Reviewed, UniProtKB/Swiss-Prot Q9UTJ7 (DHSA_SCHPO)

Names and origin

Protein names

Recommended name:
    Probable succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
    EC=1.3.5.1
Alternative name(s):
    Flavoprotein subunit of complex II
      Short name=FP

Gene names

Name:	sdh1
ORF Names:	SPAC1556.02c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	641 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q) By similarity.
Catalytic activity	Succinate + ubiquinone = fumarate + ubiquinol.
Cofactor	FAD By similarity.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle.
Subunit structure	Component of complex II composed of four subunits: a flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b composed of a large and a small subunit By similarity.
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Matrix side By similarity.
Sequence similarities	Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

Ontologies

Keywords
Biological process	Electron transport Transport Tricarboxylic acid cycle
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW succinate metabolic process Inferred by curator. Source: GeneDB_SPombe transport Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro succinate dehydrogenase (ubiquinone) 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 – ?		Mitochondrion Potential
	Chain	? – 641		Probable succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial		PRO_0000010341
Regions
	Nucleotide binding	84 – 99	16	FAD By similarity
Sites
	Active site	333	1	Proton acceptor By similarity
	Binding site	289	1	Substrate By similarity
	Binding site	301	1	Substrate By similarity
	Binding site	400	1	Substrate By similarity
	Binding site	445	1	Substrate By similarity
Amino acid modifications
	Modified residue	92	1	Tele-8alpha-FAD histidine By similarity
Experimental info
	Sequence conflict	214	1	A → G in BAA13924. Ref.2
	Sequence conflict	218	1	I → L in BAA13924. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9UTJ7-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 5E5FCD857C372199	FASTA	641	70,466
	10 20 30 40 50 60 MLRFRKVAPS LKNGGNLKLF STSSTLKKIA SSQPLRAKQV STSESVKYPV IDHTYDAIVV 70 80 90 100 110 120 GAGGAGLRAT FGLAEAGFNT ACITKLFPTR SHTVAAQGGI NAALGNMTKD DWRWHFYDTV 130 140 150 160 170 180 KGSDWLGDQD AIHYMTKEAP KAVLELEHFG VPFSRTKEGK IYQRAFGGQS LEYGKGGQAY 190 200 210 220 230 240 RCAAVADRTG HSILHTLYGQ SLKHNTNFFI EYFAMDLIME GGECRGVIAM NLEDGSIHRF 250 260 270 280 290 300 RAHKTILATG GYGRAYFSCT SAHTCTGDGN AMVSRAGLPL QDLEFVQFHP TGIYGAGCLI 310 320 330 340 350 360 TEGCRGEGGY LLNSKGERFM ERYAPTAKDL ASRDVVSRAM TVEIREGRGV GPEKDHCYLQ 370 380 390 400 410 420 LSHLPAEILK ERLPGISETA AIFAGVDVTK EPIPVLPTVH YNMGGIPTRF TGEVLTIDEN 430 440 450 460 470 480 GKDKIVPGLY AAGEAACVSV HGGNRLGANS LLDIVVFGRA CALHIKDTLE PNTPHKPLAA 490 500 510 520 530 540 DAGLDSLKFL DQIRTSQGPK HTSEIRLDMQ KTMQRDVSVF RMEETLQEGV KNIARVDGTY 550 560 570 580 590 600 KDIGIRDRGL IWNTDLVEAL ELRNLLTCAV QTANAALNRK ESRGAHARED YPERDDKNWI 610 620 630 640 KHTLTWQHKT GDPVTLKYRA VTRTTMDENE VKPVPPFKRV Y

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

[2]

"Identification of open reading frames in Schizosaccharomyces pombe cDNAs." Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H. DNA Res. 4:363-369(1997) [PubMed: 9501991] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-641. Strain: PR745.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAB61213.1. D89263 mRNA. Translation: BAA13924.1.
PIR	T50081.
RefSeq	NP_594319.1.
3D structure databases
HSSP	HSSP built from PDB template 1NEK based on UniProtKB P10444.
ModBase	Search...
Genome annotation databases
GeneID	2541690.
KEGG	spo:SPAC1556.02c.
NMPDR	fig|4896.1.peg.4289.
Organism-specific databases
GeneDB_Spombe	SPAC1556.02c.
Phylogenomic databases
OMA	Q9UTJ7. TLEFDNL.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-002428-MON.
BRENDA	1.3.5.1. 653.
Gene expression databases
ArrayExpress	Q9UTJ7.
Family and domain databases
InterPro	IPR003953. FAD_bind2_N. IPR003952. FRD_SDH_FAD_BS. IPR004112. Fum_Rdtase/Succ_DH_flav_C. IPR011281. Succ_DH_flav_su_fwd. IPR014006. Succ_Dhase_frdA_Gneg. [Graphical view]
Pfam	PF00890. FAD_binding_2. 1 hit. PF02910. Succ_DH_flav_C. 1 hit. [Graphical view]
TIGRFAMs	TIGR01816. sdhA_forward. 1 hit. TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITE	PS00504. FRD_SDH_FAD_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHSA_SCHPO

Accession

Primary (citable) accession number: Q9UTJ7
Secondary accession number(s): P78912

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 23, 2003
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)