GCST_CUPNH
ID GCST_CUPNH Reviewed; 375 AA.
AC Q0K5P5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=H16_A3619;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
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; AM260479; CAJ94676.1; -; Genomic_DNA.
DR RefSeq; WP_011616220.1; NZ_CP039287.1.
DR AlphaFoldDB; Q0K5P5; -.
DR SMR; Q0K5P5; -.
DR STRING; 381666.H16_A3619; -.
DR EnsemblBacteria; CAJ94676; CAJ94676; H16_A3619.
DR GeneID; 57645751; -.
DR KEGG; reh:H16_A3619; -.
DR PATRIC; fig|381666.6.peg.4007; -.
DR eggNOG; COG0404; Bacteria.
DR HOGENOM; CLU_007884_10_2_4; -.
DR OMA; MPVQYPA; -.
DR OrthoDB; 282830at2; -.
DR Proteomes; UP000008210; Chromosome 1.
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..375
FT /note="Aminomethyltransferase"
FT /id="PRO_1000114105"
SQ SEQUENCE 375 AA; 40103 MW; 48729C2D77BEB921 CRC64;
MTLQATPLNA IHRALGARMV DFGGWDMPVN YGSQIEEHNA VRTDAGMFDV SHMCVVDLAG
ANTRSFLRGL LANNVDKLQT PGKALYSCML DEKGGVIDDL IVYFFAEDRF RLVVNASTAL
GDIEWIRARN AATGSDVTIT PRREDVAPAG VQPLAIVAVQ GPNARTKVWS TFPSTQPSDT
LKPFNAAVVQ DPALGEIMVA RTGYTGEDGF ELVVPAENVA AIWEKLNAAG VRPAGLGARD
TLRLEAGMNL YGQDMDINTS PLDAGLAWTV DLQSERDFTG KAALAAAGSR QQFLGLILRD
KGGVLRAHQK VITPAGDGEI TSGTFSPSLS QSIAFARLPK DVAVGDTVQV EIRDRKLNAT
VVKLPFVRNG KALVS