KGCY_HEDDI
ID KGCY_HEDDI Reviewed; 393 AA.
AC P51546;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Glycocyamine kinase;
DE Short=GK;
DE EC=2.7.3.1;
DE AltName: Full=Guanidinoacetate kinase;
OS Hediste diversicolor (Sandworm) (Nereis diversicolor).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Errantia; Phyllodocida; Nereididae; Hediste;
OC Hediste diversicolor species group.
OX NCBI_TaxID=126592;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8145248; DOI=10.1006/jmbi.1994.1237;
RA Suzuki T., Furukohri T.;
RT "Evolution of phosphagen kinase. Primary structure of glycocyamine kinase
RT and arginine kinase from invertebrates.";
RL J. Mol. Biol. 237:353-357(1994).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + guanidinoacetate = ADP + H(+) + phosphoguanidinoacetate;
CC Xref=Rhea:RHEA:14145, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57612, ChEBI:CHEBI:57742, ChEBI:CHEBI:456216; EC=2.7.3.1;
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
CC ProRule:PRU00843}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D26103; BAA05099.1; -; mRNA.
DR PIR; S77896; S77896.
DR AlphaFoldDB; P51546; -.
DR SMR; P51546; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004111; F:creatine kinase activity; IEA:InterPro.
DR GO; GO:0047973; F:guanidinoacetate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.135.10; -; 1.
DR InterPro; IPR000749; ATP-guanido_PTrfase.
DR InterPro; IPR022415; ATP-guanido_PTrfase_AS.
DR InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR InterPro; IPR022413; ATP-guanido_PTrfase_N.
DR InterPro; IPR036802; ATP-guanido_PTrfase_N_sf.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR PANTHER; PTHR11547; PTHR11547; 2.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR Pfam; PF02807; ATP-gua_PtransN; 1.
DR SUPFAM; SSF48034; SSF48034; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
DR PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..393
FT /note="Glycocyamine kinase"
FT /id="PRO_0000212008"
FT DOMAIN 7..94
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT DOMAIN 120..362
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT REGION 367..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 123..127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 287..291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 315..320
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 330
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
SQ SEQUENCE 393 AA; 44462 MW; CB529ADC9B3CCFC1 CRC64;
MFKDYSREKF AKENFPDLSK HNNVMASHLT YELYEKYWDK VTPNGVTLDK CIQTGVDNPG
NKFYGKKTGC VFGDEHSYET FKDFFDRVIE EIHHFKPEDV HPATDLDETK LVGGVFDEKY
VKSCRIRCGR SVRGVCLPPA MSRAERRLVE KVVSNALGGL KEDLAGKYFP LTTMNDKDME
ALIEDHFLFE KPTGALLTTS GCARDWPDGR GIWHNNGKNF LVWINEEDHI RIISMQKGGD
MRAVFSRFGR GLTEVERLMK EKGYELMRNE RLGYICTCPT NLGTVVRASV HLRLANLEKD
KRFDDFLAKL RLGKRGTGGE SSLAEDSTYD ISNLARLGKS ERELVQVLVD GVNVLIEADK
RLEAGKPIDD LTPRLNSSTG TSISATASRH MTL
