ID A0A1H4HIB9_9BURK Unreviewed; 827 AA.
AC A0A1H4HIB9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=4-methylaminobutanoate oxidase (Formaldehyde-forming) {ECO:0000313|EMBL:SEB21421.1};
GN ORFNames=SAMN05192564_10998 {ECO:0000313|EMBL:SEB21421.1};
OS Paraburkholderia sartisoli.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=83784 {ECO:0000313|EMBL:SEB21421.1, ECO:0000313|Proteomes:UP000198638};
RN [1] {ECO:0000313|EMBL:SEB21421.1, ECO:0000313|Proteomes:UP000198638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24000 {ECO:0000313|EMBL:SEB21421.1,
RC ECO:0000313|Proteomes:UP000198638};
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; FNRQ01000009; SEB21421.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4HIB9; -.
DR STRING; 83784.SAMN05192564_10998; -.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000198638; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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:UP000198638}.
FT DOMAIN 10..376
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 380..434
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 436..708
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 733..819
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 827 AA; 90094 MW; C9D22AB42B0E7003 CRC64;
MAVTLPQHAR VVIVGGGIVG CSVAYHLTKL GWTDVVLLEQ GQLSCGTTWH AAGLVGQLRA
QESMTKLIRY STALYARLEA ETGLGTGWKQ CGSLSVARTA ERMTQLKRTA AVARAYGVAC
DVIGPKEAGE LWPVMRTDDL LGAVWLPGDG KANPTDLTQA LARGARTGGA RIVENTRVTA
IHTRPSISGG REACGLAWQN KDGDAGTIEA EVIVNCAGQW AKAVGRLCGV TVPLHSAEHY
YIVTERIAGV HPDLPVMRDP DGFIYFKEEV GGLVMGGFEP DAKPWGMNGI PENFEFQLLP
DDWDQFQILM ENALQRVPAL ETAQVRQFYN GPESFTPDNN FILGEAPELK RFFVGAGFNS
MGIASAGGAG MALAEWIVAG EPTMDLWPVD IRRFARFNGN DTWLHDRVKE TLGLHYAMPW
PNRELDSARP FRRSPLYALL KEDGACFGSK MGWERANFFA PSPAEAHVDY AFGQQNWLAW
SGAEHRACRE AVALFDMTSF SKFLVKGRDA ETVLQRIVAN DVAVPPGTTV YTGMLNERGT
YESDFTLTRL ADDQYLIVTG SAQTTRDFDT IEKLIPRDSH CTLVDVTGQY AVLAVMGPHS
RALLQRVSRA DFSNETFAFG QSREVDIGYA TVRATRLTYV GELGWELYVP VEFAVGVYET
LHAAGKEFGL VNAGYYAIDS LRIEKGYRAW GRELTPDSNP FEAGLGFACK LAGDVAFRGR
DALLKLKNEP LRRRMIVLTV DGASDRMLWG GEAILRDGVV VGFVSSAAFG HTFGCPVAMG
YVSNAAGTID EAFLAGGRFA VDVAGDMLPA TLHVKAPYDP KSSRIKA
//
