Reviewed, UniProtKB/Swiss-Prot O94523 (ACO1_SCHPO)

Names and origin

Protein names

Recommended name:
    Probable acyl-CoA desaturase
    EC=1.14.19.1
Alternative name(s):
    Stearoyl-CoA desaturase
    Fatty acid desaturase
    Delta(9)-desaturase

Gene names

ORF Names:

SPCC1281.06c

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	479 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Utilizes O2 and electrons from the reduced cytochrome b5 domain to catalyze the insertion of a double bond into a spectrum of fatty acyl-CoA substrates By similarity.
Catalytic activity	Stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O.
Cofactor	Iron By similarity.
Subcellular location	Membrane; Multi-pass membrane protein. Ref.2
Domain	The histidine box domains may contain the active site and/or be involved in metal ion binding By similarity.
Sequence similarities	Belongs to the fatty acid desaturase family. Contains 1 cytochrome b5 heme-binding domain.

Ontologies

Keywords
Biological process	Electron transport Fatty acid biosynthesis Lipid synthesis Transport
Cellular component	Membrane
Domain	Transmembrane
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW fatty acid biosynthetic process Inferred by curator. Source: GeneDB_SPombe transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intrinsic to endoplasmic reticulum membrane Non-traceable author statement. Source: GeneDB_SPombe
Molecular function	heme binding Inferred from electronic annotation. Source: InterPro stearoyl-CoA 9-desaturase 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
	Chain	1 – 479	479	Probable acyl-CoA desaturase		PRO_0000185405
Regions
	Transmembrane	62 – 82	21	Potential
	Transmembrane	90 – 110	21	Potential
	Transmembrane	205 – 225	21	Potential
	Transmembrane	230 – 250	21	Potential
	Transmembrane	305 – 325	21	Potential
	Domain	357 – 433	77	Cytochrome b5 heme-binding
	Motif	110 – 115	6	Histidine box-1
	Motif	147 – 151	5	Histidine box-2
	Motif	284 – 288	5	Histidine box-3
Sites
	Metal binding	390	1	Iron (heme axial ligand) By similarity
	Metal binding	416	1	Iron (heme axial ligand) By similarity
Experimental info
	Sequence conflict	54 – 59	6	TMQNWW → GPCKTV Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O94523-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: ED5666E7B35EFCF2	FASTA	479	54,438
	10 20 30 40 50 60 MTAPSATAFS SATTQPTTEG NASMRKRTIP VVPSVPERKW DPKAPKHIQE QPWTMQNWWR 70 80 90 100 110 120 HLNWLHCMLI FGLPMIAIYG VFTTPLQTKT LIFAIIYYAY SGLGITAGYH RLWSHRAYKA 130 140 150 160 170 180 KKPLEYFLAA GGAAAFEGSI RWWSRDHRAH HRYTDTDKDP YNVKKGFWYA HVGWMIILQN 190 200 210 220 230 240 PRRIGRSDVS DLNSDPFVMF NHRHFLPIAS FMAFIFPSLF CGLLWGDYRG GYFYAGVCRL 250 260 270 280 290 300 VFVHHATFCV NSLAHLIGSQ PFDDTNSARN HFITALVTLG EGNHNYHHAF PNDYRNGLRW 310 320 330 340 350 360 YEYDPTKIFI YIASLFGLAY NLNTFPDNEI QKGIVQQKQK VLDRWRAKLN WGIPLEQLPV 370 380 390 400 410 420 MEFEDFLEQS KTRPLVLING VVHDMTGFEH PGGQGLLRSA FGKDATAAFN GGVYDHTNGA 430 440 450 460 470 HNLLSTYRVA VVRGGMEVEV WKSGAGAQLP MKDTQGQKIV RVGEQITRIQ PPIEAAAAN

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]

"Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library." Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., Hiraoka Y. Genes Cells 5:169-190(2000) [PubMed: 10759889] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 54-257, SUBCELLULAR LOCATION. Strain: ATCC 38364 / 968.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329672 Genomic DNA. Translation: CAA22827.1. AB027859 Genomic DNA. Translation: BAA87163.1.
PIR	T40925.
RefSeq	NP_588170.1.
3D structure databases
HSSP	HSSP built from PDB template 1AWP based on UniProtKB P04166.
ModBase	Search...
Genome annotation databases
GeneID	2538753.
KEGG	spo:SPCC1281.06c.
NMPDR	fig|4896.1.peg.508.
Organism-specific databases
GeneDB_Spombe	SPCC1281.06c.
Phylogenomic databases
OMA	O94523. HRIHHRY.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-000109-MON.
BRENDA	1.14.19.1. 653.
Gene expression databases
ArrayExpress	O94523.
Family and domain databases
InterPro	IPR001199. Cyt_B5. IPR018506. Cyt_B5_heme-BS. IPR005804. Fatty_acid_desaturase-1. IPR001522. Fatty_acid_desaturase-1_C. IPR015876. Fatty_acid_desaturase-1_core. IPR009160. OLE1_hae_ster_bd. [Graphical view]
Gene3D	G3DSA:3.10.120.10. Cyt_B5. 1 hit.
Pfam	PF00173. Cyt-b5. 1 hit. PF00487. FA_desaturase. 1 hit. [Graphical view]
PIRSF	PIRSF000345. OLE1. 1 hit.
PRINTS	PR00075. FACDDSATRASE.
ProDom	PD000612. Cyt_B5. 1 hit. PD002221. Desaturase. 1 hit. PD001081. FA_desat_sub. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00191. CYTOCHROME_B5_1. False negative. PS50255. CYTOCHROME_B5_2. 1 hit. PS00476. FATTY_ACID_DESATUR_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACO1_SCHPO

Accession

Primary (citable) accession number: O94523
Secondary accession number(s): Q9UU24

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	May 1, 1999
Last modified:	June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)