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Database: UniProt
Entry: A0A0L6CWW2_9RHOB
LinkDB: A0A0L6CWW2_9RHOB
Original site: A0A0L6CWW2_9RHOB 
ID   A0A0L6CWW2_9RHOB        Unreviewed;      1002 AA.
AC   A0A0L6CWW2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Aminomethyltransferase {ECO:0000313|EMBL:KNX41938.1};
DE            EC=2.1.2.10 {ECO:0000313|EMBL:KNX41938.1};
GN   Name=gcvT_3 {ECO:0000313|EMBL:KNX41938.1};
GN   ORFNames=ROTO_15400 {ECO:0000313|EMBL:KNX41938.1};
OS   Roseovarius tolerans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=74031 {ECO:0000313|EMBL:KNX41938.1, ECO:0000313|Proteomes:UP000037046};
RN   [1] {ECO:0000313|Proteomes:UP000037046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EL-164 {ECO:0000313|Proteomes:UP000037046};
RA   Voget S., Bruns H., Wagner-Doebler I., Schulz S., Daniel R.;
RT   "Draft Genome Sequence of Roseovarius tolerans EL-164, a producer of N-
RT   Acylated Alanine Methyl Esters (NAMEs).";
RL   Submitted (JUL-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:KNX41938.1}.
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DR   EMBL; LGVV01000015; KNX41938.1; -; Genomic_DNA.
DR   RefSeq; WP_050662445.1; NZ_LGVV01000015.1.
DR   AlphaFoldDB; A0A0L6CWW2; -.
DR   STRING; 74031.SAMN04488077_101262; -.
DR   PATRIC; fig|74031.6.peg.1572; -.
DR   OrthoDB; 5287468at2; -.
DR   Proteomes; UP000037046; Unassembled WGS sequence.
DR   GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008115; F:sarcosine oxidase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0046653; P:tetrahydrofolate metabolic process; IEA:InterPro.
DR   Gene3D; 3.10.20.440; 2Fe-2S iron-sulphur cluster binding domain, sarcosine oxidase, alpha subunit, N-terminal domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR042204; 2Fe-2S-bd_N.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
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; IPR006277; Sarcosine_oxidase_asu.
DR   InterPro; IPR041117; SoxA_A3.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   NCBIfam; TIGR01372; soxA; 1.
DR   PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF12831; FAD_oxidored; 1.
DR   Pfam; PF13510; Fer2_4; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   Pfam; PF17806; SO_alpha_A3; 1.
DR   PIRSF; PIRSF037980; SoxA; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF103025; Folate-binding domain; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000313|EMBL:KNX41938.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037046};
KW   Transferase {ECO:0000313|EMBL:KNX41938.1}.
FT   DOMAIN          521..603
FT                   /note="SoxA A3"
FT                   /evidence="ECO:0000259|Pfam:PF17806"
FT   DOMAIN          618..883
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          909..994
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
FT   REGION          482..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1002 AA;  108584 MW;  0C8932873CB4A6D8 CRC64;
     MSTRLAKTGR LVDHSRAIEF TFNGKRLKGH PGDTLASALL ANDQMLVGRS FKYHRPRGIV
     ASGAEEPNAL VGLGEGTRFE PNQRVTTTEL FDGLTCISQN HWPSLDFDIG AVNTHLSRFL
     PAGFYYKMFI HPRPFWKHVY EPFIRQSAGL GKASNPGDPD RYEHFYYFCD VLVVGGGVAG
     LQAAVTAAEA GSKVMLIEQT AHWGGRSPVD GGEVDGQPVA EWVDATIAKL QGMPNVTLRN
     RCMGAGVYDH GYALGYERVA DHTPGSDAPR HRLWRIRAGQ IVTATGAIER PLSFAGNDIP
     GVMLASAVRD YAVDFGVSIG DRTVVVTNND DAYRTAITLK KLGLEIPVIL DARQRGGGAL
     AEEARRLGIR VENGKGIAKV KGGKRVTGVA ICAQAGEGAV LEEIACDAVA MSGGWSPVVH
     LWSHCGGKLI WDEASAHFRP DPDQPPKGAK GEGFVIPAGV ANGAGDLASV VSDAHAAGQV
     AAKAMGGKPK GKAPKASTSE EAPMQPVWLM PQGAGIKLRM KSWLDYQNDV KVSDVQLAAR
     EGYESVEHAK RYTTLGMATD QGKLSNINGL AILSDALNQP IPQTGTTTFR PPYTPISLSS
     IAGEAKGEIF QPIRKTPMHA WHEANGADFE PVGQWRRPYC FPKGEEGRHE AVNREIKQTR
     ASLALLDAST LGKIIVKGAD AGRFMDMLYT NMMSTLKPGR CRYGLMCNEN GFLMDDGVVA
     RLDEDTFLVH TTTGGAESIH GHMEDWLQCE WWDWKVYTAN VTEQYAQVGV AGPNSRKVIE
     KLTGDDISAD ALTFMGWTEI TVAGIPARVF RISFAGELSF ELSVPASHGR ALWDALLEAG
     EEYGVMPYGT EAMHVMRAEK GFIMIGDETD GTVIPQDLNM DWAISKKKDD YLGKRAQERE
     HMADPNRWKL VGLETLEGEV LPDGAYATAP GTNANGQRNT QGRVTSTYHS PTLGRGIAMG
     LVHHGLDRMG EVLEFPKVDG GIVKAKIVDP IFYDKDGEKQ NV
//
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