Adenylate cyclase - Spirulina platensis

Preferred order of sections

Names and origin

Protein names

Submitted name:
Adenylate cyclase EMBL BAA22997.1
EC=4.6.1.1 EMBL BAA22997.1

Gene names

Name:

cyaC EMBL BAA22997.1

Organism

Spirulina platensis EMBL BAA22997.1

Taxonomic identifier

118562 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Oscillatoriales › Arthrospira

Protein attributes

Sequence length	1202 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Contains 1 histidine kinase domain. SAAS SAAS009082

Ontologies

Keywords
Ligand	Calcium PDB 1WC0 PDB 1WC5 PDB 2BW7 Magnesium PDB 1WC1 PDB 1WC6 PDB 1WC5 PDB 2BW7 Metal-binding PDB 1WC1 PDB 1WC6 PDB 1WC0 PDB 1WC5 PDB 2BW7
Molecular function	Lyase EMBL BAA22997.1
PTM	Phosphoprotein SAAS SAAS005467
Technical term	3D-structure PDB 1WC1 PDB 1WC6 PDB 1WC0 PDB 1WC5 PDB 2BW7 PDB 1WC3 PDB 1WC4
Gene Ontology (GO)
Biological process	peptidyl-histidine phosphorylation Inferred from electronic annotation. Source: InterPro protein-chromophore linkage Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro
Cellular component	membrane Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro G-protein coupled photoreceptor activity Inferred from electronic annotation. Source: InterPro adenylate cyclase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW two-component response regulator activity Inferred from electronic annotation. Source: InterPro two-component sensor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

1017

1

Calcium PDB 1WC0 PDB 1WC5 PDB 2BW7

Metal binding

1017

1

Magnesium 1 PDB 1WC1 PDB 1WC6

Metal binding

1017

1

Magnesium 2 PDB 1WC6

Metal binding

1018

1

Calcium; via carbonyl oxygen PDB 1WC0 PDB 1WC5 PDB 2BW7

Metal binding

1018

1

Magnesium 1; via carbonyl oxygen PDB 1WC1 PDB 1WC6

Metal binding

1059

1

Magnesium 2; via carbonyl oxygen PDB 1WC6

Metal binding

1061

1

Calcium PDB 1WC0 PDB 1WC5 PDB 2BW7

Metal binding

1061

1

Magnesium 1 PDB 1WC1 PDB 1WC6

Metal binding

1061

1

Magnesium 2 PDB 1WC6

Sequences

Sequence

Length

Mass (Da)

Tools

O32393 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 275BEC0C120AFD4D
Show »

FASTA

1,202

133,924

        10         20         30         40         50         60 
MSSPNRKLKP TILVVDDEPD NLDLLYRTFH REFKVLKAES GPAALKILEE VGEVAVIISD 

        70         80         90        100        110        120 
QRMPYMSGTE FLSLTATQYP DSIRIILTGY TDVEDLVEAI NSGKVFKYVT KPWKSDELKA 

       130        140        150        160        170        180 
IVQQGLETHN VLKSRTEELR LAQKQESLLY EVTSTIRACP NSQEMLQRIV ETVGKMFEVS 

       190        200        210        220        230        240 
YCLLRSFGVG SDLIGLGAGV SPTKQDITAT QGKEWFAYLA EGQNHQNSTT DNISVINNND 

       250        260        270        280        290        300 
LELRSLVWET TEVMILSEGL GNDISDHDGP EWQQRRDVYQ RADIRSSLIV PLYYRQELLA 

       310        320        330        340        350        360 
VLALHHTGSP RNWHEHEVQL AAGVADQAAL ALSQVRAYEQ VRELARREAL VNTITNAIRS 

       370        380        390        400        410        420 
SLDPQKIFAA ITEQLGEALE VDGCALSLWS PGDEYMQCVG LYNAAIKETV VETRPAALSE 

       430        440        450        460        470        480 
PDTSTTTNLP LLGVETNQSI ESDQSDDLPQ SAAPISGNPV LQELIRTRAP VAIADIEQRP 

       490        500        510        520        530        540 
DSMVMLPLRS PSKALLVVPL LLDGDIIGSI SLRQNHQVRH WQPSEIDMVL LVAAQAALAV 

       550        560        570        580        590        600 
QQARLYQKTR QQAERLLEAD RLKTEFFQNV SHEFRTPLTL MIGPLETVVN QQQDLSLDQA 

       610        620        630        640        650        660 
KIALRNSRRL LRLVNQLLDL QRFDAGRMQP SFRPCDLVEF CQQTVESFKS YCDRKQINLV 

       670        680        690        700        710        720 
TNLQSCPQLY LDLERFDKVL YNLLSNAMKF TPTDGTITVS LQPEGNYCRL MVKDTGIGIK 

       730        740        750        760        770        780 
QEQLPHLFER FRQAEGSANR SFEGSGLGLA LVKELVELHH GRITVESEYG QGTTFTVWLQ 

