Reviewed, UniProtKB/Swiss-Prot A5PL98 (DHSB_DANRE)

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:

sdhb

Organism

Danio rerio (Zebrafish) (Brachydanio rerio)

Taxonomic identifier

7955 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Ostariophysi › Cypriniformes › Cyprinidae › Danio

Protein attributes

Sequence length	280 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	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: 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 sideBy 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
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: InterPro
Cellular component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-KW
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 – 25	25	Mitochondrion By similarity
	Chain	26 – 280	255	Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial		PRO_0000343801
Regions
	Domain	39 – 129	91	2Fe-2S ferredoxin-type
	Domain	175 – 205	31	4Fe-4S ferredoxin-type
Sites
	Metal binding	92	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	97	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	100	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	112	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	185	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	188	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	191	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	195	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	242	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	248	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	252	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Binding site	200	1	Ubiquinone; shared with dhsd By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5PL98-1 [UniParc]. Last modified July 10, 2007. Version 1. Checksum: A16A68A72849B844	FASTA	280	31,740
	10 20 30 40 50 60 MAAVCFSLSR CCSAVHRPAV TAVRFAQTAA APAAQPRIKK FQIYRWDPDT VGDKPRMQTY 70 80 90 100 110 120 EIDLNTCGPM VLDALIKIKN EMDSTLTFRR SCREGICGSC AMNINGGNTL ACLNKIDTNT 130 140 150 160 170 180 SKVTKIYPLP HMYVVKDLVP DMSNFYAQYK SIEPYLKKKD ESQQGKQQYL QSVEDRQKLD 190 200 210 220 230 240 GLYECILCAC CSTSCPSYWW NADKYLGPAV LMQAYRWMID SRDDFTEDRL SKLQDPFSLY 250 260 270 280 RCHTIMNCTR TCPKGLNPGK AIAEIKKMMV TYKQKDAVAA

References

[1]	NIH - Zebrafish Gene Collection (ZGC) project Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Eye.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BC142799 mRNA. Translation: AAI42800.1.
RefSeq	NP_001092210.1.
UniGene	Dr.75182
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	562149.
KEGG	dre:562149.
Organism-specific databases
ZFIN	ZDB-GENE-030131-8005. sdhb.
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]
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_DANRE

Accession

Primary (citable) accession number: A5PL98

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 22, 2008
Last sequence update:	July 10, 2007
Last modified:	November 25, 2008
This is version 14 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Zebrafish annotation project