Reviewed, UniProtKB/Swiss-Prot Q04718 (FUMA_BACST)

Names and origin

Protein names

Recommended name:
    Fumarate hydratase class I, aerobic
      Short name=Fumarase
    EC=4.2.1.2

Gene names

Name:

fumA

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	514 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	(S)-malate = fumarate + H2O.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the class-I fumarase family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Lyase
Gene Ontology (GO)
Biological process	tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW fumarate hydratase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 514	514	Fumarate hydratase class I, aerobic		PRO_0000195655
Sites
	Active site	358	1	Potential
	Metal binding	62	1	Iron-sulfur Potential
	Metal binding	187	1	Iron-sulfur Potential
	Metal binding	274	1	Iron-sulfur Potential
	Binding site	422	1	Substrate Potential

Sequences

	Sequence		Length	Mass (Da)
	Q04718-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 238F2890E8CC54E1	FASTA	514	56,792
	10 20 30 40 50 60 MEKLYESMYQ LIVETSTKLP KDVRRAILKA KQRENAGTRA AMSLATITEN IKMADENVSP 70 80 90 100 110 120 ICQDTGLPTF KIKVPVGINQ IQIKETIKKA IAQATKDGKL RPNSVDSLTG ENSGDNLGEG 130 140 150 160 170 180 LPVVKFEQWE KDYMDVRLIL KGGGCENKNI QYSLPCELEG LGRAGRDLDG IRKCILHAVY 190 200 210 220 230 240 QAQGQGCSAG FIGVGIGGDR SAGYDLAKEQ LFREVDDVNP NEELRQLEEY IMENANKLGI 250 260 270 280 290 300 GTMGFGGETT LLGCKVGAMH RIPASFFVSV AYNCWAFRRL GVHIDPNTGE IIKWLYQDGE 310 320 330 340 350 360 DVDFQENAAQ EEHLASTDSE RRVITLQAPI TEEQIRELKV GDVVRINGII YTGRDAIHKY 370 380 390 400 410 420 LMDHDAPVDL NGQIIYHCGP VMLKDENGNW EVKAAGPTTS IREEPYQGDI MKKFGIRAVM 430 440 450 460 470 480 GKGGMGQKTL QALKEHGGVY LNAIGGAAQY YADCIEAVEG VDLLEFGIPE AMWHLRVKDF 490 500 510 TAVVTMDSHG NSLHEDIEKS SLEKLSQFKE PVFS

References

[1]

"Molecular and enzymological evidence for two classes of fumarase in Bacillus stearothermophilus (var. non-diastaticus)." Reaney S.K., Bungard S.J., Guest J.R. J. Gen. Microbiol. 139:403-416(1993) [PubMed: 8473853] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DSM 2334 / Var. Non-diastaticus.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L05611 Genomic DNA. Translation: AAA72317.1.
PIR	A47692.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.2.1.2. 266715.
Family and domain databases
InterPro	IPR011167. Fe_dep_fumarate_hydratase. IPR020557. Fumarate_lyase_CS. IPR004646. TtdA_fumA_fumB. IPR004647. TtdB_fumA_fumB. [Graphical view]
Gene3D	G3DSA:3.20.130.10. TtdB_fumA_fumB. 1 hit.
Pfam	PF05681. Fumerase. 1 hit. PF05683. Fumerase_C. 1 hit. [Graphical view]
PIRSF	PIRSF001394. Fe_dep_fumar_hy. 1 hit.
TIGRFAMs	TIGR00722. ttdA_fumA_fumB. 1 hit. TIGR00723. ttdB_fumA_fumB. 1 hit.
PROSITE	PS00163. FUMARATE_LYASES. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FUMA_BACST

Accession

Primary (citable) accession number: Q04718

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	September 22, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)