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Database: UniProt
Entry: A0A0F0G135_9BURK
LinkDB: A0A0F0G135_9BURK
Original site: A0A0F0G135_9BURK 
ID   A0A0F0G135_9BURK        Unreviewed;       835 AA.
AC   A0A0F0G135;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:KJK25986.1};
GN   ORFNames=UB46_03020 {ECO:0000313|EMBL:KJK25986.1};
OS   Burkholderiaceae bacterium 16.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae.
OX   NCBI_TaxID=1619952 {ECO:0000313|EMBL:KJK25986.1, ECO:0000313|Proteomes:UP000033515};
RN   [1] {ECO:0000313|EMBL:KJK25986.1, ECO:0000313|Proteomes:UP000033515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16 {ECO:0000313|EMBL:KJK25986.1,
RC   ECO:0000313|Proteomes:UP000033515};
RA   Roco C.A., Bergaust L., Bakken L., Yavitt J., Shapleigh J.P.;
RT   "The modularity of denitrifying soil bacteria: using gas kinetics and
RT   genome sequencing to connect denitrifier phenotype to genotype.";
RL   Submitted (FEB-2015) 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:KJK25986.1}.
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DR   EMBL; JYOD01000007; KJK25986.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0G135; -.
DR   STRING; 1619952.UB46_03020; -.
DR   PATRIC; fig|1619952.3.peg.7616; -.
DR   Proteomes; UP000033515; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          14..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          736..827
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   835 AA;  91203 MW;  4B53F3402C8FFBFD CRC64;
     MSASYRRPVP EHARVVIIGG GIIGCSVAYH LTKLGWTDVV LLEQGQLSCG TTWHAAGLVG
     QLRAQESMTK LIRYSTRLYS ELEAETGLGT GWKQCGSLSV ARTAERMTQL KRTAAVARAY
     GVDCEVISPR QAGELWPVMR TDDLHGAVWL PGDGKGNPTD LTQALARGAR SRGAFIVQDT
     KVTAIHTRDG RAGGVSWQDK QGASGRIEAE IVVNCAGQWA RQVGRLCGVT VPLHSAEHYY
     IVTERIAGVH PDLPVMRDPD GFIYFKEEVG GLVMGGFEPN AKPWGMQGIP EPFEFQLLPD
     DWDQFEILMQ NALQRVPALE TAQVKQFYNG PESFTPDNNF ILGEAPELRN FYVGAGFNSM
     GIASAGGAGM ALAEWIVAGE PTMDLWPVDI RRFAGFNGNE SWLHDRVKET LGLHYAMPWP
     NRELDTARPF RRSPLYAHLR EAGASFGSKM GWERPNFFAP AGETPEIRYA FSQQNWLPWS
     GAEHRACREG VALFDMSSFS KYIVKGADAQ AVLQQLMSND VAVPPGQTVY TAMLNEGGTY
     ESDLTVTRLA QDQYLLVTGS AQTTRDFSYI ERLIPADQRC AIVDVTGQYA VLAVMGPRSR
     ELLQRVSRAD FSSAAFPFGS SREIDLGYAT VRATRLTYVG ELGWELYVPV EFAVGVYETL
     HAAGKPLGLV NAGYYAIESL RIEKGYRAWS RELTTGIHPF EAGLSFACKL DKPIPFRGRE
     ALLKLRTSGG AAQVKRHVAV LTLDGASQAM LWGGEAVLRT GPDGTVRPAG FITSAAFGHT
     LGCPVGLALL QREDGAADAE WIAAGKYHVD LAGELMPASV HLRPPYDPGN ARVRV
//
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