Q9ZCQ4 (FUMC_RICPR) 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:	RP665

Organism

Rickettsia prowazekii (strain Madrid E)

Taxonomic identifier

272947 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	(S)-malate = fumarate + H2O. HAMAP MF_00743
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. HAMAP MF_00743
Subunit structure	Homotetramer By similarity. HAMAP MF_00743
Subcellular location	Cytoplasm By similarity HAMAP MF_00743.
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 MF_00743
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 tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	tricarboxylic acid cycle enzyme complex Inferred from electronic annotation. Source: InterPro
Molecular function	fumarate hydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 461

461

Fumarate hydratase class II HAMAP MF_00743

PRO_0000161307

Regions

Region

129 – 132

4

B site By similarity

Region

139 – 141

3

Substrate binding By similarity

Sites

Binding site

100

1

Substrate By similarity

Secondary structure

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461

Helix Strand Turn

Details...

Beta strand

4 – 7

4

Beta strand

14 – 17

4

Helix

25 – 32

8

Helix

42 – 61

20

Helix

67 – 81

15

Beta strand

92 – 94

3

Helix

101 – 118

18

Helix

130 – 134

5

Helix

140 – 158

19

Helix

160 – 175

16

Helix

178 – 180

3

Helix

197 – 201

5

Helix

205 – 219

15

Turn

220 – 223

4

Helix

243 – 254

12

Helix

264 – 269

6

Helix

272 – 277

6

Helix

281 – 297

17

Helix

328 – 340

13

Helix

344 – 349

6

Helix

362 – 386

25

Helix

395 – 404

10

Helix

406 – 408

3

Helix

409 – 412

4

Turn

413 – 415

3

Helix

419 – 430

12

Helix

435 – 441

7

Helix

447 – 454

8

Sequences

	Sequence		Length	Mass (Da)
	Q9ZCQ4 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: C9929CC94E7E617D	FASTA	461	51,008
	10 20 30 40 50 60 MKNYRIESDS FGEIQIEEKF YWGAQTQRSL NNFKISKQKM PKILIRALAI LKKCAAQVNY 70 80 90 100 110 120 EFGDLEYKIA TSIDKAIDRI LAGEFEDNFP LVVWQTGSGT QTNMNMNEVI ASIANEELTG 130 140 150 160 170 180 KKGGKFPVHP NDHVNKGQSS NDSFPTAMHI ATVLATKQQL IPALNNLLTY LQDKSKDWDK 190 200 210 220 230 240 IIKIGRTHLQ DATPLTLKQE FSGYITQIEY ALERIEDALK KVYLLAQGGT AVGTGINSKI 250 260 270 280 290 300 GFDIKFAQKV AEFTQQPFKT APNKFESLAA HDALVEFSGT LNTIAVSLMK IANDIRLLGS 310 320 330 340 350 360 GPRCGLGELH LPENEPGSSI MPGKVNPTQV EALTMVCTQV MGNHVTVTIA GSNGHLELNV 370 380 390 400 410 420 FKPVIIYNIL QSIELLSDSV NSFVTHCVKG LEPNIARINT LRDKSLMLVT VLNPHIGYDN 430 440 450 460 AAKIAKEAHK YGITLKEAAK KLNFLSEEEF DKIVVPEKMI S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Rickettsia prowazekii and the origin of mitochondria." Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G. Nature 396:133-140(1998) [PubMed: 9823893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Madrid E.
[2]	"2.4 Angstrom crystal structure of fumarate hydratase from Rickettsia prowazekii." Seattle structural genomics center for infectious disease (SSGCID) Submitted (JUL-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH MALONATE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ235272 Genomic DNA. Translation: CAA15103.1.

PIR

E71672.

RefSeq

NP_221027.1. NC_000963.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3GTD	X-ray	2.40	A/B	1-461	[»]

ProteinModelPortal

Q9ZCQ4.

SMR

Q9ZCQ4. Positions 4-460.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

883633.

GenomeReviews

Gene locus RP665 in contig AJ235269_GR.

KEGG

rpr:RP665.

PATRIC

17902157. VBIRicPro72556_0685.

Phylogenomic databases

HOGENOM

HBG284369.

OMA

CAAQVNY.

ProtClustDB

PRK00485.

Enzyme and pathway databases

BioCyc

RPRO272947:RP665-MONOMER.

Family and domain databases

HAMAP

MF_00743. FumaraseC.
[Tree]

InterPro

IPR003031. D_crystallin.
IPR005677. Fum_hydII.
IPR018951. Fumarase_C_C.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR008948. L-Aspartase-like.
IPR024083. L-Aspartase-like_N.
IPR022761. Lyase1_N.
[Graphical view]

Gene3D

G3DSA:1.10.275.10. G3DSA:1.10.275.10. 1 hit.

KO

K01679.

Pfam

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

PRINTS

PR00145. ARGSUCLYASE.
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_RICPR

Accession

Primary (citable) accession number: Q9ZCQ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	May 1, 1999
Last modified:	January 25, 2012
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program