ID A0A176WBQ4_MARPO Unreviewed; 835 AA.
AC A0A176WBQ4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Aminomethyltransferase, mitochondrial {ECO:0000256|ARBA:ARBA00015825};
DE EC=2.1.2.10 {ECO:0000256|ARBA:ARBA00012616};
DE AltName: Full=Glycine cleavage system T protein {ECO:0000256|ARBA:ARBA00031395};
GN ORFNames=AXG93_1474s1190 {ECO:0000313|EMBL:OAE30073.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE30073.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE30073.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE30073.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|ARBA:ARBA00011690}.
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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:OAE30073.1}.
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DR EMBL; LVLJ01001368; OAE30073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176WBQ4; -.
DR OrthoDB; 5473523at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
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 CDD; cd00038; CAP_ED; 2.
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 Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
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; IPR014710; RmlC-like_jellyroll.
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; PF00027; cNMP_binding; 2.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR PRINTS; PR00103; CAMPKINASE.
DR SMART; SM00100; cNMP; 2.
DR SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR SUPFAM; SSF103025; Folate-binding domain; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 2.
DR PROSITE; PS00889; CNMP_BINDING_2; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 89..210
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 213..328
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 338..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 835 AA; 91657 MW; 2EC59F2408D1DCAA CRC64;
MGSSGGGRDI SMGVADMKLK AKAKSLAGGP IDKNIQIIRQ RDRSKTMSIR RTGVSAEVFT
GDEKFEKKIV EKSEEAKKRI RACFLKSYLL EHLDKEQTET VVEAVEEVRF KENDIIIQQG
EPGEYFYLLE QGAAEVWITK EGETKPIMVK QYTAGDSFGE LALLYNAPRA ATVKATTDCV
LWAVDRNTFR AILMTSTQEK RNLYEEFLKE VPLLKSLDKY ERSAIADVLQ PEYFNPQQVI
IVEGAKGDKF FVLEEGEAEA RSQGKVVMKY KRGDYFGELA LLNDAPRAAT ITALTKCKVV
SIEREQFKRL LGKLEDILHR KKEDYEKVNA AVAVSPEDAP AQLPDLPPGA APSAPSASVS
ETSTVPSSPT KDNVRGRVVL VVVLRLWLVA RIVHLGSSSI GIVSSCRLEE RKGREASGEA
RREEGASMMR RATCQWAASA KQLAERAVAP QLQRRGYADQ STLKKTVLYD FHVENGGKMV
PFAGWSMPIQ YKDSIMDSTT NCRSHGSLFD VSHMCGLSLK GKDAIPFLES LVVADIASLP
NGTGTLSVFT NDKGGVIDDT VITKVTDEHI YMVVNAGCRD KDLEHMENHL KPFQQKGKDV
GWHIHDERSL LAIQGPLAAP TLQKLTNADV SQIYFADFKF LDVNGAACYV TRTGYTGEDG
FEISVPHENA VDLTKAFLEK SDGQIRMTGL GARDSLRLEA GLCLYGNDLE QHITPIEAGL
AWTIGKRRRA EANFPGAQVI LQQLKDGPTK RRVGLSAGGA PARSHAEILD ASGKVIGEVT
SGGYSPCLKK NIAMGYVETG NHKAGTPIQV VVRGRTSAGA ITKMPFVPTT YYKKP
//
