ID A0A1J5LGA2_9PROT Unreviewed; 806 AA.
AC A0A1J5LGA2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:OIQ32916.1};
GN ORFNames=BM562_04045 {ECO:0000313|EMBL:OIQ32916.1};
OS Alphaproteobacteria bacterium MedPE-SWcel.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1860092 {ECO:0000313|EMBL:OIQ32916.1, ECO:0000313|Proteomes:UP000183546};
RN [1] {ECO:0000313|EMBL:OIQ32916.1, ECO:0000313|Proteomes:UP000183546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MedPE-SWcel {ECO:0000313|EMBL:OIQ32916.1};
RX PubMed=27446036; DOI=10.3389/fmicb.2016.00996;
RA Lopez-Perez M., Kimes N.E., Haro-Moreno J.M., Rodriguez-Valera F.;
RT "Not All Particles Are Equal: The Selective Enrichment of Particle-
RT Associated Bacteria from the Mediterranean Sea.";
RL Front. Microbiol. 7:996-996(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:OIQ32916.1}.
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DR EMBL; MPDC01000003; OIQ32916.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5LGA2; -.
DR STRING; 1860092.BM562_04045; -.
DR Proteomes; UP000183546; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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;
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 423..692
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 718..798
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 806 AA; 88907 MW; 3F6396C9A4E1717D CRC64;
MRTQAKAVVI GGGVIGCSIL YHLTKLGWSD VVLLERDELT SGSTWHAAAN IHGLHDSTNI
SRLQHYTMTL YKELEKETGQ GCGVFQPGSL YLAQTEAREH QLRLQAAKAR LYGMNFHEIS
IAEAQELNPL VNYDGIRCVM YEPDGGNVDP SGVTQAYATG ARQRGGEIHR FTPVTATEPQ
DDGSWIVKTP KGDIRTDWVV NAAGLWGREV AALAGLDLPL QPTEHQYFVT ETIREVADMG
RRLPSVSDRD GEYYLRQEGQ GLLVGAYERD MKFWAEEGTP LDFAHDLFPD DLDRIEDNMM
NAIARVPLIA EAGIKRVING PMIWSPDANV LFGPVPEMQG YFCCNGIIPG FSQSGGMGLM
AAQWMIEGET QYDMFAWDVA RFGSWATRDF TRARVQDQYA HRFSIHFPNE ERSAGRPART
RPVYDAQKQM GAVFGLTAGW EHPLWFADRP GLCDTNGFTR QNWWGPVGAE CRMLRDAAGI
IDISNFAKYR CAGPDAEAWL NAVFANTMPT AVGRSCLTPL ISKRGGIAGD FTVTRTEDRE
FWIIGSGMAE RYHKRFFASV PLPEGTSFES LTQDVCGFNV AGPRSREMLQ RMTNVALDSA
SFPFMRSKRL MLDGINVLAL RVSFTGDLGW ELHCATEDQE KLYMTLIHAG RSIGAGPVGS
RALMSLRIEK GYGSWSREYS PEYLPHEVGL DRLCKMEKEF LNKPAAAAAL SAPARERLVI
LHLNEDDVAR SNADATGGEP IFKDGVGIGH VTSGTYGYTV GKSLALGYVN DAAPGDAVDV
MVLGRPHRAV ILAEPPFDPA GLRLRG
//
