Reviewed, UniProtKB/Swiss-Prot P32420 (DHSB_USTMA)

Names and origin

Protein names

Recommended name:
    Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
    EC=1.3.5.1
Alternative name(s):
    Iron-sulfur subunit of complex II
      Short name=Ip

Gene names

Name:	SDH2
Synonyms:	CBXR

Organism

Ustilago maydis (Smut fungus) [Complete proteome]

Taxonomic identifier

5270 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Ustilaginomycotina › Ustilaginomycetes › Ustilaginales › Ustilaginaceae › Ustilago

Protein attributes

Sequence length	295 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Iron-sulfur protein (IP) 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	Binds 1 2Fe-2S cluster By similarity. Binds 1 3Fe-4S cluster By similarity. Binds 1 4Fe-4S cluster 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 succinate dehydrogenase/fumarate reductase iron-sulfur protein family. Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 4Fe-4S ferredoxin-type domain.

Ontologies

Keywords
Biological process	Electron transport Transport Tricarboxylic acid cycle
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	2Fe-2S 3Fe-4S 4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW 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	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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	? – 295		Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial		PRO_0000010352
Regions
	Domain	67 – 144	78	2Fe-2S ferredoxin-type
	Domain	185 – 215	31	4Fe-4S ferredoxin-type
Sites
	Metal binding	106	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	111	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	114	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	126	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	195	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	198	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	201	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	205	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	252	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	258	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	262	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Binding site	210	1	Ubiquinone; shared with DHSD By similarity
Natural variations
	Natural variant	253	1	H → L in carboxin-resistant mutant.

Sequences

	Sequence		Length	Mass (Da)
	P32420-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: F374A20BA8F8E7E5	FASTA	295	33,282
	10 20 30 40 50 60 MSLFNVSNGL RTALRPSVAS SSRVAAFSTT AAARLATPTS DNVGSSGKPQ HLKQFKIYRW 70 80 90 100 110 120 NPDKPSEKPR LQSYTLDLNQ TGPMVLDALI KIKNEIDPTL TFRRSCREGI CGSCAMNIDG 130 140 150 160 170 180 VNTLACLCRI DKQNDTKIYP LPHMYIVKDL VPDLTQFYKQ YRSIEPFLKS NNTPSEGEHL 190 200 210 220 230 240 QSPEERRRLD GLYECILCAC CSTSCPSYWW NQDEYLGPAV LMQAYRWMAD SRDDFGEERR 250 260 270 280 290 QKLENTFSLY RCHTIMNCSR TCPKNLNPGK AIAQIKKDMA VGAPKASERP IMASS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation, characterization and sequence of a gene conferring resistance to the systemic fungicide carboxin from the maize smut pathogen, Ustilago maydis." Keon J.P.R., White G.A., Hargreaves J.A. Curr. Genet. 19:475-481(1991) [PubMed: 1879000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 38509 / 92.
[2]	"A single amino-acid change in the iron-sulphur protein subunit of succinate dehydrogenase confers resistance to carboxin in Ustilago maydis." Broomfield P.L.E., Hargreaves J.A. Curr. Genet. 22:117-121(1992) [PubMed: 1423716] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis." Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J. , Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L., Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W. Nature 444:97-101(2006) [PubMed: 17080091] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 521.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X62762 Genomic DNA. Translation: CAA44612.1. Z11738 Genomic DNA. Translation: CAA77798.1. AACP01000027 Genomic DNA. Translation: EAK81918.1.
PIR	S26978.
RefSeq	XP_756991.1.
3D structure databases
HSSP	HSSP built from PDB template 1NEK based on UniProtKB P07014.
SMR	P32420. Positions 52-280.
ModBase	Search...
Genome annotation databases
GeneID	3628909.
KEGG	uma:UM00844.1.
Phylogenomic databases
OMA	P32420. ASIEPWL.
Enzyme and pathway databases
BRENDA	1.3.5.1. 2320.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR012675. b-grasp_ferredoxin-like. IPR001041. Ferredoxin. IPR012285. Fum_reductase_C. IPR004489. Succ_DH/fum_Rdtase_Fe-S. [Graphical view]
Gene3D	G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit. G3DSA:1.10.1060.10. Fum_reductase_C. 1 hit.
Pfam	PF00111. Fer2. 1 hit. [Graphical view]
TIGRFAMs	TIGR00384. dhsB. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS00198. 4FE4S_FER_1. 1 hit. PS51379. 4FE4S_FER_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHSB_USTMA

Accession

Primary (citable) accession number: P32420
Secondary accession number(s): Q12722, Q4PGB9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	June 16, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)