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
//