ID A0A231MZX5_9GAMM Unreviewed; 866 AA.
AC A0A231MZX5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Adenylate cyclase {ECO:0000256|ARBA:ARBA00021420};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
DE AltName: Full=ATP pyrophosphate-lyase {ECO:0000256|ARBA:ARBA00032597};
DE AltName: Full=Adenylyl cyclase {ECO:0000256|ARBA:ARBA00032637};
GN ORFNames=CGX12_08450 {ECO:0000313|EMBL:OXS15590.1};
OS Zobellella denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Zobellella.
OX NCBI_TaxID=347534 {ECO:0000313|EMBL:OXS15590.1, ECO:0000313|Proteomes:UP000215233};
RN [1] {ECO:0000313|EMBL:OXS15590.1, ECO:0000313|Proteomes:UP000215233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZD1 {ECO:0000313|EMBL:OXS15590.1,
RC ECO:0000313|Proteomes:UP000215233};
RA Wu Y.-W., Chu K.-H.;
RT "Draft genome of Zobellella denitrificans ZD1.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001593};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-1 family.
CC {ECO:0000256|ARBA:ARBA00007901, ECO:0000256|RuleBase:RU004184}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXS15590.1}.
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DR EMBL; NMUO01000029; OXS15590.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A231MZX5; -.
DR OrthoDB; 5571448at2; -.
DR Proteomes; UP000215233; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR000274; Adenylate_cyclase_1.
DR InterPro; IPR024686; Adenylate_cyclase_1_CS.
DR InterPro; IPR024685; Adenylate_cyclase_1_N.
DR PANTHER; PTHR38760; ADENYLATE CYCLASE; 1.
DR PANTHER; PTHR38760:SF1; ADENYLATE CYCLASE; 1.
DR Pfam; PF12633; Adenyl_cycl_N; 1.
DR Pfam; PF01295; Adenylate_cycl; 1.
DR PIRSF; PIRSF001444; Adenylate_cycl; 1.
DR PROSITE; PS01092; ADENYLATE_CYCLASE_1_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 37..231
FT /note="Adenylate cyclase class-I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12633"
SQ SEQUENCE 866 AA; 98975 MW; 56EA1DE794387445 CRC64;
MADIVHLLAN CYHDHTFDLS RVCVGPTKAC TLHANFHRLV ERCDQFNQQK QARALAVMSR
YGQQVFQLLP VLLHYHHPLL PGYLPGDVPA GVCHFRPNER QQEFIDELCQ AANGHQGLQH
GKNEIFGLYS MGSTSSIGQC RHSDLDVWVC YSHQMAPERV ELLQQKCLLI SKWAEQRQVE
LNLFLIPDNK FRTDNQQWVQ GESCGSAQHL LLLDEFYRSN LRIAGKRLVW MFAPGKLGPK
YDQFVAEQFA NGTLNTDEWL DLGGFARIPA EEYFGSALWQ LYKGIDSPYK AVLKTVLMEA
YSHEYPDTQL LCRHLKGHFQ SSEVLDEYQD HYMLMLEKVT GYLKSIGDEK RLDLVRRCFY
LKVSEGLHRT HGNDAQYAWR RKLINRLVAA WGWPADKLAR LDDRAHWKVE EVKAAYGELL
EALMQSYRNL IQFARRNNIS ECINPEDIGI LSRKLYAAFE NLPGKVQLIN LKIAPDLSEP
DISLVQVPEG RVNPAGWYLY KCGLAPGDII GRSPLEYSGY VGKLVAWAHF NGLLVPSTRL
HLFNQNTDLT RRHLQEFCGD LARIFPVRTP APTNLALSRP CEVRNLGIFL NLETDPTARW
RNRAIEFSAK TSDPFSFGHQ LENLVGSVDL IYRNSWDEIR TLHFSGPTAV VEALTTILGK
MHQDANAPES LDVHCYSLNF RSLIRTRFEQ LVKECIGLRL ARAQGSTIKT LVLGGDKYGI
FFERRGVSVQ KMENAVDFYR QLSSQKQSRH ALRLDQQDDK AVPDIVDAYA SEGLMQFFFE
DAGDGYNLYI LDEANRVEVY RQVSGSKDEL VQSINRFYTS HHEHGVGQSH FANFNLPQYY
EIVAADGQPR VLPYRTVKDD PRACLG
//