GCST_HALMA
ID GCST_HALMA Reviewed; 363 AA.
AC Q5V230;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 25-MAY-2022, entry version 83.
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}; Synonyms=gcvT2;
GN OrderedLocusNames=rrnAC1500;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV46422.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY596297; AAV46422.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011223662.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5V230; -.
DR SMR; Q5V230; -.
DR STRING; 272569.rrnAC1500; -.
DR EnsemblBacteria; AAV46422; AAV46422; rrnAC1500.
DR GeneID; 40152463; -.
DR KEGG; hma:rrnAC1500; -.
DR PATRIC; fig|272569.17.peg.2190; -.
DR eggNOG; arCOG00756; Archaea.
DR HOGENOM; CLU_007884_10_2_2; -.
DR Proteomes; UP000001169; Chromosome I.
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..363
FT /note="Probable aminomethyltransferase"
FT /id="PRO_0000122621"
SQ SEQUENCE 363 AA; 39071 MW; 25D6209AF6CD9EE4 CRC64;
MTLRAPPLSA IHERADASFT DFGGWEMPVE FESIRIEHEA VRSEAGKFDV SHMGQITVAG
PDAATLTQRL TTNDVTVLDP GEAQYGAITD EDGIMLDDTV VYRLPEGAAD EFLFIPNAGH
DGEMTERWLS ERDERGLDAT VTNRTEEYAM IAVQGPDAPD LLSAETDVSL TALSRFEVAA
GAVAGVDSLI ARTGYTGEPG FEILCPPDDA GVVWDALECQ PCGLGARDTL RLEMGFLLSG
QEFHPVDEPR TPYEAGIGWT VKLDTEFVAR DALEGVAADG PEEKLIGIEL VDRGVPRHGY
DVTTPDGEPI GHITSGTMSP TLGAPIALAY VPSAYAEPDK SVRVVVRGEP KKARTRSTPF
LDR