ID A0A142MEJ2_AMIAI Unreviewed; 825 AA.
AC A0A142MEJ2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=4-methylaminobutanoate oxidase (Formaldehyde-forming) {ECO:0000313|EMBL:MBB3704443.1};
DE EC=1.5.3.19 {ECO:0000313|EMBL:MBB3704443.1};
GN ORFNames=FHS67_000746 {ECO:0000313|EMBL:MBB3704443.1};
OS Aminobacter aminovorans (Chelatobacter heintzii).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Aminobacter.
OX NCBI_TaxID=83263 {ECO:0000313|EMBL:MBB3704443.1, ECO:0000313|Proteomes:UP000577697};
RN [1] {ECO:0000313|EMBL:MBB3704443.1, ECO:0000313|Proteomes:UP000577697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10368 {ECO:0000313|EMBL:MBB3704443.1,
RC ECO:0000313|Proteomes:UP000577697};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) 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:MBB3704443.1}.
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DR EMBL; JACICB010000002; MBB3704443.1; -; Genomic_DNA.
DR RefSeq; WP_067968056.1; NZ_JACICB010000002.1.
DR AlphaFoldDB; A0A142MEJ2; -.
DR OrthoDB; 9804379at2; -.
DR Proteomes; UP000577697; Unassembled WGS sequence.
DR GO; GO:0102317; F:4-methylaminobutyrate oxidase (demethylating) activity; IEA:UniProtKB-EC.
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 Oxidoreductase {ECO:0000313|EMBL:MBB3704443.1}.
FT DOMAIN 10..366
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 369..424
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 426..697
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 724..808
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 825 AA; 90085 MW; 9E19FF179ACD7044 CRC64;
MAQQFPTQAR VVIIGGGIIG CSVAYHLTKL GWTDVVLLEQ GQLSGGTTWH AAGLVGQLRS
HANMTSLIKY STQLYSELEA ETGLATGWKN CGSLSVARSA DRMTVLKRTA ASARAQGVDI
EVISAREAQE KWPVMAIDDL VGAVWLPGDG KANPTDLTQS LAKGARNRGA RVIERVRVTG
IQTKDGRATG VSTDKGDIAA EIVVNCAGQW ARKVGAMCGV TVPLHSAEHM YIVTGKIEGV
HPDLPVLRDP DGYIYFKEEV GGLVMGGFEP EAKPWGMKGI PDDFEFALLP DDWDQFEILM
QNALIRVPQL ETSEVKKFYN GPESFTADNN FILGEAPELK NFYVGAGFNS MGIASAGGAG
RALAEWIVNG AATMDLWPVD IRRFAGFNNN PRWLHDRVKE TLGLHYAMPW PNRELDTARP
FRRSALYDRL AAKGACFGSK MGWERANWFA AQGEKPETQY AFGKQNWHEA VKREMKATRE
ASGIFDQTSF AKILVQGRDA ARVLNRICAA DIDVEIGRSI YTGLLNERGG YESDLTVMRL
GRDKFLLVTG SAQAVHDADW ISKNVPEDAH VTLTDVTSSY AVLALMGPRS RDILTKLTSA
DLSNTGFPFA TIREIDIGYA TAYANRMTYV GELGWELIVP TEFAIGVYEA LHEAGRVHGL
ADCGYYALEA LRIEKGFRAW SRELTPDITP YEAGLAFAVS MDKPDGFIGK EALVAAKAKG
KLTRRIVQFT VDDAAPMLWG GELILRDGKP VGEVRSAAYG HTLGRSVALG LLHNEAGIDK
DFIESGRFEI DLAGERYTAT AHLKAPYDPK SERVKADSTE LHEAA
//
