ID   A6VL92_ACTSZ            Unreviewed;       846 AA.
AC   A6VL92;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Adenylate cyclase {ECO:0000256|ARBA:ARBA00021420, ECO:0000256|RuleBase:RU000604};
DE            EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201, ECO:0000256|RuleBase:RU000604};
GN   OrderedLocusNames=Asuc_0361 {ECO:0000313|EMBL:ABR73739.1};
OS   Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS   130Z).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=339671 {ECO:0000313|EMBL:ABR73739.1, ECO:0000313|Proteomes:UP000001114};
RN   [1] {ECO:0000313|Proteomes:UP000001114}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z
RC   {ECO:0000313|Proteomes:UP000001114};
RX   PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA   McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA   Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA   Burkhart K.B., Harkins V., Vieille C.;
RT   "A genomic perspective on the potential of Actinobacillus succinogenes for
RT   industrial succinate production.";
RL   BMC Genomics 11:680-680(2010).
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         ECO:0000256|RuleBase:RU000604};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU000604}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-1 family.
CC       {ECO:0000256|ARBA:ARBA00007901, ECO:0000256|RuleBase:RU004184}.
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DR   EMBL; CP000746; ABR73739.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6VL92; -.
DR   STRING; 339671.Asuc_0361; -.
DR   KEGG; asu:Asuc_0361; -.
DR   eggNOG; COG3072; Bacteria.
DR   HOGENOM; CLU_013280_0_0_6; -.
DR   OrthoDB; 5571448at2; -.
DR   Proteomes; UP000001114; Chromosome.
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   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   InterPro; IPR000274; Adenylate_cyclase_1.
DR   InterPro; IPR024686; Adenylate_cyclase_1_CS.
DR   InterPro; IPR024685; Adenylate_cyclase_1_N.
DR   InterPro; IPR043519; NT_sf.
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.
DR   PROSITE; PS01093; ADENYLATE_CYCLASE_1_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998,
KW   ECO:0000256|RuleBase:RU000604}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000604};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001114}.
FT   DOMAIN          5..203
FT                   /note="Adenylate cyclase class-I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12633"
SQ   SEQUENCE   846 AA;  98970 MW;  4FDF0918A9EA7C65 CRC64;
     MKYDLEFARK QVADLEKFRL FRALSGTTDE FRYVFQLIAL LLHANHPNLP GFVADAPTGI
     ADFKLTDYQR HYLHEILAQS SDIQFPQIFD RTSYAIDGVY VMGSIASIAQ TTSSDLDIWV
     CLREGLKARE REKLQQKAAA LQRWAKQYEV DVNLFLMDQN RFRNFQSSGV MTKENCGSTQ
     YMLLLDEFYR SAIRLAGKPL LWLHLLVEDE KNYESEVDDL IRRGEIDPLE WVDFGGLGKF
     SANEYFGASL WQLYKGIDAP YKAVIKILLL EEYSWEYPNT RLIASDFKFH LLMGHTEDHH
     FDPYLEMLER VTDYLTYRKD FKRLDDMRHC FYLKATEDWW YRNESNWRVD LINRLAQDWG
     WSKETIQDLN LRPFWKIKRV KQSYNKLMQM LMVSYRNLID FARKHHVDAN IVPQDISILT
     RKIYTAFEEL PGKVLLINPQ ISTDLSEPYL TFVEVTATDR PVKKGWYMLN QAPEVSGFSH
     PRYTEYSATL HKLVASAYFN GLLMPHTRLH IQSPNVSLPI LQEFITNLAE TLPVHALPPT
     NDDLHHPCEI RQLMVAINLS NDPTKQLTDS KMPIQQSDLF SFGSEQQNLV GSIDFIYRNL
     WNEIRTLHFE GPNAILMALK VLSNKIHHGS TALANIEVYS YSRNYRYSLA NIVTALIKKC
     IDIQLGTNQA ANSQSMLRVA GKNWQFFFEE RGISLHELPE NQELPVNELD KELYAEINKN
     DSVLPVRYEQ NMPEKLQYPS EIDSFASEGF LQFFFEDNSD DTFNVYILDE KNHVEIYHRC
     DGEKEQKINE INYIYTNADS SGNNPYGIIQ QNFNYPQFYR IIHNRYYEGN NPPVHIVPFQ
     RQAKYT
//