[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Embryo, and Testis; NIH - Xenopus Gene Collection (XGC) project; Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.

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).
COFACTOR: Binds 1 3Fe-4S cluster (By similarity).
COFACTOR: Binds 1 4Fe-4S cluster (By similarity).
PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle .
SUBUNIT: Component of complex II composed of four subunits: the flavoprotein (FP) sdha, iron-sulfur protein (IP) sdhb, and a cytochrome b composed of sdhc and sdhd (By similarity).
SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side (By similarity).
SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
SIMILARITY: Contains 1 4Fe-4S ferredoxin-type domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BC043859; AAH43859.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC106300; AAI06301.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001080247.1; -.

UniGene

Xl.12560

3D structure databases

SMR

Q3B8J8; 40-277.

ModBase

Q3B8J8.

Organism-specific databases

Xenbase

XB-FEAT-970192; sdhb.

Ontologies

GO:0005743;	Cellular component: mitochondrial inner membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0051537;	Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051538;	Molecular function: 3 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008177;	Molecular function: succinate dehydrogenase (ubiquinone) activity (inferred from electronic annotation from EC).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR006058; 2Fe2S_fd_BS.
IPR001450; 4Fe4S_Fe_S_bd.
IPR012675; b-grasp_ferredoxin-like.
IPR001041; Ferredoxin.
IPR012285; Fum_reductase_C.
IPR004489; Succ_DHase/fum_Rdtase_Fe-S.
Graphical view of domain structure.

Gene3D

G3DSA:3.10.20.30; Ferredoxin_fold; 1.
G3DSA:1.10.1060.10; Fum_reductase_C; 1.

Pfam

PF00111; Fer2; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00384; dhsB; 1.

PROSITE

PS00197; 2FE2S_FER_1; 1.
PS51085; 2FE2S_FER_2; 1.
PS00198; 4FE4S_FER_1; 1.
PS51379; 4FE4S_FER_2; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

379939; -.

KEGG

xla:379939; -.

Phylogenomic databases

HOVERGEN

Q3B8J8; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

2Fe-2S; 3Fe-4S; 4Fe-4S; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Transit peptide; Transport; Tricarboxylic acid cycle.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 26`	`26`	`Mitochondrion (By similarity).`
`CHAIN`	`27 282`	`256`	`Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial.`	`PRO_0000343802`
`DOMAIN`	`42 135`	`94`	`2Fe-2S ferredoxin-type.`
`DOMAIN`	`178 208`	`31`	`4Fe-4S ferredoxin-type.`
`METAL`	`95 95`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`100 100`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`103 103`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`115 115`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`188 188`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`191 191`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`194 194`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`198 198`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`245 245`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`251 251`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`255 255`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`BINDING`	`203 203`		`Ubiquinone; shared with dhsd (By similarity).`
`CONFLICT`	`164 164`		`K -> E (in Ref. 1; AAH43859).`
`CONFLICT`	`279 279`		`A -> V (in Ref. 1; AAH43859).`

Sequence information

Length: 282 AA [This is the length of the unprocessed precursor]

Molecular weight: 31777 Da [This is the MW of the unprocessed precursor]

CRC64: FCEE9AA00E84E689 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAVVFSLRR SGPVLRLSGA LQVSRGAQTA AAPASQAAAR IKKFAIYRWD PDKPGDKPRM 

        70         80         90        100        110        120 
QTYEVDLNTC GPMVLDALIK IKNEVDPTLT FRRSCREGIC GSCAMNINGG NTLACTVRID 

       130        140        150        160        170        180 
TNLSKVSKIY PLPHMYVVKD LVPDLSNFYA QYKSIEPYLK KKDKSQQGKE QYLQSIEDRD 

       190        200        210        220        230        240 
KLDGLYECIL CACCSTSCPS YWWNADKYLG PAVLMQAYRW MIDSRDDFTE ERLSKLQDPF 

       250        260        270        280 
SLYRCHTIMN CTRTCPKGLN PGKAIAEIKK MMAMYKERAV SA

Q3B8J8 in FASTA format

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View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools