GCS2_ECOLI
ID GCS2_ECOLI Reviewed; 372 AA.
AC P77213;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Putative glutamate--cysteine ligase 2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE AltName: Full=Gamma-glutamylcysteine synthetase 2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE Short=GCS 2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE Short=Gamma-GCS 2 {ECO:0000255|HAMAP-Rule:MF_01609};
GN Name=ybdK; OrderedLocusNames=b0581, JW0570;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), FUNCTION, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=15211520; DOI=10.1002/prot.20103;
RA Lehmann C., Doseeva V., Pullalarevu S., Krajewski W., Howard A.,
RA Herzberg O.;
RT "YbdK is a carboxylate-amine ligase with a gamma-glutamyl:cysteine ligase
RT activity: crystal structure and enzymatic assays.";
RL Proteins 56:376-383(2004).
CC -!- FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits weak
CC glutamate--cysteine ligase activity. However, because of the low
CC catalytic rate, the question remains whether L-cysteine is the actual
CC biological substrate. {ECO:0000255|HAMAP-Rule:MF_01609,
CC ECO:0000269|PubMed:15211520}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-
CC cysteine + H(+) + phosphate; Xref=Rhea:RHEA:13285, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01609};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01609,
CC ECO:0000269|PubMed:15211520}.
CC -!- MISCELLANEOUS: Catalytic activity was tested towards all 20 common
CC amino acids, but was only observed with L-cysteine.
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family.
CC YbdK subfamily. {ECO:0000255|HAMAP-Rule:MF_01609}.
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DR EMBL; U82598; AAB40779.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73682.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35221.1; -; Genomic_DNA.
DR PIR; C64791; C64791.
DR RefSeq; NP_415113.1; NC_000913.3.
DR RefSeq; WP_001130654.1; NZ_SSZK01000104.1.
DR PDB; 1R8G; X-ray; 2.15 A; A/B=1-372.
DR PDBsum; 1R8G; -.
DR AlphaFoldDB; P77213; -.
DR SMR; P77213; -.
DR BioGRID; 4260711; 13.
DR BioGRID; 851576; 1.
DR IntAct; P77213; 6.
DR STRING; 511145.b0581; -.
DR jPOST; P77213; -.
DR PaxDb; P77213; -.
DR PRIDE; P77213; -.
DR EnsemblBacteria; AAC73682; AAC73682; b0581.
DR EnsemblBacteria; BAA35221; BAA35221; BAA35221.
DR GeneID; 947246; -.
DR KEGG; ecj:JW0570; -.
DR KEGG; eco:b0581; -.
DR PATRIC; fig|1411691.4.peg.1693; -.
DR EchoBASE; EB3408; -.
DR eggNOG; COG2170; Bacteria.
DR HOGENOM; CLU_044848_1_1_6; -.
DR InParanoid; P77213; -.
DR OMA; LIFGLHV; -.
DR PhylomeDB; P77213; -.
DR BioCyc; EcoCyc:G6326-MON; -.
DR BioCyc; MetaCyc:G6326-MON; -.
DR EvolutionaryTrace; P77213; -.
DR PRO; PR:P77213; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IDA:EcoCyc.
DR GO; GO:0042398; P:cellular modified amino acid biosynthetic process; IEA:InterPro.
DR HAMAP; MF_01609; Glu_cys_ligase_2; 1.
DR InterPro; IPR006336; GCS2.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR011793; YbdK.
DR Pfam; PF04107; GCS2; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR TIGRFAMs; TIGR02050; gshA_cyan_rel; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..372
FT /note="Putative glutamate--cysteine ligase 2"
FT /id="PRO_0000218196"
FT STRAND 14..24
FT /evidence="ECO:0007829|PDB:1R8G"
FT TURN 25..28
FT /evidence="ECO:0007829|PDB:1R8G"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:1R8G"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:1R8G"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:1R8G"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:1R8G"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:1R8G"
FT HELIX 69..89
FT /evidence="ECO:0007829|PDB:1R8G"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1R8G"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:1R8G"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:1R8G"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:1R8G"
FT HELIX 158..165
FT /evidence="ECO:0007829|PDB:1R8G"
FT HELIX 182..186
FT /evidence="ECO:0007829|PDB:1R8G"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:1R8G"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:1R8G"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:1R8G"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:1R8G"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:1R8G"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:1R8G"
FT HELIX 247..267
FT /evidence="ECO:0007829|PDB:1R8G"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:1R8G"
FT HELIX 280..290
FT /evidence="ECO:0007829|PDB:1R8G"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:1R8G"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:1R8G"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:1R8G"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:1R8G"
FT HELIX 307..317
FT /evidence="ECO:0007829|PDB:1R8G"
FT HELIX 319..324
FT /evidence="ECO:0007829|PDB:1R8G"
FT HELIX 328..340
FT /evidence="ECO:0007829|PDB:1R8G"
FT HELIX 344..353
FT /evidence="ECO:0007829|PDB:1R8G"
FT HELIX 358..369
FT /evidence="ECO:0007829|PDB:1R8G"
SQ SEQUENCE 372 AA; 41688 MW; 898310FD35B8032E CRC64;
MPLPDFHVSE PFTLGIELEM QVVNPPGYDL SQDSSMLIDA VKNKITAGEV KHDITESMLE
LATDVCRDIN QAAGQFSAMQ KVVLQAATDH HLEICGGGTH PFQKWQRQEV CDNERYQRTL
ENFGYLIQQA TVFGQHVHVG CASGDDAIYL LHGLSRFVPH FIALSAASPY MQGTDTRFAS
SRPNIFSAFP DNGPMPWVSN WQQFEALFRC LSYTTMIDSI KDLHWDIRPS PHFGTVEVRV
MDTPLTLSHA VNMAGLIQAT AHWLLTERPF KHQEKDYLLY KFNRFQACRY GLEGVITDPH
TGDRRPLTED TLRLLEKIAP SAHKIGASSA IEALHRQVVS GLNEAQLMRD FVADGGSLIG
LVKKHCEIWA GD
