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Database: UniProt
Entry: A4F1G9_9RHOB
LinkDB: A4F1G9_9RHOB
Original site: A4F1G9_9RHOB 
ID   A4F1G9_9RHOB            Unreviewed;       816 AA.
AC   A4F1G9;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=FAD dependent oxidoreductase/aminomethyl transferase {ECO:0000313|EMBL:EBA14312.1};
GN   ORFNames=RSK20926_09684 {ECO:0000313|EMBL:EBA14312.1};
OS   Roseobacter sp. SK209-2-6.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=388739 {ECO:0000313|EMBL:EBA14312.1, ECO:0000313|Proteomes:UP000005964};
RN   [1] {ECO:0000313|EMBL:EBA14312.1, ECO:0000313|Proteomes:UP000005964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK209-2-6 {ECO:0000313|EMBL:EBA14312.1,
RC   ECO:0000313|Proteomes:UP000005964};
RA   Ward B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2006) 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:EBA14312.1}.
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DR   EMBL; AAYC01000023; EBA14312.1; -; Genomic_DNA.
DR   RefSeq; WP_008210036.1; NZ_AAYC01000023.1.
DR   AlphaFoldDB; A4F1G9; -.
DR   eggNOG; COG0404; Bacteria.
DR   eggNOG; COG0665; Bacteria.
DR   OrthoDB; 7156675at2; -.
DR   Proteomes; UP000005964; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR028896; GCST/YgfZ/DmdA.
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; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000005964};
KW   Transferase {ECO:0000313|EMBL:EBA14312.1}.
FT   DOMAIN          9..370
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          373..427
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          431..701
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          726..808
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   816 AA;  89772 MW;  26D84D58BB845165 CRC64;
     MSELPNKARV VIIGGGVIGC SVAYHLAKLG WKDVVLLERK QLTSGTTWHA AGLIAQLRAT
     ANMTKLAKYS QELYGSLEEE TGVATGFKRC GSITVALTEE RKEEIFRQAA MARAFGVEVE
     EISPEEVKAR YEHLNVGDVT GGVWLPKDGQ GDPANIALAL AKGARQRGAL VKERIKVTDI
     SKTGRRVTGV DWASDDGKSQ GHIEADMVVN CAGMWGHEVG RMAGVNVPLH ACEHFYIVTE
     GITGLTQMPV LRVPDECAYY KEDAGKILLG AFEPNAKPWA MKGIPDSFEF DQLPEDFDHF
     EPILEAACNR MPMLAEAGIH TFFNGPESFT PDDAYHLGLA PEMDNFWVAA GFNSIGIQSA
     GGAGMALAQW MDEGQKPFDL GDVDISRMQP FQGNKHYLFE RSKETLGLLY ADHFPYRQKA
     TARGVRRTPF HHHLLEQGAV MGEIGGWERA NWFANAGQER EYQYSWKRQN WFENSAAEHK
     AVRENVGMYD MSSFGKIRVE GPDAEAFLNY ICGANLSVPT GKIVYTQFLN SRGGIEADVT
     VTRLSETAYL VVTPAVTRLA DQTWMMRHKG DFNVVITDVT AGEGVLAVMG PNARKLLQKV
     SPNDFSNEVN PFGTAQEIEL GMGLARVHRV TYVGELGWEI YVGADMAGHA FETLFEAGQD
     MGLKLCGMHM MDSCRIEKGF RHFGHDITCE DNVIDAGLGF AVKTDKEDFI GKAAVLERKE
     SGPKNRMLQF KLTDAEPLLF HNEPIIRDGK YVGYLSSGNY GHTLGAAIGM GYVPCEGESA
     AEILGSTYEI DVMGTKVKAE ASLKPMYDPK SERVKV
//
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