ID A0A239BZS2_9RHOB Unreviewed; 814 AA.
AC A0A239BZS2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=4-methylaminobutanoate oxidase (Formaldehyde-forming) {ECO:0000313|EMBL:SNS13396.1};
GN ORFNames=SAMN05421757_10112 {ECO:0000313|EMBL:SNS13396.1};
OS Tropicimonas sediminicola.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tropicimonas.
OX NCBI_TaxID=1031541 {ECO:0000313|EMBL:SNS13396.1, ECO:0000313|Proteomes:UP000198426};
RN [1] {ECO:0000313|EMBL:SNS13396.1, ECO:0000313|Proteomes:UP000198426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29339 {ECO:0000313|EMBL:SNS13396.1,
RC ECO:0000313|Proteomes:UP000198426};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; FZOY01000001; SNS13396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239BZS2; -.
DR OrthoDB; 7156675at2; -.
DR Proteomes; UP000198426; 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:UP000198426}.
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 428..699
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 723..806
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 814 AA; 89594 MW; 5D07B899DCC96A21 CRC64;
MPLPPKQARV VIIGGGVIGC SVAYHLTKLG WTDVVLLERK QLCSGTTWHA AGLIAQLRAT
QNMTRLARYS QELYGTLEEE TSMSTGFKRV GSITVALTAE RQEELLRQAS MARAFGVEVE
PISPTEVQAR YGHLNCEGVV GGVYLPLDGQ GDPSNIALAL AKGARIRGAQ VLERTRVTGL
RRDGRRVTGV HWQSAEGEGE IACDHVVNCA GMWAHEVGRM AGTNVPLHAC EHFYIVTDKI
PGLEQLPVLR VPDECAYYKE DAGSILLGAF EPNAKPWGMN GIPESFEFDQ LPEDFDHFEP
ILEMAVNRLP MLAEAGIQTF FNGPESFTPD DAYHLGLAPE MDNVWVAAGF NSVGIQSAGG
AGMALADWME TGEKPFDLGD VDISRMQPFQ GNRHYLFERS KETLGLLYAD HFPYRQKATA
RGVRRTPLHE QLKARGAVFG ELAGWERANW FANEGEPGEY RYSWKRQNWF ENSAAEHRAV
RERVGLYDMS SFGKLRVEGP DAEAFLNYVG GGDYSVPVGK IVYTQFLNSR AGIEADVTVT
RLSETAFLVV TPAATRLSDE TWLRRHVGDH RVVITDVTAG EAVLAVMGPN ARALLQSVSP
NDFSNEANPF GTAQMIELGM GLARVHRVTY VGELGWEVYV SADMAAHAFE TLWEAGADHG
LKLCGMHMMD SCRIEKAFRH FGHDITCEDH VLEAGLGFAV KRDKPEFIGR DALLRKRDAG
LERRLVQFRL TDPEPLLYHA EPILRDGEVV GHLTSGNYGH TLGGAVGLGY VPCPGETPAE
LLASRFEIEV AGVRVAAEAS LKPMYDPRSE RVKD
//
