ID A0A1I0RWG3_9RHOB Unreviewed; 814 AA.
AC A0A1I0RWG3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=4-methylaminobutanoate oxidase (Formaldehyde-forming) {ECO:0000313|EMBL:SEW45868.1};
GN ORFNames=SAMN04488515_3400 {ECO:0000313|EMBL:SEW45868.1};
OS Cognatiyoonia koreensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Cognatiyoonia.
OX NCBI_TaxID=364200 {ECO:0000313|EMBL:SEW45868.1, ECO:0000313|Proteomes:UP000199167};
RN [1] {ECO:0000313|EMBL:SEW45868.1, ECO:0000313|Proteomes:UP000199167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17925 {ECO:0000313|EMBL:SEW45868.1,
RC ECO:0000313|Proteomes:UP000199167};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; FOIZ01000002; SEW45868.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0RWG3; -.
DR STRING; 364200.SAMN04488515_3400; -.
DR OrthoDB; 7156675at2; -.
DR Proteomes; UP000199167; 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: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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000199167}.
FT DOMAIN 9..368
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 371..425
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 429..699
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 724..806
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 814 AA; 89578 MW; F3F40376D0DF9EB9 CRC64;
MASVPSAARV VIIGGGVIGC SVAYHLSKLG WKDVVLLERK QLTSGTTWHA AGLIAQLRAT
ANMTKLAKYS QELYGNLEDE TGVATGFKRV GSITVALTAE RKEEIFRQAG MARAFGVEVE
EISPDEVKQR YEHLNIDGVT AGVYLPLDGQ GDPANIALAL AKGARQNGAQ VIEKTLVTGV
KRDGRCITGV DWEQGAETGH IACDMVVNCG GMWGHQVGKM LGVNVPLHAC EHFYIVTEAI
PGLTQMPVLR VPDECAYYKE DAGKMLLGAF EPNAKPWAMD GIPKNFEFDQ LPEDFDHFEP
ILEAACERLP MLAEAGIHTF FNGPESFTPD DAYHLGQAPE MDNVWVAAGF NSIGIQSAGG
AGMALAQWME TGEKPFDLGD VDISRMQPFQ GNKTYLFERS KETLGLLYAD HFPFRQKATA
RGIRRTPFHH HLFERGAVMG ELGGWERANW FARDGQEPEY QYSWQRQNFF ENVRDEHLAV
RQNVGMYDMS SFGKIRVEGR DATDFMNHVG GGQYDVPIGK IVYTQFLNRE GGIEADVTVT
RLSETAYLVV TPAATRLADE TWMRRNTGDF NVVITDVTAG EGVLAVMGPN SRALLQAVSP
NDFSNDTNPF GTAQEIEIGM GLARVHRVTY VGELGWEVYV PSDQCGHVFE TLAVAGQDFD
LKFCGMHMMD TCRMEKGFRH FGHDITSEDH VLEAGLGFAV KTDKPDFIGR DAVLKRKEEG
LRSRLVQFKL TDPEPLLYHN EPILRDGAYV GHLTSGGYAH HLGTAIGMGY VPCPAETVAD
LLASSFEIDV MGTRVKAEAQ LKPFYDPTGE RAKA
//
