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Database: UniProt
Entry: A0A0Q6F8D8_9ACTN
LinkDB: A0A0Q6F8D8_9ACTN
Original site: A0A0Q6F8D8_9ACTN 
ID   A0A0Q6F8D8_9ACTN        Unreviewed;       840 AA.
AC   A0A0Q6F8D8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Glycine cleavage system protein T {ECO:0000313|EMBL:KQT90716.1};
GN   ORFNames=ASG49_13250 {ECO:0000313|EMBL:KQT90716.1};
OS   Marmoricola sp. Leaf446.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Marmoricola.
OX   NCBI_TaxID=1736379 {ECO:0000313|EMBL:KQT90716.1, ECO:0000313|Proteomes:UP000051542};
RN   [1] {ECO:0000313|EMBL:KQT90716.1, ECO:0000313|Proteomes:UP000051542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf446 {ECO:0000313|EMBL:KQT90716.1,
RC   ECO:0000313|Proteomes:UP000051542};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT90716.1, ECO:0000313|Proteomes:UP000051542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf446 {ECO:0000313|EMBL:KQT90716.1,
RC   ECO:0000313|Proteomes:UP000051542};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQT90716.1}.
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DR   EMBL; LMRF01000005; KQT90716.1; -; Genomic_DNA.
DR   RefSeq; WP_056542647.1; NZ_LMRF01000005.1.
DR   AlphaFoldDB; A0A0Q6F8D8; -.
DR   STRING; 1736379.ASG49_13250; -.
DR   OrthoDB; 2055370at2; -.
DR   Proteomes; UP000051542; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1.
DR   Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR032503; FAO_M.
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; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR13847:SF181; TRANSFERASE CAF17, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16350; FAO_M; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF103025; Folate-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051542}.
FT   DOMAIN          10..373
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          376..431
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          435..712
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          758..823
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   840 AA;  91322 MW;  969A94249DA2E9BD CRC64;
     MATVPSTANV VVIGAGIVGN SLVHHLTRLG WKDVVQLDKG ALPNPGGSTG HASNFIFPVD
     HSREITDLTM DSVRQYQEMG VFTQSGGFEV ARTEERMEEL RRRMSSAKAW GIDSELVTPA
     QVVEKVPFLD PDQIIGAFWT PTVGVVDSLR AGTIMREQAL ATGELTVVAG AEVEDLVVED
     GEHGRRIRSV VTDQGTIEAS YVVIAAGVWS PKLGDMAGVR IALTPAVHQM ISVGPCPQLA
     ETDGEISFPI IRDMDTFCYE RQHGADMEVG SYAHRPILHE PEEIPSIEQA RLSPTEMPFT
     EDDFDQQLEE ALELMPELLG AEGAEIRYAI NGLLSLTADG NPILGESEVK GLWVSAAVWI
     KEGPGVGRAV AEWMTHGHSE IDLHHSDIAR FHPHETTREH VRARTSEAFN KTYGIVHPGE
     QWGSDREVRY SPMADSQKAL GAVFHETVGW ERPFWYDSNA DLLETYGDRV MPREHEWDSR
     WWSPIINAEH LAMREHAGVV DLTAFSIFDI TGPGALASVQ RTCVAQCDVA VGKVVYTPVL
     DAKGGFLSDL TVMRLGEDRF RVVTGGAHGM ADRKHFTDRL VDGAELADVT EEVSTIGIWG
     PKAREVLASL SSDDLSDGGF GFLTSREIDV KGVDAPVLAS RISYVGDLGW ELYVPFSAAA
     SLWDALLTAG REHGVRPVGI GVYGTTGRLE KGYRAFGAEL DAERTIVETG MQRPKVKAAD
     FLGREAYLAQ REAAPAAVLC TLTVDDHTSA SGVKRYMLGG EPILTTDGQL LTDGHGHHSY
     VTSAGSAPSL GKHVLLAFLP PEEATIGNRL AVSYMEELYP VTVGSVDATP LLDPDNERLR
//
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