ID A0A1Q6WRH6_9GAMM Unreviewed; 815 AA.
AC A0A1Q6WRH6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 03-MAY-2023, entry version 20.
DE SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:OLB15829.1};
GN ORFNames=AUH10_00890 {ECO:0000313|EMBL:OLB15829.1};
OS Gammaproteobacteria bacterium 13_2_20CM_66_19.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1805166 {ECO:0000313|EMBL:OLB15829.1, ECO:0000313|Proteomes:UP000186999};
RN [1] {ECO:0000313|EMBL:OLB15829.1, ECO:0000313|Proteomes:UP000186999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLB15829.1}.
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DR EMBL; MNCZ01000008; OLB15829.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q6WRH6; -.
DR STRING; 1805166.AUH10_00890; -.
DR Proteomes; UP000186999; 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;
FT DOMAIN 9..365
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 368..423
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 425..697
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 722..807
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 815 AA; 88921 MW; 24684CEDAD576200 CRC64;
MPDLPSHARV VIIGGGIVGC SVAYHLAKRG CKDVLLLERR QLTCGTTWHA AGLVGQLRAT
RNLTRLAQYT TQLYQRLERE TGQATGFRQV GSIAVAASEA RFQELKRGAS MARSFGLEVQ
ILSPDAARER WPLLSTDGLV GAVFLPKDGR TNPVDTTQAL ARGARSAGVR IVENLKVTGI
RSARGRVSGV ATEAGEVRAD AVVNCAGLWA REVGAWAGVS VPLHAAEHFY IVTEPIAGLA
PDLPVLRDAD ARSYFKEDTG KLLVGWFEPE AKPWGWQGIP ENFAFEHLPA DLGHIEPLFA
AAMRRVPALE SAGVQVFFNG PESFTPDDRY LLGEAPELRG LYVAAGFNSI GIQSAGGAGK
VLADWILDGH PPFDLWDVDI RRCAPFQRNR RYLRERTVET LGLLYAMHWP YRQAESARGV
RKSVVHDRLA AAGACFGEVA GYERANWFAT GGAEPRYAYS YGRQNWFEHS AGEHRAVRER
VGLFDQSSFA KFALLGPDAA AVLGRICANE VDVPVGRIVY TQWLNERGGI EADLTVTREA
EDAYLVVTSC ATQTRDFSWL CRSIPAEARA VALDVSPAYA VLGLMGPQSR ELLATLTDAD
LSNAAFPFAT SQVIDLGYAR VRACRITYVG ELGYELYIPT DFAQSVYDLI VGAGAAYGLR
LAGYHALDSL RMERGYRHWG HDISDEDTPL EAGLQFAVAW DKPGGFVGRE TLVRQREAGV
RRRLVALALE RADLLLYHSE PIWRNGELVG AISSGAFGHT LGRSLGLGYV ANGGAPVSAE
WITAGEYQVE IASERIPARV SLQPFFDPAG ERVRR
//
