GCST_PROMA
ID GCST_PROMA Reviewed; 373 AA.
AC Q7V9I2;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 95.
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=Pro_1851;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(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}.
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DR EMBL; AE017126; AAQ00895.1; -; Genomic_DNA.
DR RefSeq; NP_876242.1; NC_005042.1.
DR RefSeq; WP_011126000.1; NC_005042.1.
DR AlphaFoldDB; Q7V9I2; -.
DR SMR; Q7V9I2; -.
DR STRING; 167539.Pro_1851; -.
DR EnsemblBacteria; AAQ00895; AAQ00895; Pro_1851.
DR GeneID; 54201181; -.
DR KEGG; pma:Pro_1851; -.
DR PATRIC; fig|167539.5.peg.1953; -.
DR eggNOG; COG0404; Bacteria.
DR HOGENOM; CLU_007884_10_2_3; -.
DR OMA; MPVQYPA; -.
DR OrthoDB; 282830at2; -.
DR Proteomes; UP000001420; Chromosome.
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..373
FT /note="Aminomethyltransferase"
FT /id="PRO_0000122583"
SQ SEQUENCE 373 AA; 40918 MW; A555E316E4EAB653 CRC64;
MKSKNTPLYE TCLNEGARMV EFAGWNMPIQ FSGLINEHNA VRKNSGIFDI SHMGVFSIQG
KNPKDALQTL VPSDLHRIGP GEACYTVLLN NDGGIIDDLI VYDLGTNDPN NEECILIVIN
AGCTQADIDW IKEHLSDKNL KVCNAKGDGV LLALQGPDST NQLRNVLGES LTNIPKFGHR
EIQVQLKTHP VSFSIFIART GYTGEDGYEI LLNTNAGKSL WRELIENGVT PCGLGARDTL
RLEAGMPLYG NDINNTTTPF EAGLGWLVHL ETPDEFIGKA ALVKQTNEGI NKKLVALKIE
GRAIARKGYQ IMFKNKFVGE ITSGSWSPTL NEGIALAYLP IDLTKIGTAV SVQIRDKLHT
AIVAKKPFYR RVS