PCYAB_EUGGR
ID PCYAB_EUGGR Reviewed; 859 AA.
AC Q8S9F1;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Photoactivated adenylate cyclase subunit beta;
DE EC=4.6.1.1;
DE AltName: Full=Photoactivated adenylyl cyclase subunit beta;
GN Name=pacB {ECO:0000303|PubMed:11875575};
OS Euglena gracilis.
OC Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC Euglenales; Euglenaceae; Euglena.
OX NCBI_TaxID=3039;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAB85620.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-32, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=Z / UTEX 753 {ECO:0000312|EMBL:BAB85620.1};
RX PubMed=11875575; DOI=10.1038/4151047a;
RA Iseki M., Matsunaga S., Murakami A., Ohno K., Shiga K., Yoshida K.,
RA Sugai M., Takahashi T., Hori T., Watanabe M.;
RT "A blue-light-activated adenylyl cyclase mediates photoavoidance in Euglena
RT gracilis.";
RL Nature 415:1047-1051(2002).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=16121285; DOI=10.1039/b502002f;
RA Ntefidou M., Haeder D.-P.;
RT "Photoactivated adenylyl cyclase (PAC) genes in the flagellate Euglena
RT gracilis mutant strains.";
RL Photochem. Photobiol. Sci. 4:732-739(2005).
CC -!- FUNCTION: Acts as a blue light photoreceptor for the step-up
CC photophobic response. Mediates photoavoidance.
CC {ECO:0000269|PubMed:11875575}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1;
CC Evidence={ECO:0000269|PubMed:11875575};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:11875575};
CC -!- ACTIVITY REGULATION: Activity increased by up to 80-fold under blue
CC light. {ECO:0000269|PubMed:11875575}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 uM for ATP {ECO:0000269|PubMed:11875575};
CC Vmax=3.5 nmol/min/mg enzyme {ECO:0000269|PubMed:11875575};
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC {ECO:0000269|PubMed:11875575}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:11875575, ECO:0000269|PubMed:16121285}.
CC Note=Paraflagellar body, flagellum and paraxonemal bodies (PABs).
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; AB031226; BAB85620.1; -; mRNA.
DR AlphaFoldDB; Q8S9F1; -.
DR SMR; Q8S9F1; -.
DR SABIO-RK; Q8S9F1; -.
DR GO; GO:0031514; C:motile cilium; IDA:UniProtKB.
DR GO; GO:0004016; F:adenylate cyclase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009882; F:blue light photoreceptor activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0009881; F:photoreceptor activity; IDA:UniProtKB.
DR GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 2.
DR Gene3D; 3.30.70.1230; -; 2.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR InterPro; IPR007024; BLUF_domain.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR Pfam; PF04940; BLUF; 2.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR SMART; SM01034; BLUF; 2.
DR SUPFAM; SSF54975; SSF54975; 2.
DR SUPFAM; SSF55073; SSF55073; 2.
DR PROSITE; PS50925; BLUF; 2.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; cAMP biosynthesis; Cell projection; Chromophore; Cilium;
KW Direct protein sequencing; FAD; Flagellum; Flavoprotein; Lyase;
KW Nucleotide-binding; Photoreceptor protein; Receptor; Repeat;
KW Sensory transduction.
FT CHAIN 1..859
FT /note="Photoactivated adenylate cyclase subunit beta"
FT /id="PRO_0000195718"
FT DOMAIN 56..149
FT /note="BLUF 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00030"
FT DOMAIN 205..333
FT /note="Guanylate cyclase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT DOMAIN 471..563
FT /note="BLUF 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00030"
FT DOMAIN 619..748
FT /note="Guanylate cyclase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 420..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..847
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 859 AA; 94221 MW; C0EF4406D4A8F61E CRC64;
MYILVWKKGQ QIKTFHTLDE AAQFKAASNI DEAQMFSVTV APAISASGGS NEATNLRRLM
YLSKSTNPEE CNPQFLAEMA RVATIRNREI GVSGFLMYSS PFFFQVIEGT DEDLDFLFAK
ISADPRHERC IVLANGPCTG RMYGDWHMKD SHMDSITTHP AMKTILYQIA RSFSSMWSYL
PKSAGNMLLL GKDPAAQPPE PMSVVVTFIY LVEFGSILSN PNLTEQAAEV LSTFVDVCVK
NVEGSGGNIA KFITGICMAY WPINRTEEAL TAIQQISEDL AQLRSQQAPG SAVSLMYSQA
GVHYGRAMLC NAGSRKSDFT LLGDCINTTS RIATLAKKLK TPLLFSFEVR CLLGDEMREE
IEGAGMHQVK GRDKPVVVYQ FPGPELDVEM VRQKIEQFTP GRFRCQMPVV EYEALPISQR
PPIFDDTPKG NPRPRTPGYG GRQRSDSLVD RLIMIAKLAG PSVSATGDTT LTTLTYISQA
TRPMSRLDLS AIMRTATRRN AQQSITGTLL HVNGLFVQTL EGPKDAVVNL YLRIRQDPRH
TDVTTVHMAP LQERVYPSEW TLTSATEEML ATFPPLQDVL SQLAKSFTSL ETYVPSTVVR
YLTAGNNPRN LMPVSCGVVM LATDICSFTS LTEKSSLTEV WMICNTFIDA CTSAICQEGG
EVIKLIGDCV TAYFPGNNAD SAVAAAQELF TFCRQLREAF VDVLDVRGCV SCGVGLDYGQ
VVMAQCGSLG LTEYVVAGAV SARVMEVEAI TREVGYAIVV TEPVADRLSP QLRDHGIVPT
PQAIEGLPCY GIAGEEFELD VDSIKRGIKA LHAARSGEKP LTEPEEAKPD FRVSPGRVRH
GDSGRRSNSA QGKRSIQVR
