YGIC_ECOL6
ID YGIC_ECOL6 Reviewed; 386 AA.
AC P0ADT6; P24196;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Putative acid--amine ligase YgiC;
DE EC=6.3.1.-;
GN Name=ygiC; OrderedLocusNames=c3784;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: May be a ligase forming an amide bond. Shows ATPase activity
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutathionylspermidine synthase preATP-grasp
CC family. {ECO:0000305}.
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DR EMBL; AE014075; AAN82228.1; -; Genomic_DNA.
DR RefSeq; WP_000442860.1; NC_004431.1.
DR AlphaFoldDB; P0ADT6; -.
DR SMR; P0ADT6; -.
DR STRING; 199310.c3784; -.
DR EnsemblBacteria; AAN82228; AAN82228; c3784.
DR GeneID; 66673064; -.
DR KEGG; ecc:c3784; -.
DR eggNOG; COG0754; Bacteria.
DR HOGENOM; CLU_059175_0_0_6; -.
DR OMA; QWNSLHE; -.
DR BioCyc; ECOL199310:C3784-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR005494; GSPS_pre-ATP-grasp-like_dom.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR Pfam; PF03738; GSP_synth; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding.
FT CHAIN 1..386
FT /note="Putative acid--amine ligase YgiC"
FT /id="PRO_0000169403"
FT BINDING 100..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 371..373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 100
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 386 AA; 45026 MW; 5DB19CE4F3FE4783 CRC64;
MERVSITERP DWREKAHEYG FNFHTMYGEP YWCEDAYYKL TLAQVEKLEE VTAELHQMCL
KVVEKVIASD ELMTKFRIPK HTWSFVRQSW LTHQPSLYSR LDLAWDGTGE PKLLENNADT
PTSLYEAAFF QWIWLEDQLN AGNLPEGSDQ FNSLQEKLID RFVELREQYG FQLLHLTCCR
DTVEDRGTIQ YLQDCATEAE IATEFLYIDD IGLGEKGQFT DLQDQVISNL FKLYPWEFML
REMFSTKLED AGVRWLEPAW KSIISNKALL PLLWEMFPNH PNLLPAYFAE DDHPQMEKYV
VKPIFSREGA NVSIIENGKT IEAAEGPYGE EGMIVQQFHP LPKFGDSYML IGSWLVNDQP
AGIGIREDRA LITQDMSRFY PHIFVE