P50998 (AMPD_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
AMP deaminase
EC=3.5.4.6

Alternative name(s):
Myoadenylate deaminase

Gene names

Name:	ada1
ORF Names:	SPBC106.04

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	846 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	AMP deaminase plays a critical role in energy metabolism.
Catalytic activity	AMP + H2O = IMP + NH3.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Pathway	Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1.
Subunit structure	Homotetramer By similarity.
Sequence similarities	Belongs to the adenosine and AMP deaminases family.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	purine base metabolic process Inferred from electronic annotation. Source: InterPro purine ribonucleoside monophosphate biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_Spombe
Molecular function	AMP deaminase activity Inferred from direct assay. Source: GeneDB_Spombe metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 846	846	AMP deaminase		PRO_0000194413
Regions
	Region	405 – 410	6	Substrate binding By similarity
	Region	680 – 683	4	Substrate binding By similarity
Sites
	Active site	624	1	Proton acceptor By similarity
	Metal binding	334	1	Zinc; catalytic By similarity
	Metal binding	336	1	Zinc; catalytic By similarity
	Metal binding	602	1	Zinc; catalytic By similarity
	Metal binding	679	1	Zinc; catalytic By similarity
	Binding site	336	1	Substrate By similarity
	Binding site	605	1	Substrate By similarity
Amino acid modifications
	Modified residue	94	1	Phosphoserine Ref.3
	Modified residue	99	1	Phosphoserine Ref.3
	Modified residue	773	1	Phosphoserine Ref.3
	Modified residue	791	1	Phosphoserine Ref.3
	Modified residue	795	1	Phosphoserine Ref.3
	Modified residue	797	1	Phosphoserine Ref.3
Experimental info
	Sequence conflict	483 – 520	38	NVRWL…PLFEV → TFVGLFKYLVCMMCIRSPVL LRLLKRSSEMSLNHCSKF in CAA62797. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P50998 [UniParc]. Last modified January 11, 2001. Version 2. Checksum: 701CCC540A8E9C25	FASTA	846	97,455
	10 20 30 40 50 60 MSVRPLSLCG LLPAEMNMEQ EDDQVPAVAA ETVPLKRYVT NPGANRDEEV AAAPSSQDTP 70 80 90 100 110 120 YFDYAYERSL RHQDAKFLAM NGTQNGRDGL PSKSPRRPSV SASTVRNSDD VNHSKAGPGS 130 140 150 160 170 180 GKLLNDTLQS KISSIHMPHV QQGDNAVVSS VGGPETDPGN METTDPLFSD ELAEIYLSIH 190 200 210 220 230 240 KCMDMRHKYI RVSLQGELDN PIDDDSWIIY PDCKEGEDDT GLFNFADCKI PGIENEMEYH 250 260 270 280 290 300 MDHQGIFQVY ENDSAYIAGT PSFHIPTIRD YYIDLEFLLS ASSDGPSKSF SFRRLQYLEG 310 320 330 340 350 360 RWNMYMLLNE YQELADTKKV PHRDFYNVRK VDTHVHHSAL ANQKHLLRFI KAKLRKCPNE 370 380 390 400 410 420 KVIWRDGKFL TLQEVFDSLK LTSYDLSIDT LDMHAHTDTF HRFDKFNLKY NPIGESRLRT 430 440 450 460 470 480 IFLKTDNDIN GRYLAELTKE VFTDLRTQKY QMAEYRISIY GRNREEWDKL AAWIIDNELF 490 500 510 520 530 540 SPNVRWLIQV PRLYDVYKKS GIVETFEEVV RNVFEPLFEV TKDPRTHPKL HVFLQRVIGF 550 560 570 580 590 600 DSVDDESKPE RRTFRKFPYP KHWDINLNPP YSYWLYYMYA NMTSLNSWRK IRGFNTFVLR 610 620 630 640 650 660 PHCGEAGDTD HLASAFLLSH GINHGILLRK VPFLQYLWYL DQIPIAMSPL SNNALFLAYD 670 680 690 700 710 720 KNPFLTYFKR GLNVSLSTDD PLQFAFTREP LIEEYAVAAQ IYKLSAVDMC ELARNSVLQS 730 740 750 760 770 780 GFERQLKERW LGVDFQDIDR TNVPIIRLAY RALTLTQEIA LVNKHVQPSK HPSNHDLEEL 790 800 810 820 830 840 IHKYDAMTGT SDPLSASPRT NDATISSRLS LHDGHDHGAF FPGLSVISER RRRKDSMASS SQDLKD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Rochet M., Levesque H., Gaillardin C. Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 972 / ATCC 24843.
[2]	"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: 972 / ATCC 24843.
[3]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94; SER-99; SER-773; SER-791; SER-795 AND SER-797, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X91498 Genomic DNA. Translation: CAA62797.1. Sequence problems. CU329671 Genomic DNA. Translation: CAB53720.1.
PIR	T39261.
RefSeq	NP_595153.1. NM_001021062.1.
3D structure databases
ProteinModelPortal	P50998.
ModBase	Search...
Protein-protein interaction databases
STRING	P50998.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2540105.
GenomeReviews	Gene locus ada1 in contig CU329671_GR.
KEGG	spo:SPBC106.04.
NMPDR	fig|4896.1.peg.1019.
Organism-specific databases
GeneDB_Spombe	SPBC106.04.
Phylogenomic databases
eggNOG	fuNOG04148.
GeneTree	EFGT00050000003751.
HOGENOM	HBG713563.
OMA	YENDSAY.
OrthoDB	EOG44XNR5.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-003250-MONOMER.
Gene expression databases
ArrayExpress	P50998.
Family and domain databases
InterPro	IPR006650. A/AMP_deam_AS. IPR001365. A/AMP_deaminase_dom. IPR006329. AMP_deaminase. [Graphical view]
KO	K01490.
PANTHER	PTHR11359. PTHR11359. 1 hit.
Pfam	PF00962. A_deaminase. 1 hit. [Graphical view]
PIRSF	PIRSF001251. AMP_deaminase_met. 1 hit.
TIGRFAMs	TIGR01429. AMP_deaminase. 1 hit.
PROSITE	PS00485. A_DEAMINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPD_SCHPO

Accession

Primary (citable) accession number: P50998
Secondary accession number(s): Q9URV7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 11, 2001
Last modified:	December 14, 2011
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program