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Database: UniProt
Entry: Q5LW00_RUEPO
LinkDB: Q5LW00_RUEPO
Original site: Q5LW00_RUEPO 
ID   Q5LW00_RUEPO            Unreviewed;       811 AA.
AC   Q5LW00;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   SubName: Full=Aminomethyl transferase family protein {ECO:0000313|EMBL:AAV93860.1};
GN   OrderedLocusNames=SPO0544 {ECO:0000313|EMBL:AAV93860.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93860.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93860.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., Deboy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93860.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
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DR   EMBL; CP000031; AAV93860.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5LW00; -.
DR   STRING; 246200.SPO0544; -.
DR   PaxDb; 246200-SPO0544; -.
DR   KEGG; sil:SPO0544; -.
DR   eggNOG; COG0404; Bacteria.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_11_0_5; -.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023};
KW   Transferase {ECO:0000313|EMBL:AAV93860.1}.
FT   DOMAIN          5..367
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          370..424
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          427..698
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          723..798
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   811 AA;  88758 MW;  76D5A894B2A60CDF CRC64;
     MKQVRVAVIG GGVVGVSVLY HLARLGWTDC CLLERTQLTA GSTWHAAGLL PLYYPNQTMS
     LINKHSMQLY ARLQAETGQP SGFHQCGQLR LATDHDRLDE YRAYLSFARY LGIDCALITR
     EEAQKLWPLA DLGDVIAALY HPGDGHIAPA DLTQAMATGA RGMGAKIHLN TEATAISRTA
     SGEWLISTPN GDFLAEHVVT ATGNYARQTG AMVGLNVPSI PVMHQYVVTE TIKEFADHNR
     AGRPEMPVLR DDKSRFYLRQ ENDGLILGPY EPNPKSWAIN GVPPGFGAEL MTPDYDSLEP
     FIEGTLRRVS SFAAAGIRTV VNGPIAHTPD AFPLVGPAPG LQNYWLAEGM VAGICYGGGV
     GRYLAEWITE GAPTIDMWPV DPRRFNGHAG KNHTRLKNEE TYGHIFDIHY PNLEMPAARP
     GKTSPCYDRL TRAGAVWGVA GGWERARWFD AEGNRTPETL TFRRSNAFEA IGAECRAIRN
     AVGLIDFTSF AKWEVSGAGA MAFLDRALAN AMPKRDGRVT LAHALDENGR FCAEFTVARL
     AEDRFYICGP AFSEVHDDHV LRSRLRPADA ATLTNVSMGW GCFTVAGPKS RELLSRIVDA
     PLENDSFKWF DLHEGEVGWA TDVRLMRVNY CGELGWELHH PIAFQHHILD QLEQAGADLG
     LRHVGMRALD SLRIEKSYRA VAQELTTQNT LHELGLGRFI ATGKTGFIGA QAVAERVGKE
     SVKLVTLEVD CEAGGVEPAM NQAVRCGDKV IALTTSGAYG HFLGKHLAMA ILPLDHAAEG
     TRLSVEILDE RYDAVVIADS PHDPGNLRPR A
//
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