ID Q6FCQ7_ACIAD Unreviewed; 914 AA.
AC Q6FCQ7;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 122.
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 Name=cphA {ECO:0000313|EMBL:CAG68152.1};
GN OrderedLocusNames=ACIAD1279 {ECO:0000313|EMBL:CAG68152.1};
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG68152.1, ECO:0000313|Proteomes:UP000000430};
RN [1] {ECO:0000313|EMBL:CAG68152.1, ECO:0000313|Proteomes:UP000000430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430};
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
RN [2] {ECO:0007829|PDB:7LGM}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.40 ANGSTROMS).
RX PubMed=34385683; DOI=10.1038/s41589-021-00854-y;
RA Sharon I., Haque A.S., Grogg M., Lahiri I., Seebach D., Leschziner A.E.,
RA Hilvert D., Schmeing T.M.;
RT "Structures and function of the amino acid polymerase cyanophycin
RT synthetase.";
RL Nat. Chem. Biol. 17:1101-1110(2021).
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}.
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DR EMBL; CR543861; CAG68152.1; -; Genomic_DNA.
DR RefSeq; WP_004925893.1; NC_005966.1.
DR PDB; 7LGM; EM; 4.40 A; A/B=1-914.
DR AlphaFoldDB; Q6FCQ7; -.
DR EMDB; EMD-23327; -.
DR SMR; Q6FCQ7; -.
DR STRING; 202950.GCA_001485005_01040; -.
DR GeneID; 45233698; -.
DR KEGG; aci:ACIAD1279; -.
DR eggNOG; COG0189; Bacteria.
DR eggNOG; COG0769; Bacteria.
DR HOGENOM; CLU_016806_0_0_6; -.
DR OrthoDB; 9803907at2; -.
DR BioCyc; ASP62977:ACIAD_RS05880-MONOMER; -.
DR BRENDA; 6.3.2.29; 107.
DR Proteomes; UP000000430; Chromosome.
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; 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; 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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:7LGM};
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CAG68152.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000000430}.
FT DOMAIN 223..476
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 914 AA; 99705 MW; F29EDAB3EA50C1E7 CRC64;
MNIISTSVYV GPNVYASIPL IRLVIDLNPH YITQLASMGS EVLENLEKVI PTLKTEQDAK
LQHKLEELRQ APQQQIGELV AILALHLQRL AGQKGGAAFS AYCHEDETEI LYSYESEEIG
IEAGEVVCDM LVALAKAHEA GDQIDLNRDV KGFLRYADRF ALGPSALALV QAAEERNIPW
YRLNDASLIQ VGQGKYQKRI EAALTSGTSH IAVEIAGDKN VCNQLLQDLG LPVPKQRVVY
DIDDAVRAAR RVGFPVVLKP LDGNHGRGVS VNLTTDEAVE AAFDIAMSEG SAVIVESMLY
GDDHRLLVVN GELVAAARRV PGHIVGDGKH NVEALIEIVN QDPRRGVGHE NMLTKIELDE
QALKLLAEKG YDKDSIPAKD EVVYLRRTAN ISTGGTAIDV TDTIHPENKL MAERAIRAVG
LDIGAVDFLT TDITKSYRDI GGGICEVNAG PGLRMHISPS EGPSRDVGGK IMDMLFPQGS
QSRVPIAAIT GTNGKTTCSR MLAHILKMAG HVVGQTSTDA VYIDGNVTVK GDMTGPVSAK
MVLRDPSVDI AVLETARGGI VRSGLGYQFC DVGAVLNVSS DHLGLGGVDT LDGLAEVKRV
IAEVTKDTVV LNADNAYTLK MAGHSPAKHI MYVTRDAENK LVREHIRLGK RAVVLEKGLN
GDQIVIYENG TQIPLIWTHL IPATLEGKAI HNVENAMFAA GMAYALGKNL DQIRIGLRTF
DNTFFQSPGR MNVFDKHGFR VILDYGHNEA AVGAMTELVD RLNPRGRRLL GVTCPGDRRD
EDVVAIAAKV AGHFDEYYCH RDDDLRGRAP DETPKIMRDA LIQLGVPESR IHIVEQEEDS
LAAVLTEAQV DDLVLFFCEN ITRSWKQIVH FTPEFNIEND HETLELKIAE QGFDIPEGYH
AVSNDRGVMI LPRG
//
