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Database: UniProt
Entry: A0A177H485_9RHOB
LinkDB: A0A177H485_9RHOB
Original site: A0A177H485_9RHOB 
ID   A0A177H485_9RHOB        Unreviewed;       810 AA.
AC   A0A177H485;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=4-methylaminobutanoate oxidase (Formaldehyde-forming) {ECO:0000313|EMBL:OAH05765.1};
DE            EC=1.5.3.19 {ECO:0000313|EMBL:OAH05765.1};
GN   Name=mlr_7 {ECO:0000313|EMBL:OAH05765.1};
GN   ORFNames=pfor_37c3526 {ECO:0000313|EMBL:OAH05765.1};
OS   Rhodobacteraceae bacterium SB2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1689867 {ECO:0000313|EMBL:OAH05765.1, ECO:0000313|Proteomes:UP000077333};
RN   [1] {ECO:0000313|EMBL:OAH05765.1, ECO:0000313|Proteomes:UP000077333}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB2 {ECO:0000313|EMBL:OAH05765.1,
RC   ECO:0000313|Proteomes:UP000077333};
RA   Poehlein A., Billerbeck S., Voget S., Wemheuer B., Giebel H.-A.,
RA   Brinkhoff T., Daniel R., Simon M.;
RT   "A new prominent pelagic Roseobacter clade subcluster - CHAB-I-5:
RT   biogeography and genomic comparison to other roseobacters.";
RL   Submitted (MAY-2016) 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:OAH05765.1}.
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DR   EMBL; LGRT01000038; OAH05765.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A177H485; -.
DR   STRING; 1689867.pfor_37c3526; -.
DR   PATRIC; fig|1689867.3.peg.3570; -.
DR   OrthoDB; 7156675at2; -.
DR   Proteomes; UP000077333; 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:OAH05765.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077333}.
FT   DOMAIN          9..362
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          365..420
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          422..694
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          719..802
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   810 AA;  88224 MW;  E4A35F5DA53AB411 CRC64;
     MTLPSSAKTL IIGGGIIGCS TAYHLAQMGE EVLLLEKAAL TSGSTWHAAG LVGQLRSNAN
     ITQLLGYSID LYNKLEQETG LATGWKMNGG LRLACNEERW TEVKRQATTA HSFGLDMQLL
     TPKEAQDLWP LMDISDIVGA AFLPTDGQAS PSDITQALAK GARAKGAVIK ENTPVTEILI
     EGGKLAGVRT AAGDIACEKL VLCCGQWTRE LAQTIGVTVP LISVEHQYML TEAFGVPADL
     PTLRDPDRLT YYKEEVGGLI MGGYEPNGIP WAKDGIPEFF DFQLLESNFD HFEQLIEMAL
     PRVPKLESVG VKQLINGPES FTPDGNFILG EAPEMANVFI GAGFNAFGIA SGGGAGMALA
     EWVANGAPPY DMWPVDIRRF GRPHTDVDWV RTRTLEAYGK HYTMAWPSEE HDSGRPCRRS
     PLYDTLKSAG AVFGEKLGWE RPNWFAEKAE VARDIYTFER PNWHVPVGRE HKAAREAAVL
     LDQSSFAKFV LQGPDAEAAL QWIAANRVDK PVGSITYTQM LNDQGGIECD VTCVRTGHDS
     YYIVTGTGFA THDFDWIRRN IPDGMNAQLI DVTSSNAVLS LFGPKARNIL SAATRADVSN
     EAQPFATALQ IGIAGCPVLA LRITYVGELG WELHLPTEYA LSVYNALQDA GAEHGLRNAG
     YRAIETLRLE KGYRAWSSDI GPDHTPDEAG LGWAVKMKSN IAFRGREAVA AQRKEGVRKV
     LATFTTSGDT ILSGRETIYR NGVRCGWLSS GGYGHTLGHS IGMGYVRASE SIDREYVLQG
     TYELEVATER VSAEVTLNPL YDPGMDRVRG
//
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