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Database: UniProt
Entry: A0A0B4BJY2_9RHOB
LinkDB: A0A0B4BJY2_9RHOB
Original site: A0A0B4BJY2_9RHOB 
ID   A0A0B4BJY2_9RHOB        Unreviewed;       819 AA.
AC   A0A0B4BJY2;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Glycine cleavage system protein T {ECO:0000313|EMBL:KIC16898.1};
GN   ORFNames=RA20_15875 {ECO:0000313|EMBL:KIC16898.1};
OS   Leisingera sp. ANG-Vp.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Leisingera.
OX   NCBI_TaxID=1577896 {ECO:0000313|EMBL:KIC16898.1, ECO:0000313|Proteomes:UP000031177};
RN   [1] {ECO:0000313|Proteomes:UP000031177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANG-Vp {ECO:0000313|Proteomes:UP000031177};
RX   PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA   Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT   "Comparative genomics of Roseobacter clade bacteria isolated from the
RT   accessory nidamental gland of Euprymna scolopes.";
RL   Front. Microbiol. 6:123-123(2015).
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:KIC16898.1}.
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DR   EMBL; JWLD01000047; KIC16898.1; -; Genomic_DNA.
DR   RefSeq; WP_039130849.1; NZ_JWLD01000047.1.
DR   AlphaFoldDB; A0A0B4BJY2; -.
DR   STRING; 1577896.RA20_15875; -.
DR   OrthoDB; 9804379at2; -.
DR   Proteomes; UP000031177; 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:SF187; DIMETHYLGLYCINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-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;
FT   DOMAIN          11..373
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          376..428
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          432..698
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          728..803
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   819 AA;  90355 MW;  E2F5C05D7949002C CRC64;
     MADKEFPAQA KVVIVGGGVM GVGLAYHLAH EGWGPEVVLL EKSELTSGST WHAAGQITHS
     TSSFGLGKCV DYNIGLYSGK LEEETGQAVT WHGCGSFRLA YTEDEMDWLR HTLSVGRSLG
     FNIELVGPEK VAELHPFYNL EGVLGALYTP DDGHVDPTNV TMAMAAGARQ KGARIIRHCR
     ATNITQADNG EWIVASEKGT IRCEHVVNAG GTYARQMGEW SGLQLPMTSM THHYFVTEPV
     PEFEALDKEL PVIRDDKKVS GYIRMEQKRG LIGIYEKEGS NSVWHDHCPW EYENWLFDAD
     YDRVMPWLEE SLNRMPIFAD LGIQREVHGA ISHPPDGNPL IGPAPGVRNY WCCCGTQIGI
     GWGPGLTREL ARWMVHGSAD ISMREYDPRR FGSYATKDWQ VTKAHEDYKL RHEIPFPHFN
     RLAGRPIKPS PLYERLKEKG AVYEEVYGHE RPRWFAKNGV AQQDHYSFRR NEVHDMVGLE
     CKAVREGVGI MDISAFTKVE VSGPGAAALL DRLTANRLPQ KTGGIALTHM LNRRGRIELE
     TTVVKLADDS YYLVCAAFFE QRLLDHLNQN LAGEEVEITT LSTDWAALAL NGPKAREVLA
     ACTDADLTNA GFKWLTAQQI EVAGHTLWAF RMSYAGELGW ELHIPRGSTL AVYDALWAAG
     EAHGIADYGS FAMNAMRMEK GFKGAGELTN EVTLAEADVL RFARTDKNYL GKDKTLNDAE
     KPWVCAYLEI EPDGVEDGHG GEAILLEGQV VGSTASVAYG HTVGKILAFA YVKPHANVPG
     TEIEVIVAGS PRKGRILGAP AYDPESLLPR TDAALAPAE
//
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