ID A0A061QA67_9PROT Unreviewed; 618 AA.
AC A0A061QA67;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Cyanophycin synthetase {ECO:0000313|EMBL:GAK32536.1};
GN Name=cphA {ECO:0000313|EMBL:GAK32536.1};
GN ORFNames=AQ1_00402 {ECO:0000313|EMBL:GAK32536.1};
OS alpha proteobacterium Q-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1492281 {ECO:0000313|EMBL:GAK32536.1, ECO:0000313|Proteomes:UP000027360};
RN [1] {ECO:0000313|EMBL:GAK32536.1, ECO:0000313|Proteomes:UP000027360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q-1 {ECO:0000313|EMBL:GAK32536.1,
RC ECO:0000313|Proteomes:UP000027360};
RX PubMed=22447601; DOI=10.1128/AEM.00084-12;
RA Suzuki M., Eda Y., Ohsawa S., Kanesaki Y., Yoshikawa H., Tanaka K.,
RA Muramatsu Y., Yoshikawa J., Sato I., Fujii T., Amachi S.;
RT "Iodide oxidation by a novel multicopper oxidase from the
RT alphaproteobacterium strain Q-1.";
RL Appl. Environ. Microbiol. 78:3941-3949(2012).
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:GAK32536.1}.
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DR EMBL; BAYV01000006; GAK32536.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061QA67; -.
DR STRING; 1492281.AQ1_00402; -.
DR Proteomes; UP000027360; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004363; F:glutathione synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR017534; GNAT-acetyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR004218; GSHS_ATP-bd.
DR NCBIfam; TIGR03103; trio_acet_GNAT; 1.
DR PANTHER; PTHR21621:SF0; BETA-CITRYLGLUTAMATE SYNTHASE B-RELATED; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF02955; GSH-S_ATP; 1.
DR Pfam; PF08443; RimK; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000027360}.
FT DOMAIN 141..291
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT DOMAIN 360..604
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 618 AA; 69136 MW; 751EAF2A43D39B31 CRC64;
MSDAPDDQKD GPANGEQTGK RRAEPSASPG RKPGSARPDR QYRLDKMRAQ SLKPQHKTMA
HDAFIDCGWG RLYFAQTFDR LDDVVEALRQ EMPQQRDIAF YLRDPHVALS KAPQELFLDP
SHTYRLDLHT YQPAVRRFRG FHIRRLSHRS DIAEINRIYA ARNMVQVDPS FFWDRRDSRS
LTYYVAQDDE SGALVGTVTG VNHYQAYHDP ERGASLWCLA VDPQSPYPGI GEALVRRLAE
HFQARGNAYM DLSVMHDNEQ AIALYEKLGF QRLPFFALKN KNSINEKLFA GPSFDANFNP
YALIIVNEAR RRGIHVDVLD AENGYFRLSF GGRSVICRES LTELTSAIAM SRCADKMVTR
RLLGAANIRV PAQQQAALNP DRNADFLHEH GAIVVKPRHG EQGRGVSVNI TDAAHLEQAV
EAARRVDDHV LLEEYFDGID LRIIVIGFKL VAAAIRRPAA IIGDGSSTIE ALIKAQSRRR
MAATNGESRI PIDQETERTI RNGGFELSTI LPAKKQLFVR KTANLHTGGT LHDVTDRLHP
HLCQAAITCA KTIDIPVVGV DMIVKSPSEP DYIVIEANER PGLANHEPQP TAERFIDLLF
PHSLPTDLKL SKDIGGGS
//
