P55250 (FUMH_RHIOR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fumarate hydratase, mitochondrial
Short name=Fumarase
EC=4.2.1.2

Gene names

Name:

FUMR

Organism

Rhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar)

Taxonomic identifier

64495 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Fungi incertae sedis › Early diverging fungal lineages › Mucoromycotina › Mucorales › Mucoraceae › Rhizopus

Protein attributes

Sequence length	494 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	(S)-malate = fumarate + H2O.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1.
Subcellular location	Mitochondrion. Cytoplasm.
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.
Sequence similarities	Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Cytoplasm Mitochondrion
Domain	Transit peptide
Molecular function	Lyase
Gene Ontology (GO)
Biological_process	fumarate metabolic process Inferred from electronic annotation. Source: InterPro tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell 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
	Transit peptide	1 – 15	15	Mitochondrion Potential
	Chain	16 – 494	479	Fumarate hydratase, mitochondrial		PRO_0000010331
Regions
	Region	159 – 162	4	B site By similarity
	Region	169 – 171	3	Substrate binding By similarity
Sites
	Binding site	130	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P55250 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 8FDB9D323A9146EE	FASTA	494	53,157
	10 20 30 40 50 60 MLRASATRFL SQAKNMNNSP RLFSSASAAL QKFRAERDTF GDLQVPADRY WGAQTQRSLQ 70 80 90 100 110 120 NFDIGGPTER MPEPLIRAFG VLKKAAATVN MTYGLDPKVG EAIQKAADEV IDGSLIDHFP 130 140 150 160 170 180 LVVWQTGSGT QTKMNVNEVI SNRAIELLGG ELGSKAPVHP NDHVNMSQSS NDTFPTAMHV 190 200 210 220 230 240 AAVVEIHGRL IPALTTLRDA LQAKSAEFEH IIKIGRTHLQ DATPLTLGQE FSGYTQQLTY 250 260 270 280 290 300 GIARVQGTLE RLYNLAQGGT AVGTGLNTRK GFDAKVAEAI ASITGLPFKT APNKFEALAA 310 320 330 340 350 360 HDALVEAHGA LNTVACSLMK IANDIRYLGS GPRCGLGELS LPENEPGSSI MPGKVNPTQC 370 380 390 400 410 420 EAMTMVCAQV MGNNTAISVA GSNGQFELNV FKPVMIKNLI QSIRLISDAS ISFTKNCVVG 430 440 450 460 470 480 IEANEKKISS IMNESLMLVT ALNPHIGYDK AAKCAKKAHK EGTTLKEAAL SLGYLTSEEF 490 DQWVRPEDMI SAKD

References

[1]

"The fumR gene encoding fumarase in the filamentous fungus Rhizopus oryzae: cloning, structure and expression." Friedberg D., Peleg Y., Monsonego A., Maissi S., Battat E., Rokem J.S., Goldberg I. Gene 163:139-144(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 10260 / CBS 329.47 / DSM 905 / NRRL 1526.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X78576 Genomic DNA. Translation: CAA55314.1.
3D structure databases
ProteinModelPortal	P55250.
SMR	P55250. Positions 33-493.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00223; UER01007.
Family and domain databases
Gene3D	1.10.275.10. 1 hit.
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

FUMH_RHIOR

Accession

Primary (citable) accession number: P55250

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program