Q8TS07 (FUMC_METAC) 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:	MA_1001

Organism

Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)

Taxonomic identifier

188937 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length	484 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 AAM04432.1 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 – 484	484	Fumarate hydratase class II HAMAP MF_00743		PRO_0000161333
Regions
	Region	141 – 144	4	B site By similarity
	Region	151 – 153	3	Substrate binding By similarity
Sites
	Binding site	112	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8TS07 [UniParc]. Last modified December 15, 2003. Version 2. Checksum: 06F0EFE5664BEEC8	FASTA	484	52,127
	10 20 30 40 50 60 MPSILDLPIG TGATGKRKES DSLGEVEVPA DHYWGAQTQR SLIHFSIGDD YMPKEVYHAY 70 80 90 100 110 120 GYVKKAAALV NEAAGIIPPW KAELIARVAD EVIAGKLDSE FPLYVWQTGS GTQSNMNVNE 130 140 150 160 170 180 VISNRAIQLV GGSLGSKHPV HPNDDVNMSQ SSNDTFPTAM HIATVLEFSN RLIPAVTVLE 190 200 210 220 230 240 ESIWAKAREW VDIVKIGRTH LQDATPLTVG QEWSGYATQL DDALAFVKHS LRGLYRLAIG 250 260 270 280 290 300 GTAVGTGINT PPDFGEKVAD EIARLTGHPF VTAPNKFAAQ GSLDAMVTSS AALRTLAVAL 310 320 330 340 350 360 MKIANDLQWL GSGPRSGLHE LILPSDEPGS SIMPGKVNPT QEEAMLMVCI QVIGEDNAVA 370 380 390 400 410 420 FAGSQGNFEL NAMCPIIINN VLHSARTLGD ACVKFREYGI NGIMLDRSRI DKFVGTSLML 430 440 450 460 470 480 VTALSPVIGY DKASAIVQRA LDENTTLREA AVKGGFISAE DFDRIVDPKK MVGDPRHDLK LASE

References

[1]

"The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity." Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P. , McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., Metcalf W.W., Birren B. Genome Res. 12:532-542(2002) [PubMed: 11932238] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE010299 Genomic DNA. Translation: AAM04432.1. Different initiation.
RefSeq	NP_615952.1. NC_003552.1.
3D structure databases
ProteinModelPortal	Q8TS07.
SMR	Q8TS07. Positions 16-473.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1472891.
GenomeReviews	Gene locus MA_1001 in contig AE010299_GR.
KEGG	mac:MA1001.
NMPDR	fig|188937.1.peg.978.
Phylogenomic databases
HOGENOM	HBG284369.
OMA	QCEAMVM.
ProtClustDB	PRK00485.
Enzyme and pathway databases
BioCyc	MACE188937:MA1001-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_METAC

Accession

Primary (citable) accession number: Q8TS07

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	December 15, 2003
Last modified:	November 16, 2011
This is version 62 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program