ID   Q8F6W6_LEPIN            Unreviewed;       530 AA.
AC   Q8F6W6;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 121.
DE   SubName: Full=Adenylate/guanylate cyclase {ECO:0000313|EMBL:AAN48383.1};
GN   Name=cyaA {ECO:0000313|EMBL:AAN48383.1};
GN   OrderedLocusNames=LA_1184 {ECO:0000313|EMBL:AAN48383.1};
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=189518 {ECO:0000313|EMBL:AAN48383.1, ECO:0000313|Proteomes:UP000001408};
RN   [1] {ECO:0000313|EMBL:AAN48383.1, ECO:0000313|Proteomes:UP000001408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601 {ECO:0000313|EMBL:AAN48383.1,
RC   ECO:0000313|Proteomes:UP000001408};
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.X., Fu G., Jiang X.G., Zeng R., Miao Y.G., Xu H., Zhang Y.X.,
RA   Xiong H., Lu G., Lu L.F., Jiang H.Q., Jia J., Tu Y.F., Jiang J.X., Gu W.Y.,
RA   Zhang Y.Q., Cai Z., Sheng H.H., Yin H.F., Zhang Y., Zhu G.F., Wan M.,
RA   Huang H.L., Qian Z., Wang S.Y., Ma W., Yao Z.J., Shen Y., Qiang B.Q.,
RA   Xia Q.C., Guo X.K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.M.,
RA   Shi M.H., Chen Z., Xu J.G., Zhao G.P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE010300; AAN48383.1; -; Genomic_DNA.
DR   RefSeq; NP_711365.1; NC_004342.2.
DR   RefSeq; WP_000604736.1; NC_004342.2.
DR   AlphaFoldDB; Q8F6W6; -.
DR   STRING; 189518.LA_1184; -.
DR   PaxDb; 189518-LA_1184; -.
DR   EnsemblBacteria; AAN48383; AAN48383; LA_1184.
DR   GeneID; 61142383; -.
DR   KEGG; lil:LA_1184; -.
DR   PATRIC; fig|189518.3.peg.1179; -.
DR   HOGENOM; CLU_513679_0_0_12; -.
DR   InParanoid; Q8F6W6; -.
DR   OrthoDB; 9810588at2; -.
DR   Proteomes; UP000001408; Chromosome I.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR   GO; GO:0006171; P:cAMP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   CDD; cd00207; fer2; 1.
DR   CDD; cd00314; plant_peroxidase_like; 1.
DR   Gene3D; 1.10.520.10; -; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   Gene3D; 1.10.420.10; Peroxidase, domain 2; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR002016; Haem_peroxidase.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR002207; Peroxidase_I.
DR   PANTHER; PTHR43081:SF16; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC; 1.
DR   PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00459; ASPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001408}.
FT   DOMAIN          1..95
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          117..250
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   DOMAIN          371..530
FT                   /note="Plant heme peroxidase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50873"
SQ   SEQUENCE   530 AA;  59459 MW;  EBE31DDC08E45D10 CRC64;
     MILVNFENEK EISLSKPQNL LEISLNNGIP HTHACGGNAR CSTCRVLVLE NPSHLSPPEQ
     KEKELSQKKG FPKSVRLACQ TTVLGDVRVR RIVLDEEDYN LTIPGSATIS GEEKEIAILF
     SDIRDFTLFS ESHLPYDVIH ILNRYFYKMG DVILKHGGKI DKYIGDGLMA LFGVNGGSPQ
     EICISALRAA KEMELELYSL NEYLKSHLHT SFRIGVGVHY GNCILGQLGH PANMSYTAIG
     DSVNIASRIE SKTKKSGASV LISESLYKQV KEKVVKGRVF SAQLKGKTGN YKLYEIQEIL
     EKVDANLWEE AKNSLRRIIL VREVGSWLKL VYHLSCLFDE NQNWIGLSAA NSFQKFSKLP
     ENGDLVQNFY QIKDTFNEQF QNSFSFADLL ALAGAVAIEK SGGPKIPIQP GRKDRLLSEV
     FQILPLSMQT QKDQLPYLQK MKLGIRDIVL ISGARTIGWL GGESFTSNPY NFDNSYFHVL
     LKAGLEGPLL IPNDRELLKN DESRAFVLDY ALDPSKFFED FTSTYLKLTS
//