GCST_GLOVI
ID GCST_GLOVI Reviewed; 359 AA.
AC Q7NFJ5;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 25-MAY-2022, entry version 100.
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:0000255|HAMAP-Rule:MF_00259}; OrderedLocusNames=glr3530;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. {ECO:0000255|HAMAP-Rule:MF_00259}.
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 -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000255|HAMAP-
CC Rule:MF_00259}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC91471.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000045; BAC91471.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_926476.1; NC_005125.1.
DR AlphaFoldDB; Q7NFJ5; -.
DR SMR; Q7NFJ5; -.
DR STRING; 251221.35214102; -.
DR EnsemblBacteria; BAC91471; BAC91471; BAC91471.
DR KEGG; gvi:glr3530; -.
DR PATRIC; fig|251221.4.peg.3563; -.
DR eggNOG; COG0404; Bacteria.
DR HOGENOM; CLU_007884_10_2_3; -.
DR InParanoid; Q7NFJ5; -.
DR OrthoDB; 282830at2; -.
DR PhylomeDB; Q7NFJ5; -.
DR Proteomes; UP000000557; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Aminotransferase; Reference proteome; Transferase.
FT CHAIN 1..359
FT /note="Aminomethyltransferase"
FT /id="PRO_0000122560"
SQ SEQUENCE 359 AA; 39569 MW; 7857B9A1F3FDDD61 CRC64;
MSDLKRTPLC AQHLQLGARL VPFGGWEMPL QYSTLTREHR AVRTAVGLFD ISHMGKYTLS
GPDVLAQIQR LVPSDLARLQ PGQAQYTVLL NEQAGIIDDL IFYCRSPEHW VVIVNGATND
KDRRWLAEHL QGVHFDDLTG THTLLALQGP AAVETLQPLV DIDLARLGRF EHAQVSLAGK
PAFLARTGYT GEDGFEIMSL EPEGIALWQS LTAAGVPPCG LGARDTLRLE AAMHLYGQDM
DESTTPLEAS LGWVIDWDKP DYFGREILLA QKAQGTERRL VGLTVEGRQI ARHGYGLFDG
EQQVGVVTSG TLTPTVDRPI ALAYVGKPFA PIGSRLEVDI RGRRAMATVV KRPFYRRAL