ID A0A063Y628_9GAMM Unreviewed; 368 AA.
AC A0A063Y628;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Aminomethyltransferase {ECO:0000256|ARBA:ARBA00012616, ECO:0000256|HAMAP-Rule:MF_00259};
DE EC=2.1.2.10 {ECO:0000256|ARBA:ARBA00012616, ECO:0000256|HAMAP-Rule:MF_00259};
DE AltName: Full=Glycine cleavage system T protein {ECO:0000256|ARBA:ARBA00031395, ECO:0000256|HAMAP-Rule:MF_00259};
GN Name=gcvT {ECO:0000256|HAMAP-Rule:MF_00259};
GN ORFNames=ADINL_0419 {ECO:0000313|EMBL:KDE41114.1};
OS Nitrincola lacisaponensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Nitrincola.
OX NCBI_TaxID=267850 {ECO:0000313|EMBL:KDE41114.1, ECO:0000313|Proteomes:UP000027318};
RN [1] {ECO:0000313|EMBL:KDE41114.1, ECO:0000313|Proteomes:UP000027318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4CA {ECO:0000313|EMBL:KDE41114.1,
RC ECO:0000313|Proteomes:UP000027318};
RX PubMed=16280482; DOI=10.1099/ijs.0.63647-0;
RA Dimitriu P.A., Shukla S.K., Conradt J., Marquez M.C., Ventosa A.,
RA Maglia A., Peyton B.M., Pinkart H.C., Mormile M.R.;
RT "Nitrincola lacisaponensis gen. nov., sp. nov., a novel alkaliphilic
RT bacterium isolated from an alkaline, saline lake.";
RL Int. J. Syst. Evol. Microbiol. 55:2273-2278(2005).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KDE41114.1}.
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DR EMBL; JMSZ01000010; KDE41114.1; -; Genomic_DNA.
DR RefSeq; WP_036543457.1; NZ_JMSZ01000010.1.
DR AlphaFoldDB; A0A063Y628; -.
DR STRING; 267850.ADINL_0419; -.
DR PATRIC; fig|267850.7.peg.416; -.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000027318; Unassembled WGS sequence.
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 Gene3D; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 4.10.1250.10; Aminomethyltransferase fragment; 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 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:KDE41114.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027318};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00259}.
FT DOMAIN 7..259
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 286..360
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 368 AA; 40346 MW; 2AAB25A458F8CBE1 CRC64;
MGNKTVLYPQ HLAMGAKIVD FGGWDMPLHY GSQVEEHHRV RRESGMFDVS HMTVVDITGS
DAREYLRRLL CNDVARLKQK GKALYSGMLN EQGGVIDDLI VYLMTEPDVS GEWYRVVVNC
ATREKDLRWM SDQVMKMDVA LTEQPDLAMI AIQGPEALQR VKSVVSPYRQ SLIDGLAIFQ
GQESEGWFIA RTGYTGEDGL EIMLPEEEAE AFWQVLAEAG VAPCGLGARD TLRLEAGMNL
YGQDMDETVS PLVSNMGWVV AWEPSDRFFV GRAPLEAERA AGPASKLVGL AMETGKGVLR
HGQSVIVDDA VAGEITSGGF SPTLGYAVAL ARVSSATGAE AEVEMRGKRV SVRVVRPPFV
RQGQKVYS
//
