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P0A4Y0 (CYA1_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Adenylate cyclase
EC=4.6.1.1
Alternative name(s):
ATP pyrophosphate-lyase
Adenylyl cyclase
Gene names
Name:cya
Ordered Locus Names:Rv1625c, MT1661
ORF Names:MTCY01B2.17c
OrganismMycobacterium tuberculosis
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP = 3',5'-cyclic AMP + diphosphate.

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Subunit structure

Homodimer.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.

Contains 1 guanylate cyclase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 443443Adenylate cyclase
PRO_0000195727

Regions

Transmembrane47 – 6923Helical; Potential
Transmembrane74 – 9320Helical; Potential
Transmembrane98 – 12023Helical; Potential
Transmembrane124 – 14320Helical; Potential
Transmembrane148 – 16720Helical; Potential
Transmembrane180 – 20223Helical; Potential
Topological domain203 – 443241Cytoplasmic Potential
Domain251 – 378128Guanylate cyclase

Sites

Metal binding2561Magnesium By similarity
Metal binding3001Magnesium By similarity

Experimental info

Mutagenesis431R → A or G: Loss of activity.
Mutagenesis431R → K: Almost no loss of activity.
Mutagenesis441R → A or G: Loss of activity.
Mutagenesis441R → K: Almost no loss of activity.

Secondary structure

1 ........................................ 443
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A4Y0 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 64B13168B4B792E2

FASTA44347,370
        10         20         30         40         50         60 
MAARKCGAPP IAADGSTRRP DCVTAVRTQA RAPTQHYAES VARRQRVLTI TAWLAVVVTG 

        70         80         90        100        110        120 
SFALMQLATG AGGWYIALIN VFTAVTFAIV PLLHRFGGLV APLTFIGTAY VAIFAIGWDV 

       130        140        150        160        170        180 
GTDAGAQFFF LVAAALVVLL VGIEHTALAV GLAAVAAGLV IALEFLVPPD TGLQPPWAMS 

       190        200        210        220        230        240 
VSFVLTTVSA CGVAVATVWF ALRDTARAEA VMEAEHDRSE ALLANMLPAS IAERLKEPER 

       250        260        270        280        290        300 
NIIADKYDEA SVLFADIVGF TERASSTAPA DLVRFLDRLY SAFDELVDQH GLEKIKVSGD 

       310        320        330        340        350        360 
SYMVVSGVPR PRPDHTQALA DFALDMTNVA AQLKDPRGNP VPLRVGLATG PVVAGVVGSR 

       370        380        390        400        410        420 
RFFYDVWGDA VNVASRMEST DSVGQIQVPD EVYERLKDDF VLRERGHINV KGKGVMRTWY 

       430        440 
LIGRKVAADP GEVRGAEPRT AGV

« Hide

References

« Hide 'large scale' references
[1]"Eukaryotic-like adenylyl cyclases in Mycobacterium tuberculosis H37Rv: cloning and characterization."
Reddy S.K., Kamireddi M., Dhanireddy K., Young L., Davis A., Reddy P.T.
J. Biol. Chem. 276:35141-35149(2001) [PubMed: 11431477] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, MUTAGENESIS.
Strain: ATCC 25618 / H37Rv.
[2]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed: 9634230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[3]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[4]"Adenylyl cyclase Rv1625c of Mycobacterium tuberculosis: a progenitor of mammalian adenylyl cyclases."
Guo Y.L., Seebacher T., Kurz U., Linder J.U., Schultz J.E.
EMBO J. 20:3667-3675(2001) [PubMed: 11447108] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF017731 Genomic DNA. Translation: AAB70274.1.
BX842577 Genomic DNA. Translation: CAB08902.2.
AE000516 Genomic DNA. Translation: AAK45931.1.
PIRG70558.
RefSeqNP_216141.2. NC_000962.2.
NP_336117.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YK9X-ray2.70A240-443[»]
ProteinModelPortalP0A4Y0.
SMRP0A4Y0. Positions 245-428.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000002334; EBMYCP00000002334; EBMYCG00000002332.
EBMYCT00000070696; EBMYCP00000068755; EBMYCG00000070691.
GeneID888538.
924208.
GenomeReviewsGene locus MT1661 in contig AE000516_GR.
Gene locus Rv1625c in contig AL123456_GR.
KEGGmtc:MT1661.
mtu:Rv1625c.
PATRIC18125414. VBIMycTub22151_1822.
TIGRMT1661.

Organism-specific databases

TubercuListRv1625c.

Phylogenomic databases

GeneTreeEBGT00050000015402.
HOGENOMHBG564705.
OMAFVLQERG.
ProtClustDBCLSK799821.

Enzyme and pathway databases

BRENDA4.6.1.1. 3445.

Family and domain databases

InterProIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
[Graphical view]
Gene3DG3DSA:3.30.70.1230. A/G_cyclase. 1 hit.
KOK01768.
PfamPF00211. Guanylate_cyc. 1 hit.
[Graphical view]
SMARTSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMSSF55073. A/G_cyclase. 1 hit.
PROSITEPS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYA1_MYCTU
AccessionPrimary (citable) accession number: P0A4Y0
Secondary accession number(s): O06142, O30820
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents