YGIC_ECOLI
ID YGIC_ECOLI Reviewed; 386 AA.
AC P0ADT5; P24196; Q2M9G2;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Putative acid--amine ligase YgiC;
DE EC=6.3.1.-;
GN Name=ygiC; OrderedLocusNames=b3038, JW3006;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1314093; DOI=10.1016/0167-4781(92)90535-8;
RA Yang T.-P., Depew R.E.;
RT "Nucleotide sequence of a region duplicated in Escherichia coli toc
RT mutants.";
RL Biochim. Biophys. Acta 1130:227-228(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP LACK OF GLUTATHIONYLSPERMIDINE SYNTHETASE ACTIVITY, FUNCTION, ATP-BINDING,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=23097746;
RA Sui L., Warren J.C., Russell J.P., Stourman N.V.;
RT "Comparison of the functions of glutathionylspermidine synthetase/amidase
RT from E. coli and its predicted homologues YgiC and YjfC.";
RL Int. J. Biochem. Mol. Biol. 3:302-312(2012).
CC -!- FUNCTION: May be a ligase forming an amide bond. Shows ATPase activity.
CC Despite its similarity to the C-terminal synthetase domain of Gss, is
CC not a glutathionylspermidine (Gsp) synthetase. Cannot synthesize Gsp,
CC glutathione (GSH), or GSH intermediates, from GSH and spermidine,
CC cysteine and glutamate, gamma-glutamylcysteine and spermidine, and
CC gamma-glutamylcysteine and glycine. Does not bind to Gsp.
CC {ECO:0000269|PubMed:23097746}.
CC -!- DISRUPTION PHENOTYPE: Deletion of this gene does not affect the ability
CC to synthesize glutathionylspermidine. There is no visible differences
CC between wild-type and mutant strain growth in LB media.
CC {ECO:0000269|PubMed:23097746}.
CC -!- SIMILARITY: Belongs to the glutathionylspermidine synthase preATP-grasp
CC family. {ECO:0000305}.
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DR EMBL; M77129; AAA71876.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69206.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76074.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77094.1; -; Genomic_DNA.
DR PIR; S22361; S22361.
DR RefSeq; NP_417510.1; NC_000913.3.
DR RefSeq; WP_000442860.1; NZ_STEB01000001.1.
DR AlphaFoldDB; P0ADT5; -.
DR SMR; P0ADT5; -.
DR BioGRID; 4262389; 16.
DR DIP; DIP-48176N; -.
DR IntAct; P0ADT5; 14.
DR STRING; 511145.b3038; -.
DR jPOST; P0ADT5; -.
DR PaxDb; P0ADT5; -.
DR PRIDE; P0ADT5; -.
DR EnsemblBacteria; AAC76074; AAC76074; b3038.
DR EnsemblBacteria; BAE77094; BAE77094; BAE77094.
DR GeneID; 66673064; -.
DR GeneID; 947249; -.
DR KEGG; ecj:JW3006; -.
DR KEGG; eco:b3038; -.
DR PATRIC; fig|1411691.4.peg.3694; -.
DR EchoBASE; EB1153; -.
DR eggNOG; COG0754; Bacteria.
DR HOGENOM; CLU_059175_0_0_6; -.
DR InParanoid; P0ADT5; -.
DR OMA; QWNSLHE; -.
DR PhylomeDB; P0ADT5; -.
DR BioCyc; EcoCyc:EG11165-MON; -.
DR PRO; PR:P0ADT5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..386
FT /note="Putative acid--amine ligase YgiC"
FT /id="PRO_0000169401"
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
