ID B6AUX1_9RHOB Unreviewed; 813 AA.
AC B6AUX1;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Glycine cleavage T-protein (Aminomethyl transferase) {ECO:0000313|EMBL:EDZ41141.1};
GN ORFNames=RB2083_655 {ECO:0000313|EMBL:EDZ41141.1};
OS Rhodobacteraceae bacterium HTCC2083.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=314270 {ECO:0000313|EMBL:EDZ41141.1, ECO:0000313|Proteomes:UP000005746};
RN [1] {ECO:0000313|Proteomes:UP000005746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2083 {ECO:0000313|Proteomes:UP000005746};
RX PubMed=21036993; DOI=10.1128/JB.01268-10;
RA Kang I., Vergin K.L., Oh H.M., Choi A., Giovannoni S.J., Cho J.C.;
RT "Genome sequence of strain HTCC2083, a novel member of the marine clade
RT Roseobacter.";
RL J. Bacteriol. 193:319-320(2011).
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; DS995276; EDZ41141.1; -; Genomic_DNA.
DR AlphaFoldDB; B6AUX1; -.
DR STRING; 314270.RB2083_655; -.
DR eggNOG; COG0404; Bacteria.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_11_0_5; -.
DR OrthoDB; 7156675at2; -.
DR Proteomes; UP000005746; 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; 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:SF193; PYRUVATE DEHYDROGENASE PHOSPHATASE REGULATORY SUBUNIT, 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000005746};
KW Transferase {ECO:0000313|EMBL:EDZ41141.1}.
FT DOMAIN 8..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 428..698
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 723..805
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 813 AA; 89749 MW; 8F18C8AB0874AFD1 CRC64;
MSLPEKARVV IIGGGVIGCS VAYHLAKLGW KDIVLLERKQ LTSGTTWHAA GLIAQLRATK
NMTKLAKYSQ ELYGNLAAET GVETGFKRCG SITVALTDER LEEINRQAAM ARSFGVEAES
ISPAEVKAKY EHLNIDGVVG GVYLPLDGQG DPANIAHALA KGARQNGALV KEGYLVTDIQ
KEGRRVTGVR WEDKNGETGA IEAEHVVNCG GMWGHSIGRM AGVNVPLHAC EHFYIVTEAI
AGLTQMPVLR VPDECAYYKE DAGKMLLGAF EPVSKPWTLD IPKDFEFDQL PEDFDHFEPI
LEAAVERLPM LAEAGIHTFF NGPESFTPDD AYHLGLAPEL DNFWVACGFN SIGIQSAGGA
GSALAQWMDE GDKPFDLGDV DISRMQPFQG NKAYLFERSK ETLGLLYADH FPYLQKRTAR
GVRRTPFHNH LIERGAVMGE LAGWERANWF AREAQEPEYQ YSWQRQNFFD NVREEHMAVR
QGVGMYDMSS FGKIRVEGRD AEAFMNYVGG GDYSVANGKI VYTQFLNRRG GIEADVTVTR
LTEQSYLVVT PAATRLADET WLRRNQGDFE VVITDVTSGE GVLAIMGPRS RELLEAVSPN
DFTNASNPFG TAQEIEIGMG LARAHRVTYV GELGWEIYVS ADMAGHVFER LAEPGLEMGM
RLCGMHMMDT CRIEKGFRHF GHDITSEDHV MEAGLGFAVK KDKANYIGRE AILAKQENGL
DMRLLQFKLS DPEPLLYHAE PVLRDGEIVS YLTSGAYGHH EGAAMGMGYI PCKGEKLADV
LGSTFEIDVA GTRVKAEVSS KPFYDPKSER VKI
//
