GCST_ECOLI
ID GCST_ECOLI Reviewed; 364 AA.
AC P27248; Q2M9T6;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Aminomethyltransferase {ECO:0000255|HAMAP-Rule:MF_00259};
DE EC=2.1.2.10 {ECO:0000255|HAMAP-Rule:MF_00259};
DE AltName: Full=Glycine cleavage system T protein {ECO:0000255|HAMAP-Rule:MF_00259};
GN Name=gcvT {ECO:0000303|PubMed:8375392}; OrderedLocusNames=b2905, JW2873;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8219277; DOI=10.3109/10425179309020835;
RA Stauffer L.T., Ghrist A., Stauffer G.V.;
RT "The Escherichia coli gcvT gene encoding the T-protein of the glycine
RT cleavage enzyme system.";
RL DNA Seq. 3:339-346(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21, FUNCTION, AND
RP SUBUNIT.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8375392; DOI=10.1111/j.1432-1033.1993.tb18172.x;
RA Okamura-Ikeda K., Ohmura Y., Fujiwara K., Motokawa Y.;
RT "Cloning and nucleotide sequence of the gcv operon encoding the Escherichia
RT coli glycine-cleavage system.";
RL Eur. J. Biochem. 216:539-548(1993).
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 PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. {ECO:0000255|HAMAP-Rule:MF_00259, ECO:0000269|PubMed:8375392}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-
CC aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-
CC 5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] +
CC NH4(+); Xref=Rhea:RHEA:16945, Rhea:RHEA-COMP:10475, Rhea:RHEA-
CC COMP:10492, ChEBI:CHEBI:15636, ChEBI:CHEBI:28938, ChEBI:CHEBI:57453,
CC ChEBI:CHEBI:83100, ChEBI:CHEBI:83143; EC=2.1.2.10;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00259};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000255|HAMAP-Rule:MF_00259,
CC ECO:0000269|PubMed:8375392}.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000255|HAMAP-
CC Rule:MF_00259, ECO:0000305}.
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DR EMBL; M97263; AAC36843.1; -; Unassigned_DNA.
DR EMBL; X73958; CAA52144.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69073.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75943.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76970.1; -; Genomic_DNA.
DR PIR; A56689; A56689.
DR RefSeq; NP_417381.1; NC_000913.3.
DR RefSeq; WP_000068701.1; NZ_STEB01000001.1.
DR PDB; 1VLO; X-ray; 1.70 A; A=2-363.
DR PDB; 3A8I; X-ray; 1.99 A; A/B/C/D=1-364.
DR PDB; 3A8J; X-ray; 1.98 A; A/B/C/D=1-364.
DR PDB; 3A8K; X-ray; 1.95 A; A/B/C/D=1-364.
DR PDBsum; 1VLO; -.
DR PDBsum; 3A8I; -.
DR PDBsum; 3A8J; -.
DR PDBsum; 3A8K; -.
DR AlphaFoldDB; P27248; -.
DR SMR; P27248; -.
DR BioGRID; 4262343; 44.
DR ComplexPortal; CPX-3949; Glycine cleavage system complex.
DR IntAct; P27248; 6.
DR STRING; 511145.b2905; -.
DR jPOST; P27248; -.
DR PaxDb; P27248; -.
DR PRIDE; P27248; -.
DR EnsemblBacteria; AAC75943; AAC75943; b2905.
DR EnsemblBacteria; BAE76970; BAE76970; BAE76970.
DR GeneID; 66673221; -.
DR GeneID; 947390; -.
DR KEGG; ecj:JW2873; -.
DR KEGG; eco:b2905; -.
DR PATRIC; fig|1411691.4.peg.3827; -.
DR EchoBASE; EB1412; -.
DR eggNOG; COG0404; Bacteria.
DR HOGENOM; CLU_007884_10_2_6; -.
DR InParanoid; P27248; -.
DR OMA; MPVQYPA; -.
DR PhylomeDB; P27248; -.
DR BioCyc; EcoCyc:GCVT-MON; -.
DR BioCyc; MetaCyc:GCVT-MON; -.
DR BRENDA; 1.4.1.27; 2026.
DR EvolutionaryTrace; P27248; -.
DR PRO; PR:P27248; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005960; C:glycine cleavage complex; IC:ComplexPortal.
DR GO; GO:0004047; F:aminomethyltransferase activity; IDA:EcoCyc.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IC:ComplexPortal.
DR GO; GO:0006730; P:one-carbon metabolic process; IC:ComplexPortal.
DR Gene3D; 3.30.1360.120; -; 1.
DR HAMAP; MF_00259; GcvT; 1.
DR InterPro; IPR006223; GCS_T.
DR InterPro; IPR022903; GCS_T_bac.
DR InterPro; IPR028896; GCST/YgfZ/DmdA.
DR InterPro; IPR013977; GCV_T_C.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR PANTHER; PTHR43757; PTHR43757; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR SUPFAM; SSF101790; SSF101790; 1.
DR TIGRFAMs; TIGR00528; gcvT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Direct protein sequencing;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8375392,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 2..364
FT /note="Aminomethyltransferase"
FT /id="PRO_0000122554"
FT HELIX 8..13
FT /evidence="ECO:0007829|PDB:1VLO"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:1VLO"
FT STRAND 24..31
FT /evidence="ECO:0007829|PDB:1VLO"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:1VLO"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:1VLO"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:1VLO"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:1VLO"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1VLO"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1VLO"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:1VLO"
FT STRAND 95..105
FT /evidence="ECO:0007829|PDB:1VLO"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:1VLO"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:1VLO"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:1VLO"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1VLO"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:1VLO"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:1VLO"
FT HELIX 152..157
FT /evidence="ECO:0007829|PDB:1VLO"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:1VLO"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:1VLO"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:1VLO"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:1VLO"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:1VLO"
FT HELIX 201..213
FT /evidence="ECO:0007829|PDB:1VLO"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:1VLO"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:1VLO"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:1VLO"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:1VLO"
FT HELIX 267..276
FT /evidence="ECO:0007829|PDB:1VLO"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:1VLO"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:1VLO"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:1VLO"
FT STRAND 307..318
FT /evidence="ECO:0007829|PDB:1VLO"
FT TURN 319..322
FT /evidence="ECO:0007829|PDB:1VLO"
FT STRAND 323..330
FT /evidence="ECO:0007829|PDB:1VLO"
FT STRAND 336..342
FT /evidence="ECO:0007829|PDB:1VLO"
FT STRAND 345..352
FT /evidence="ECO:0007829|PDB:1VLO"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:3A8I"
SQ SEQUENCE 364 AA; 40147 MW; 1F58C5A244F82242 CRC64;
MAQQTPLYEQ HTLCGARMVD FHGWMMPLHY GSQIDEHHAV RTDAGMFDVS HMTIVDLRGS
RTREFLRYLL ANDVAKLTKS GKALYSGMLN ASGGVIDDLI VYYFTEDFFR LVVNSATREK
DLSWITQHAE PFGIEITVRD DLSMIAVQGP NAQAKAATLF NDAQRQAVEG MKPFFGVQAG
DLFIATTGYT GEAGYEIALP NEKAADFWRA LVEAGVKPCG LGARDTLRLE AGMNLYGQEM
DETISPLAAN MGWTIAWEPA DRDFIGREAL EVQREHGTEK LVGLVMTEKG VLRNELPVRF
TDAQGNQHEG IITSGTFSPT LGYSIALARV PEGIGETAIV QIRNREMPVK VTKPVFVRNG
KAVA
