ID A0A0B0HDW2_SOVGS Unreviewed; 363 AA.
AC A0A0B0HDW2;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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 ECO:0000313|EMBL:OOY35846.1};
GN ORFNames=BOV88_02025 {ECO:0000313|EMBL:OOY35846.1}, JV46_21380
GN {ECO:0000313|EMBL:KHF26119.1};
OS Solemya velum gill symbiont.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=2340 {ECO:0000313|EMBL:KHF26119.1, ECO:0000313|Proteomes:UP000030856};
RN [1] {ECO:0000313|EMBL:KHF26119.1, ECO:0000313|Proteomes:UP000030856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH {ECO:0000313|EMBL:KHF26119.1,
RC ECO:0000313|Proteomes:UP000030856};
RX PubMed=25342549; DOI=10.1186/1471-2164-15-924;
RA Dmytrenko O., Russell S.L., Loo W.T., Fontanez K.M., Liao L., Roeselers G.,
RA Sharma R., Stewart F.J., Newton I.L., Woyke T., Wu D., Lang J.M.,
RA Eisen J.A., Cavanaugh C.M.;
RT "The genome of the intracellular bacterium of the coastal bivalve, Solemya
RT velum: a blueprint for thriving in and out of symbiosis.";
RL BMC Genomics 15:924-924(2014).
RN [2] {ECO:0000313|EMBL:OOY35846.1, ECO:0000313|Proteomes:UP000190962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MA-KB16 {ECO:0000313|EMBL:OOY35846.1};
RA Russell S.L., Corbett-Detig R.B., Cavanaugh C.M.;
RT "Mixed transmission modes and dynamic genome evolution in an obligate
RT animal-bacterial symbiosis.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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:KHF26119.1}.
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DR EMBL; JRAA01000001; KHF26119.1; -; Genomic_DNA.
DR EMBL; MPNX01000002; OOY35846.1; -; Genomic_DNA.
DR RefSeq; WP_043115848.1; NZ_MPRY01000009.1.
DR AlphaFoldDB; A0A0B0HDW2; -.
DR STRING; 2340.JV46_21380; -.
DR GeneID; 67403556; -.
DR PATRIC; fig|2340.3.peg.630; -.
DR eggNOG; COG0404; Bacteria.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000030856; Unassembled WGS sequence.
DR Proteomes; UP000190962; Unassembled WGS sequence.
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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000030856};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00259}.
FT DOMAIN 7..254
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 280..353
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 363 AA; 40103 MW; 3DAB68561674DF4E CRC64;
MDQKTILNES HRAMGARMVP FGGWDMPVNY GSQIEEHHAV RQDAGMFDVS HMLVIDIKGS
DSTHFLRHLI ANDVARLKES GKALYSCMLN EQGGVIDDLI VYYLDDTWFR MVVNAGTADK
DLGWIIGQSS GFDIEVAPRR DLAMIAVQGP NAVAKTLPLL NDEIRDSAGT LKPFHATWDS
SWFIGRTGYT GEDGFEIILP ENDATDFWQQ LADAGVRPCG LGSRDTLRLE AGMNLYGSDM
DEETSPLEAG LKWTIALEPA ERDFVGRQAL EAKLAEGNLK TFVGLVLEGR GILRDHLPLF
DGDKQIGEIT SGGFSPTLER SIAYARVDAD APEQFEVEIR GKRLPVRKTK ISFVRNGKAC
VDL
//
