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Database: UniProt
Entry: A0A2T7GBP7_9RHOB
LinkDB: A0A2T7GBP7_9RHOB
Original site: A0A2T7GBP7_9RHOB 
ID   A0A2T7GBP7_9RHOB        Unreviewed;       806 AA.
AC   A0A2T7GBP7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:PVA11839.1};
GN   ORFNames=DC366_02550 {ECO:0000313|EMBL:PVA11839.1};
OS   Pelagivirga sediminicola.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pelagivirga.
OX   NCBI_TaxID=2170575 {ECO:0000313|EMBL:PVA11839.1, ECO:0000313|Proteomes:UP000244446};
RN   [1] {ECO:0000313|EMBL:PVA11839.1, ECO:0000313|Proteomes:UP000244446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH-SD19 {ECO:0000313|EMBL:PVA11839.1,
RC   ECO:0000313|Proteomes:UP000244446};
RA   Ji X.;
RT   "Pelagivirga bohaiensis gen. nov., sp. nov., a bacterium isolated from the
RT   Bohai Sea.";
RL   Submitted (APR-2018) 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:PVA11839.1}.
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DR   EMBL; QCYH01000001; PVA11839.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7GBP7; -.
DR   OrthoDB; 7156675at2; -.
DR   Proteomes; UP000244446; 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:SF187; DIMETHYLGLYCINE DEHYDROGENASE, 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:UP000244446}.
FT   DOMAIN          7..364
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          367..420
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          424..691
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          732..798
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   806 AA;  87958 MW;  43ED2C016B5F582B CRC64;
     MKTHAQAVVI GGGVIGCSIL YHLTKLGWTD VILLERDELT SGSTWHAAAN IHGLHDSANI
     SRLQHYTMTL YNRLEAETGQ SCGVFQPGSL YLAQTEAREH QLRLQAAKAR LYGMNFSEID
     RAEAEALHPL VNFDGIRCIM WEPDGGNVDP SGVTAAYAAG ARAAGAEIHR FTPVTATRHQ
     PDGSWIVETP KGNISTPWIV NAAGLWGREV AALAGITLPL QPTEHQYFVT ETIAEIAALD
     RRLPSVADRD GEYYLRQEGK GLLIGAYEKD MRFWAEEGTP LDFAHELFAD DLDRIEYNMM
     RAIDRVPAAG AAGIKRVING PMIWTPDANV ILGPVPEKKG YFCCNGIIPG FSQSAGMGLM
     VADWIVEGEM RHDMFAWDMA RFGDWADKAF TKAKVGDQYA NRFAIHFPYE ERSAGRPCRV
     RPAYEMQKDM GAVFGLNYGW EHPLWFAGTP GVEETKGFTR QNWWAPVGEE CRMLRERAGI
     IDISNFAKYR CAGPGAEAWL NAVFANRMPG AVGRSCLTPL ISVRGGIAGD FTVTRTAEDE
     FWIIGSGMAE RYHKRFFNMV PLPEGTIFES RTEAICGFNV AGPGSRELLQ GLTDASLATA
     DFPFMRSASI RVAGVECLAL RVSFTGDLGW ELHCATGDQV ALYTALLEAG RALGAGPVGS
     RALMSLRIEK GYGSWGREYS PEYWPQEVGL APLVKLDKDF LHRDAAAAAM REPARETLVL
     LHLDEADTQA SGADATGGEP IFKDGAGIGR VTSGSYGYWV GMSLALGYVK GAQPGDRVEV
     MVLGRPHGAT ILPAPPFDPD GARLRG
//
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