       790        800        810        820        830        840 
MGNLHLPPSP LLDVPAEFDA RRAAVELADV EVDLPDVQID DINLPEVLVA DGSASLTDHG 

       850        860        870        880        890        900 
QLGSNTVLVV DDNPDLRRYV SMMLQNAGFN AVLAKNGADG FNKAQTYHPD VIVTDLMMPQ 

       910        920        930        940        950        960 
VSGLELIRMI RSSPELRGTP IILLTAKADE DTRIEGVERG ADAYVSKPFN DRELIAEVRN 

       970        980        990       1000       1010       1020 
LQALKAEERR VAHLNKYLTE SVLRRFLPES MVKKAAAGDL TLDLRPEPRL ITILFSDIVG 

      1030       1040       1050       1060       1070       1080 
FTRMSNALQS QGVAELLNEY LGEMTRAVFE NQGTVDKFVG DAIMALYGAP EEMSPSEQVR 

      1090       1100       1110       1120       1130       1140 
RAIATARQML VALEKLNQGW QERGLVGRNE VPPVRFRCGI HQGMAVVGLF GSQERSDFTA 

      1150       1160       1170       1180       1190       1200 
IGPSVNIAAR LQEATAPNSI MVSAMVAQYV PDEEIIKREF LELKGIDEPV MTCVINPNML 


NQ

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References

[1]	"The Spirulina platensis adenylate cyclase gene, cyaC, encodes a novel signal transduction protein." Kasahara M., Yashiro K., Sakamoto T., Ohmori M. Plant Cell Physiol. 38:828-836(1997) [PubMed: 9297847] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: IAM M-135 EMBL BAA22997.1.
[2]	"A novel mechanism for adenylyl cyclase inhibition from the crystal structure of its complex with catechol estrogen." Steegborn C., Litvin T.N., Hess K.C., Capper A.B., Taussig R., Buck J., Levin L.R., Wu H. J. Biol. Chem. 280:31754-31759(2005) [PubMed: 16002394] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1005-1199 IN COMPLEX WITH CALCIUM.
[3]	"Bicarbonate activation of adenylyl cyclase via promotion of catalytic active site closure and metal recruitment." Steegborn C., Litvin T.N., Levin L.R., Buck J., Wu H. Nat. Struct. Mol. Biol. 12:32-37(2005) [PubMed: 15619637] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1005-1202 IN COMPLEX WITH CALCIUM AND MAGNESIUM.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D49692 Genomic DNA. Translation: BAA22997.1.

PIR

T17197.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WC0	X-ray	2.40	A/B	1005-1202	[»]
1WC1	X-ray	1.93	A/B/C	998-1202	[»]
1WC3	X-ray	1.90	A/B	1005-1202	[»]
1WC4	X-ray	3.00	A/B	1005-1202	[»]
1WC5	X-ray	2.30	A/B/C/D	1005-1202	[»]
1WC6	X-ray	2.51	A/B/C	998-1202	[»]
2BW7	X-ray	2.30	A/B/C/D	1005-1199	[»]

ProteinModelPortal

O32393.

SMR

O32393. Positions 1004-1199.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR001054. A/G_cyclase.
IPR003594. ATPase-like_ATP-bd.
IPR011006. CheY-like_superfamily.
IPR003018. GAF.
IPR016132. Phyto_chromo_attachment.
IPR004358. Sig_transdc_His_kin-like_C.
IPR003661. Sig_transdc_His_kin_sub1_dim/P.
IPR005467. Sig_transdc_His_kinase_core.
IPR009082. Sig_transdc_His_kinase_dimeric.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]

Gene3D

G3DSA:3.30.70.1230. A/G_cyclase. 1 hit.
G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.

Pfam

PF01590. GAF. 2 hits.
PF00211. Guanylate_cyc. 1 hit.
PF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
PF00072. Response_reg. 2 hits.
[Graphical view]

PRINTS

PR00344. BCTRLSENSOR.

SMART

SM00044. CYCc. 1 hit.
SM00065. GAF. 2 hits.
SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00448. REC. 2 hits.
[Graphical view]

SUPFAM

SSF55073. A/G_cyclase. 1 hit.
SSF55874. ATP_bd_ATPase. 1 hit.
SSF52172. CheY_like. 2 hits.
SSF47384. His_kin_homodim. 1 hit.

PROSITE

PS50125. GUANYLATE_CYCLASE_2. 1 hit.
PS50109. HIS_KIN. 1 hit.
PS50046. PHYTOCHROME_2. 1 hit.
PS50110. RESPONSE_REGULATORY. 2 hits.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

O32393_SPIPL

Accession

Primary (citable) accession number: O32393

Entry history

Integrated into UniProtKB/TrEMBL:	January 1, 1998
Last sequence update:	January 1, 1998
Last modified:	January 25, 2012
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)