Q8NRN8 (FUMC_CORGL) 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:	Cgl1010, cg1145

Organism

Corynebacterium glutamicum (Brevibacterium flavum)

Taxonomic identifier

1718 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	473 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.
Sequence caution	The sequence CAF19712.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Cytoplasm
Molecular function	Lyase
Technical term	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 – 473	473	Fumarate hydratase class II HAMAP MF_00743		PRO_0000161272
Regions
	Region	128 – 131	4	B site By similarity
	Region	138 – 140	3	Substrate binding By similarity
Sites
	Binding site	106	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8NRN8 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 315AF884777A39F0	FASTA	473	50,244
	10 20 30 40 50 60 MSDFMTEQEF RIEHDTMGEV KVPAKALWQA QTQRAVENFP ISGRGLESAQ IRAMGLLKAA 70 80 90 100 110 120 CAQVNKDSGA LDAEKADAII AAGKEIASGK HDAEFPIDVF QTGSGTSSNM NTNEVIASIA 130 140 150 160 170 180 KANGVEVHPN DHVNMGQSSN DTFPTATHVA ATEAAVNDLI PGLKVLHESL AKKANEWSEV 190 200 210 220 230 240 VKSGRTHLMD AVPVTLGQEF GGYARQIQLG IERVEATLPR LGELAIGGTA AGTGINTSAD 250 260 270 280 290 300 FGGKVVAELI NLTDVKELKE AENHFEAQAA RDALVEFSGA MRVIAVSLYK IANDIRLMGS 310 320 330 340 350 360 GPLTGLGEIR LPDLQPGSSI MPGKVNPVLC ETATQVSAQV IGNDAAVAFS GTQGQFELNV 370 380 390 400 410 420 FIPVMARNVL ESARLLANTS RVFATRLVDG IEPNEAHMKE LAESSPSIVT PLNSAIGYEA 430 440 450 460 470 AAKVAKTALA EGKTIRQTVI DLGLVDGEKL TEEELDKRLD VLAMAHTERE NKF

References

[1]	"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]	"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000036 Genomic DNA. Translation: BAB98403.1. BX927151 Genomic DNA. Translation: CAF19712.1. Different initiation.
RefSeq	NP_600233.1. NC_003450.3. YP_225298.1. NC_006958.1.
3D structure databases
ProteinModelPortal	Q8NRN8.
ModBase	Search...
2D gel databases
World-2DPAGE	0001:Q8NRN8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1018996. 3344954.
GenomeReviews	Gene locus Cgl1010 in contig BA000036_GR. Gene locus cg1145 in contig BX927147_GR.
KEGG	cgb:cg1145. cgl:NCgl0967.
PATRIC	21494066. VBICorGlu203724_0990.
Phylogenomic databases
HOGENOM	HBG284369.
OMA	RIEKDTM.
PhylomeDB	Q8NRN8.
ProtClustDB	PRK00485.
Enzyme and pathway databases
BioCyc	CGLU196627:CG1145-MONOMER.
BRENDA	4.2.1.2. 1648.
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.
PROSITE	PS00163. FUMARATE_LYASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FUMC_CORGL

Accession

Primary (citable) accession number: Q8NRN8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	October 1, 2002
Last modified:	January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program