ID H5U497_9ACTN Unreviewed; 818 AA.
AC H5U497;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Putative dimethylglycine oxidase {ECO:0000313|EMBL:GAB40555.1};
GN ORFNames=GOSPT_109_00080 {ECO:0000313|EMBL:GAB40555.1};
OS Gordonia sputi NBRC 100414.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1089453 {ECO:0000313|EMBL:GAB40555.1, ECO:0000313|Proteomes:UP000005845};
RN [1] {ECO:0000313|EMBL:GAB40555.1, ECO:0000313|Proteomes:UP000005845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100414 {ECO:0000313|EMBL:GAB40555.1,
RC ECO:0000313|Proteomes:UP000005845};
RA Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Gordonia sputi NBRC 100414.";
RL Submitted (FEB-2012) 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:GAB40555.1}.
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DR EMBL; BAFC01000107; GAB40555.1; -; Genomic_DNA.
DR RefSeq; WP_005207627.1; NZ_BAFC01000107.1.
DR AlphaFoldDB; H5U497; -.
DR eggNOG; COG0404; Bacteria.
DR eggNOG; COG0665; Bacteria.
DR Proteomes; UP000005845; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase 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; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR13847:SF181; TRANSFERASE CAF17, MITOCHONDRIAL-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;
FT DOMAIN 5..372
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 375..430
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 432..710
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 733..810
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 818 AA; 88995 MW; DF8B06AB19068AA1 CRC64;
MPTPKVVIVG AGIVGTSLAD ELTARGWTDV TVLDRGPLFA TGGSTSHAPG LVFATNPSKT
MTELASYTLE KFSTLEHPDG WCFSHLGGLE VATTEARLDD LHRKAGWAAS RGVEHELLSP
AECLERHPLL DPDQIVGGFF TPRDGLAKAL RAAEAQATRA ISRGARFVPH TEVIDVVECN
GEVRGVRTAT GVVDADIVVC CTGFWGREFG RRVGLTIPLV PMAHQYAYTT PLESRHGANS
VVAEASLPIL RHQDHDLYYR EHGDRLGIGY YGHRPMPSDV NALDYDSTVS LEEMPSKLMF
TPDDFAEAWD QTITLIPELA TGKVDDGFNG IFSFTPDGHS VVGEHRGLKG FWVAEAVWVT
HSAGIARTVA EWMVDGAPSV DTHEFDLYRF ENAALTDDYI LTTSSQSFVE VYDIIHPHDQ
VAAPRGVRTS PFYDRQAALG AEFWVANLWE RPAWFEANQP ILDELVAGGL QIPLRDAWSA
RNWSPISVAE AAWTRSHVAM YDMTPLTRYE VSGPGAADFL QRMTTNNVDK SIGSITYTLM
LDDEGGVRSD LTVARLGADL FQVGANGPID FDWLSRHLPA DRSVTLRDIT GATCCIGLWG
PSARDVVAPL TPTGLTNDGL KYFRCVQTTI GSVPVTLMRV SYVGELGWEI YADAEYGRGL
WDLLMAAGAE HRIIAAGRIA FNALRIEKGY RSAGVDMTTE HTPDAAGLSF AVKSSKPEFV
GKNALDQRVC PLRLRTLKFD DPAAVVLGKE PVRVDGDVVG YVTSAGWSPT VGACLAYAWL
PSDLPDSTAV AVDYLRTSYG ALVISDPVVD PEMARIKQ
//