ID A0A1I3GVL8_9BURK Unreviewed; 826 AA.
AC A0A1I3GVL8;
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:SFI27615.1};
GN ORFNames=SAMN05192543_102718 {ECO:0000313|EMBL:SFI27615.1};
OS Paraburkholderia megapolitana.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=420953 {ECO:0000313|EMBL:SFI27615.1, ECO:0000313|Proteomes:UP000199548};
RN [1] {ECO:0000313|EMBL:SFI27615.1, ECO:0000313|Proteomes:UP000199548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 23650 {ECO:0000313|EMBL:SFI27615.1,
RC ECO:0000313|Proteomes:UP000199548};
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; FOQU01000002; SFI27615.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3GVL8; -.
DR STRING; 420953.SAMN05192543_102718; -.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000199548; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000199548}.
FT DOMAIN 10..375
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 379..433
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 435..707
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 732..818
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 826 AA; 90772 MW; 4EFE61178D84E680 CRC64;
MSTNIPRHAR VVIVGGGIIG CSVAYHLTKL GWTDVVLLEQ GQLSCGTTWH AAGLVGQLRA
QESMTKLIRY STALYAELEA DTGLATGWKQ CGSLSVARTA ERMTQLKRTA AVARAYGVAC
DVIGPKEAGD LWPVMRTDDL LGAVWLPGDG KANPTDLTQA LARGARTRGA RIVENTRVTA
IHTRQAEAGR EVSGLAWRNK DGEEGTIAAE IVVNCAGQWA KAIGRMCDVT VPLHSAEHYY
IVTERIAGVH PDLPVMRDPD GYIYFKEEVG GLVMGGFEPN AKPWGMNGIP ENFEFQLLPD
DWDQFQILME NALQRVPALE TAQVKQFYNG PESFTPDNNF ILGEAPELRR FFVGAGFNSM
GIASAGGAGM ALAEWIVAGS PTMDLWPVDI RRFARFNGND TWLHDRVKET LGLHYAMPWP
NRELDTARPF RRSPLYTLLR DEGAYFGSKM GWERPNFFAP SPAEARVEYG FGQQNWLPWS
GAEHRACREG VALFDMTSFS KLLVKGRDAE AVLQGIVAND VAVPVGTTVY TGMLNERGNY
ESDFTLTRLA DDQYLIVTGS AQTTRDFDYI EKSIPHDKHC TLVDVTGQYA VLAVMGPRAR
DLLQSVSKAD WSPAAFPFGQ SREVDIGYAT VRATRLTYVG ELGWELYVPV EFAAGVYETL
HAAGKPFGLV NAGYYAIDSL RIEKGYRAWG RELTPDYNPF EAGLSFACKL NKDIPFRGRE
ALLKLRDEPL RRRMVVLTVD GASDRMVWGS EAILRDGKPV GFVTSAAFGH TLGCPVAMGY
ISNPDGVADA SYLNSGHYTI DLAGELLPAT VHLKAPYDPR SERVKS
//
