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GCST_NATPD
ID   GCST_NATPD              Reviewed;         358 AA.
AC   Q3IN28;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Probable 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=NP_4774A;
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC   2260 / Gabara;
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
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; CR936257; CAI50478.1; -; Genomic_DNA.
DR   RefSeq; WP_011324090.1; NC_007426.1.
DR   AlphaFoldDB; Q3IN28; -.
DR   SMR; Q3IN28; -.
DR   STRING; 348780.NP_4774A; -.
DR   EnsemblBacteria; CAI50478; CAI50478; NP_4774A.
DR   GeneID; 3702746; -.
DR   KEGG; nph:NP_4774A; -.
DR   eggNOG; arCOG00756; Archaea.
DR   HOGENOM; CLU_007884_10_2_2; -.
DR   OMA; MPVQYPA; -.
DR   OrthoDB; 25548at2157; -.
DR   Proteomes; UP000002698; 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..358
FT                   /note="Probable aminomethyltransferase"
FT                   /id="PRO_1000047681"
SQ   SEQUENCE   358 AA;  38159 MW;  0BB8413B93E05142 CRC64;
     MSLRTPPLFD AHTDAGAKLT EFGGWEMPVE FDSIRTEHDA VRESAGKFDI SHMGEIEVSG
     PDAAALTNRL TTNDVASLAP GEATYAGITD DDGVLLDDTV VYRLPDGATY LFVPNAGNDE
     LMAERWRSFA DRWDLAATVD NATDDYAMVA LQGPDALELL SSLDVDVFDL SRFEAAERTV
     AGVDCLVSRT GYTGEDGVEL LFETAAAETV WSALDCQPCG LGARDTLRLE AGFLLGGNEF
     DPETNPRTPY EANIGFAVDL GTEFVGSDAL AAQREAGPDE RLVGLRLQDR GIARHGHDIV
     AAGDVVGEVT SGTMSPTLGA AIALGYVPVE YTEPGTELAV VVRGDEKDAV VEALPFYE
 
 
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