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
//