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Database: UniProt
Entry: F8D710_HALXS
LinkDB: F8D710_HALXS
Original site: F8D710_HALXS 
ID   F8D710_HALXS            Unreviewed;       383 AA.
AC   F8D710;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Probable aminomethyltransferase {ECO:0000256|HAMAP-Rule:MF_00259};
DE            EC=2.1.2.10 {ECO:0000256|HAMAP-Rule:MF_00259};
DE   AltName: Full=Glycine cleavage system T protein {ECO:0000256|HAMAP-Rule:MF_00259};
GN   Name=gcvT {ECO:0000256|HAMAP-Rule:MF_00259};
GN   OrderedLocusNames=Halxa_0800 {ECO:0000313|EMBL:AEH35439.1};
OS   Halopiger xanaduensis (strain DSM 18323 / JCM 14033 / SH-6).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Halopiger.
OX   NCBI_TaxID=797210 {ECO:0000313|EMBL:AEH35439.1, ECO:0000313|Proteomes:UP000006794};
RN   [1] {ECO:0000313|EMBL:AEH35439.1, ECO:0000313|Proteomes:UP000006794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18323 / JCM 14033 / SH-6
RC   {ECO:0000313|Proteomes:UP000006794};
RX   PubMed=22675596; DOI=10.4056/sigs.2505605;
RA   Anderson I., Tindall B.J., Rohde M., Lucas S., Han J., Lapidus A.,
RA   Cheng J.F., Goodwin L., Pitluck S., Peters L., Pati A., Mikhailova N.,
RA   Pagani I., Teshima H., Han C., Tapia R., Land M., Woyke T., Klenk H.P.,
RA   Kyrpides N., Ivanova N.;
RT   "Complete genome sequence of Halopiger xanaduensis type strain (SH-6(T)).";
RL   Stand. Genomic Sci. 6:31-42(2012).
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. {ECO:0000256|HAMAP-Rule:MF_00259}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + N(6)-[(R)-S(8)-
CC         aminomethyldihydrolipoyl]-L-lysyl-[protein] = (6R)-5,10-
CC         methylene-5,6,7,8-tetrahydrofolate + N(6)-[(R)-dihydrolipoyl]-L-
CC         lysyl-[protein] + NH4(+); Xref=Rhea:RHEA:16945, Rhea:RHEA-COMP:10475,
CC         Rhea:RHEA-COMP:10492, ChEBI:CHEBI:15636, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57453, ChEBI:CHEBI:83100, ChEBI:CHEBI:83143; EC=2.1.2.10;
CC         Evidence={ECO:0000256|ARBA:ARBA00043710, ECO:0000256|HAMAP-
CC         Rule:MF_00259};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. {ECO:0000256|HAMAP-Rule:MF_00259}.
CC   -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000256|ARBA:ARBA00008609,
CC       ECO:0000256|HAMAP-Rule:MF_00259}.
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DR   EMBL; CP002839; AEH35439.1; -; Genomic_DNA.
DR   RefSeq; WP_013878339.1; NC_015666.1.
DR   AlphaFoldDB; F8D710; -.
DR   STRING; 797210.Halxa_0800; -.
DR   GeneID; 10795776; -.
DR   KEGG; hxa:Halxa_0800; -.
DR   eggNOG; arCOG00756; Archaea.
DR   HOGENOM; CLU_007884_10_2_2; -.
DR   OrthoDB; 2001at2157; -.
DR   Proteomes; UP000006794; Chromosome.
DR   GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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   NCBIfam; TIGR00528; gcvT; 1.
DR   PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   PIRSF; PIRSF006487; GcvT; 1.
DR   SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR   SUPFAM; SSF103025; Folate-binding domain; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW   Rule:MF_00259}; Methyltransferase {ECO:0000313|EMBL:AEH35439.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006794};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00259}.
FT   DOMAIN          10..278
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          304..381
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   383 AA;  41888 MW;  E8F0296289E4756F CRC64;
     MPLQTPPLRG THDERGAKFT EFGGWDMPVE FDSIRTEHAA VREDVGIFDV SHMGQIHVTG
     PDATELMQRL TTNDVSRLGV GDAQYAAITD EDGTIIDDTV IYRLPDEGET PQGSREDGEA
     TYLFIPNAGT DESTHERWIG YRNEWDLEAT VDNRTDEYAM FAVQGPNAAD LVGDVVDVAD
     TADAIDGSVT DLSRFEATES TIDGVDCWTA RTGYTGEDGF ELIVPWPEAE RIWSAFDCQP
     CGLGARDTLR IEAGLLLAGQ DFDPEDNPRT PYEAGIGFTV DLETEFVGRD ALAQVRAEGV
     EEELVGFQLI DRGVPRHGYD ITNPESRVIG TVTSGTMSPT LEQAIGLGYV PVEYADPGTT
     LQVVVRGQSK KARVEQTPFI DTQ
//
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