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Database: UniProt
Entry: A0A2I3M6J5_PAPAN
LinkDB: A0A2I3M6J5_PAPAN
Original site: A0A2I3M6J5_PAPAN 
ID   A0A2I3M6J5_PAPAN        Unreviewed;       376 AA.
AC   A0A2I3M6J5;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Aminomethyltransferase {ECO:0000256|RuleBase:RU003981};
DE            EC=2.1.2.10 {ECO:0000256|RuleBase:RU003981};
DE   AltName: Full=Glycine cleavage system T protein {ECO:0000256|RuleBase:RU003981};
GN   Name=AMT {ECO:0000313|Ensembl:ENSPANP00000031274.1};
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000031274.1, ECO:0000313|Proteomes:UP000028761};
RN   [1] {ECO:0000313|Ensembl:ENSPANP00000031274.1, ECO:0000313|Proteomes:UP000028761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA   Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA   Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA   Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA   Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA   Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA   Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA   Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA   Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA   Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA   Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA   Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA   Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA   Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA   Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA   Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA   Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA   Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA   Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA   Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA   Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA   Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA   Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT   "Whole Genome Assembly of Papio anubis.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPANP00000031274.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. {ECO:0000256|ARBA:ARBA00003631,
CC       ECO:0000256|RuleBase:RU003981}.
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,
CC         ECO:0000256|RuleBase:RU003981};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. {ECO:0000256|ARBA:ARBA00011690,
CC       ECO:0000256|RuleBase:RU003981}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|RuleBase:RU003981}.
CC   -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000256|ARBA:ARBA00008609,
CC       ECO:0000256|RuleBase:RU003981}.
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DR   AlphaFoldDB; A0A2I3M6J5; -.
DR   Ensembl; ENSPANT00000047361.2; ENSPANP00000031274.1; ENSPANG00000015012.3.
DR   GeneTree; ENSGT00940000157524; -.
DR   Proteomes; UP000028761; Chromosome 2.
DR   Bgee; ENSPANG00000015012; Expressed in pancreas and 64 other cell types or tissues.
DR   ExpressionAtlas; A0A2I3M6J5; baseline.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
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   InterPro; IPR006223; GCS_T.
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:SF15; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   PIRSF; PIRSF006487; GcvT; 2.
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,
KW   ECO:0000256|RuleBase:RU003981};
KW   Mitochondrion {ECO:0000256|RuleBase:RU003981};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028761};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003981};
KW   Transit peptide {ECO:0000256|RuleBase:RU003981}.
FT   DOMAIN          86..264
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          291..368
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   376 AA;  40950 MW;  6F9C6665B321375F CRC64;
     MQRVVSVVAH LGFRLQALPP ALCRPLSCAQ DVLRRTPLYD FHLAHGGKMV AFAGWSLPVQ
     YRDSHTDSHL HTRQHCSLFD VSHMLQGTLS LFTNEAGGIL DDLIVTNTSE GHLYVVSNAG
     CWEKDLALMQ DKVRELQNQG RDVGLEVLDN ALLALQGPTA AQVLQASVAD DLKKLPFMTS
     AVMEVFGVSG CRVTRCGYTG EDGVEISVPA AEAVHLATAL LKNPEVKLAG LAARDSLRLE
     AGLCLYGNDI DEHTTPVEGS LSWTLGKRRR AAMDFPGAKV IVPQLKGKVQ RRRVGLMCEG
     APMRAHSPIL NMEGTKIGTV TSGCPSPSLK KNVAMGYVPC EYSRPGTMLL VEVRRKQQMA
     VVSKMPFVST NYYTLK
//
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