ID A0A1Q7S8T3_9CHLR Unreviewed; 892 AA.
AC A0A1Q7S8T3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Cyanophycin synthetase {ECO:0000256|ARBA:ARBA00022036};
DE EC=6.3.2.29 {ECO:0000256|ARBA:ARBA00013005};
DE EC=6.3.2.30 {ECO:0000256|ARBA:ARBA00012968};
DE AltName: Full=Cyanophycin synthase {ECO:0000256|ARBA:ARBA00031353};
GN ORFNames=AUF61_02835 {ECO:0000313|EMBL:OLD72683.1};
OS Chloroflexi bacterium 13_1_20CM_66_33.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1805065 {ECO:0000313|EMBL:OLD72683.1, ECO:0000313|Proteomes:UP000187547};
RN [1] {ECO:0000313|EMBL:OLD72683.1, ECO:0000313|Proteomes:UP000187547}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
CC -!- FUNCTION: Catalyzes the ATP-dependent polymerization of arginine and
CC aspartate to multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a
CC water-insoluble reserve polymer). {ECO:0000256|ARBA:ARBA00003184}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[L-4-(L-arginin-2-N-yl)aspartate](n) + ATP + L-aspartate = [L-
CC 4-(L-arginin-2-N-yl)aspartate](n)-L-aspartate + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:13277, Rhea:RHEA-COMP:13728, Rhea:RHEA-
CC COMP:13733, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:137986, ChEBI:CHEBI:137990,
CC ChEBI:CHEBI:456216; EC=6.3.2.29;
CC Evidence={ECO:0000256|ARBA:ARBA00000535};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[L-4-(L-arginin-2-N-yl)aspartate](n)-L-aspartate + ATP + L-
CC arginine = [L-4-(L-arginin-2-N-yl)aspartate](n+1) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:23888, Rhea:RHEA-COMP:13732, Rhea:RHEA-
CC COMP:13733, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:137986, ChEBI:CHEBI:137990,
CC ChEBI:CHEBI:456216; EC=6.3.2.30;
CC Evidence={ECO:0000256|ARBA:ARBA00000917};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MurCDEF family.
CC {ECO:0000256|ARBA:ARBA00009060}.
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:OLD72683.1}.
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DR EMBL; MNIE01000049; OLD72683.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7S8T3; -.
DR Proteomes; UP000187547; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0071161; F:cyanophycin synthetase activity (L-arginine-adding); IEA:UniProtKB-EC.
DR GO; GO:0071160; F:cyanophycin synthetase activity (L-aspartate-adding); IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0009059; P:macromolecule biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR011810; Cya_phycin_syn.
DR InterPro; IPR044019; Cyanophycin_syn_N.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR004101; Mur_ligase_C.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR NCBIfam; TIGR02068; cya_phycin_syn; 1.
DR PANTHER; PTHR23135:SF18; CYANOPHYCIN SYNTHETASE; 1.
DR PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR Pfam; PF13549; ATP-grasp_5; 1.
DR Pfam; PF18921; Cyanophycin_syn; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 224..479
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 892 AA; 96789 MW; EAE9916AA3249BFC CRC64;
MSPDLKILES QVLRGPNYWS YEPAIRLLVD LGSLEHWPSN TLPKFTDVLV GLLPGLHDHG
CSLHRPGGFI ERLRDGTWMG HVAEHVALEL QREAGGSTTR GKTRRAGTPG QYNVVYGYSE
EQVGLAAGKL AVRLLNHLVQ ANPTFDFVAE LESLVLLADR AAFGPSTQAI LDEAARRDIP
YIRLNDQSFV QLGQGKYQQR IRATMTSRTS ALGVDIAGDK KLTTTLLAAA GLPVPRSDMV
RSADEAGAVA ARIGYPVVTK PLDGNHGRGV SLDLRTDADV RRGFERAIEQ TRSGIVVVES
YIQGNDYRVL VIDGHMVAVA QRVPAHVIGD GEHTVRELVD ITNRDPRRGI GHEKVLTRIK
VDGSAEELVK RQGFDLDAVP PKGSVLKLAA TGNMSTGGIS IDRTWEADHD NVEIAEEAAR
VVGLDVAGID FLTPDICQPV RETGGAIVEV NAAPGFRMHT HPTEGDPQYV AKAVIDMMFP
QGTSARIPIV AVTGSNGKTT TARMIAHIVR GLGHHVGMTT TDGIYIDGRL VKQADASGPR
SARMVLQNPR VDFAVFEVAR GGILREGLGY SANDVAVVLN VTGDHIGLKE VNSLRQLAAI
KRVIVEAVPR SGTAVLNADD ELVADMRTHC SGSVILFSLR DDNELVERWV RRGRKAFVIQ
KQAGGGEMMV LREGRRSTQI GWVHLLPATF EGRARANVQN ALAAAAAAHA AGAHLHDIRQ
GLRSFHPSFH EAPGRLNMFE LHGVKVIVDY AHNPHGLEMA GDFVERLTAP GVNGPEPGRR
IAVIATPGDR RDEDIRELGR VAARVFDDLI VREDANPRGR QRGEIAQHVM EGIKAATESR
VRYAEVIIDE RPAIDAALRR ARAGDVVLLC VDKPADTWHD LEARRALPVS PA
//
