ID GCST_ECOUT Reviewed; 364 AA.
AC Q1R7C6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 01-MAY-2013, entry version 49.
DE RecName: Full=Aminomethyltransferase;
DE EC=2.1.2.10;
DE AltName: Full=Glycine cleavage system T protein;
GN Name=gcvT; OrderedLocusNames=UTI89_C3290;
OS Escherichia coli (strain UTI89 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=364106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTI89 / UPEC;
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R.,
RA Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R.,
RA Hultgren S.J., Gordon J.I.;
RT "Identification of genes subject to positive selection in
RT uropathogenic strains of Escherichia coli: a comparative genomics
RT approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine (By similarity).
CC -!- CATALYTIC ACTIVITY: [Protein]-S(8)-aminomethyldihydrolipoyllysine
CC + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-
CC methylenetetrahydrofolate + NH(3).
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins:
CC P, T, L and H (By similarity).
CC -!- SIMILARITY: Belongs to the GcvT family.
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DR EMBL; CP000243; ABE08738.1; -; Genomic_DNA.
DR RefSeq; YP_542269.1; NC_007946.1.
DR ProteinModelPortal; Q1R7C6; -.
DR SMR; Q1R7C6; 4-364.
DR STRING; 364106.UTI89_C3290; -.
DR EnsemblBacteria; ABE08738; ABE08738; UTI89_C3290.
DR GeneID; 3990521; -.
DR KEGG; eci:UTI89_C3290; -.
DR PATRIC; 18456090; VBIEscCol42261_3263.
DR eggNOG; COG0404; -.
DR HOGENOM; HOG000239381; -.
DR KO; K00605; -.
DR OMA; KALYGGM; -.
DR ProtClustDB; PRK00389; -.
DR BioCyc; ECOL364106:GHPQ-3313-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:HAMAP.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:HAMAP.
DR Gene3D; 3.30.1360.120; -; 2.
DR HAMAP; MF_00259; GcvT; 1; -.
DR InterPro; IPR013977; GCV_T_C.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR006223; GcvT.
DR InterPro; IPR022903; NH2_Me_Trfase.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR PANTHER; PTHR13847:SF5; PTHR13847:SF5; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR PIRSF; PIRSF006487; GcvT; 1.
DR TIGRFAMs; TIGR00528; gcvT; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Complete proteome; Transferase.
FT CHAIN 1 364 Aminomethyltransferase.
FT /FTId=PRO_1000047662.
SQ SEQUENCE 364 AA; 40149 MW; F54BFBB25282F43A CRC64;
MAQQTPLYEQ HTLCGARMVD FHGWMMPLHY GSQIDEHHAV RTDAGMFDVS HMTIVDLRGS
RTREFLRYLL ANDVAKLTKS GKALYSGMLN ASGGVIDDLI VYYFTEDFFR LVVNSATREK
DLSWITQHAE PFGIEITVRD DLSMIAVQGP NAQAKAATLF NDAQRQAVEG MKPFFGVQAG
DLFIATTGYT GEAGYEIALP NEKAADFWRA LVEAGVKPCG LGARDTLRLE AGMNLYSQEM
DETISPLAAN MGWTIAWEPA DRDFIGREAL EAQREHGTEK LVGLVMTEKG VLRNELPVRF
TDAQGNQHEG IITSGTFSPT LGYSIALARV PEGIGETAIV QIRNREMPVK VTKPVFVRNG
KAVA
//
