Reviewed, UniProtKB/Swiss-Prot P0A4Y0 (CYA1_MYCTU)

Names and origin

Protein names

Recommended 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

Organism

Mycobacterium tuberculosis [Complete proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	443 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	cAMP biosynthesis
Cellular component	Cell membrane Membrane
Domain	Transmembrane
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Lyase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cAMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW intracellular signaling cascade Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate cyclase activity Inferred from electronic annotation. Source: EC magnesium 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 – 443

443

Adenylate cyclase

PRO_0000195727

Regions

Transmembrane

47 – 69

23

Potential

Transmembrane

74 – 93

20

Potential

Transmembrane

98 – 120

23

Potential

Transmembrane

124 – 143

20

Potential

Transmembrane

148 – 167

20

Potential

Transmembrane

180 – 202

23

Potential

Topological domain

203 – 443

241

Cytoplasmic Potential

Domain

251 – 378

128

Guanylate cyclase

Sites

Metal binding

256

1

Magnesium By similarity

Metal binding

300

1

Magnesium By similarity

Experimental info

Mutagenesis

43

1

R → A or G: Loss of activity.

Mutagenesis

43

1

R → K: Almost no loss of activity.

Mutagenesis

44

1

R → A or G: Loss of activity.

Mutagenesis

44

1

R → K: Almost no loss of activity.

Secondary structure

1

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443

Helix Strand Turn

Details...

Beta strand

250 – 258

9

Beta strand

269 – 271

3

Turn

272 – 274

3

Helix

275 – 280

6

Turn

281 – 284

4

Helix

285 – 287

3

Beta strand

298 – 300

3

Beta strand

302 – 306

5

Helix

315 – 320

6

Helix

322 – 329

8

Beta strand

335 – 337

3

Beta strand

343 – 350

8

Beta strand

352 – 354

3

Beta strand

359 – 361

3

Beta strand

366 – 368

3

Helix

369 – 373

5

Helix

376 – 379

4

Beta strand

386 – 388

3

Helix

390 – 394

5

Beta strand

400 – 404

5

Beta strand

411 – 415

5

Beta strand

420 – 425

6

Sequences

	Sequence		Length	Mass (Da)
	P0A4Y0-1 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 64B13168B4B792E2	FASTA	443	47,370
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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

EMBLGenBankDDBJ

AF017731 Genomic DNA. Translation: AAB70274.1.
BX842577 Genomic DNA. Translation: CAB08902.2.
AE000516 Genomic DNA. Translation: AAK45931.1.

PIR

G70558.

RefSeq

NP_216141.2.
NP_336117.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YK9	X-ray	2.70	A	240-443	[»]

ModBase

Search...

Genome annotation databases

GeneID

888538.
924208.

GenomeReviews

Gene locus MT1661 in contig AE000516_GR.
Gene locus Rv1625c in contig AL123456_GR.

KEGG

mtc:MT1661.
mtu:Rv1625c.

TIGR

MT1661.

Organism-specific databases

TubercuList

Rv1625c.

Phylogenomic databases

HOGENOM

P0A4Y0.

OMA

ISHETYS.

Enzyme and pathway databases

BRENDA

4.6.1.1. 809.

Family and domain databases

InterPro

IPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
[Graphical view]

Gene3D

G3DSA:3.30.70.1230. A/G_cyclase. 1 hit.

Pfam

PF00211. Guanylate_cyc. 1 hit.
[Graphical view]

SMART

SM00044. CYCc. 1 hit.
[Graphical view]

PROSITE

PS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CYA1_MYCTU

Accession

Primary (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:	November 3, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)