404

10

Helix

407 – 411

5

Helix

413 – 416

4

Helix

418 – 431

14

Helix

435 – 440

6

Turn

441 – 443

3

Helix

447 – 453

7

Helix

456 – 458

3

Beta strand

459 – 461

3

Sequences

	Sequence		Length	Mass (Da)
	Q92PB6 [UniParc]. Last modified December 15, 2003. Version 2. Checksum: A500EDE8A6789C5F	FASTA	463	49,133
	10 20 30 40 50 60 MTSTRTETDT FGPIEVASDR YWGAQAQRSL GNFKIGWEKQ PLAIVRALGI VKQAAARANM 70 80 90 100 110 120 ALGRLDPAIG DAIVKAAQEV IDGKLDEHFP LVVWQTGSGT QSNMNANEVV SNRAIELLGG 130 140 150 160 170 180 VMGSKKPVHP NDHVNMSQSS NDTYPTAMHI ACAERVIHDL LPALKHLHKA LEEKVKAFDH 190 200 210 220 230 240 IIKIGRTHTQ DATPLTLGQE FSGYAAQVAS SIKRIEMTLP GLCELAQGGT AVGTGLNAPV 250 260 270 280 290 300 GFAEKVAEEI AAITGIGFTS APNKFEALAA HDSMVFSHGA INATAAALFK IANDIRFLGS 310 320 330 340 350 360 GPRSGLGELS LPENEPGSSI MPGKVNPTQC EALTQVCVQV FGNHAALTFA GSQGHFELNV 370 380 390 400 410 420 YNPLMAYNFL QSVQLLADAA ISFTDNCVVG IEAREDNIKA ALDRSLMLVT ALAPKIGYDN 430 440 450 460 AAKIAKTAHK NGTTLREEAV GGGYVTDEEF DAVVRPETMI GPA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021." Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F. Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.
[2]	"The composite genome of the legume symbiont Sinorhizobium meliloti." Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J. Science 293:668-672(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.
[3]	"Crystal structure of a fumarate hydratase." New York structural genomics research consortium (NYSGRC) Eswaramoorthy S., Evans B., Foti R., Gizzi A., Hillerich B., Kar A., Seidel J.L.R., Villigas G., Zencheck W., Almo S.C., Swaminathan S. Submitted (JUL-2010) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AL591688 Genomic DNA. Translation: CAC46438.1. Different initiation.

RefSeq

NP_385965.3. NC_003047.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4HGV	X-ray	2.09	A/B/C/D	1-463	[»]

ProteinModelPortal

Q92PB6.

SMR

Q92PB6. Positions 5-462.

ModBase

Search...

Protein-protein interaction databases

STRING

266834.SMc00149.

Proteomic databases

ProMEX

Q92PB6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAC46438; CAC46438; SMc00149.

GeneID

1233524.

KEGG

sme:SMc00149.

PATRIC

23633127. VBISinMel96828_3302.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG0114.

HOGENOM

HOG000061736.

KO

K01679.

ProtClustDB

PRK00485.

Enzyme and pathway databases

BioCyc

SMEL266834:GJF6-1907-MONOMER.

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.

TIGRFAMs

TIGR00979. fumC_II. 1 hit.

PROSITE

PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

FUMC_RHIME

Accession

Primary (citable) accession number: Q92PB6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	December 15, 2003
Last modified:	May 1, 2013
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program