ID A0A099F361_9RHOB Unreviewed; 830 AA.
AC A0A099F361;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Diguanylate cyclase {ECO:0000313|EMBL:KGJ05105.1};
DE SubName: Full=Dimethylglycine dehydrogenase {ECO:0000313|EMBL:SFA44152.1};
GN ORFNames=IT41_06845 {ECO:0000313|EMBL:KGJ05105.1}, SAMN04487972_103170
GN {ECO:0000313|EMBL:SFA44152.1};
OS Paracoccus halophilus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=376733 {ECO:0000313|EMBL:KGJ05105.1, ECO:0000313|Proteomes:UP000029846};
RN [1] {ECO:0000313|EMBL:KGJ05105.1, ECO:0000313|Proteomes:UP000029846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14014 {ECO:0000313|EMBL:KGJ05105.1,
RC ECO:0000313|Proteomes:UP000029846};
RA McGinnis J.M., Wolfgang W.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGJ05105.1, ECO:0000313|Proteomes:UP000029846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14014 {ECO:0000313|EMBL:KGJ05105.1,
RC ECO:0000313|Proteomes:UP000029846};
RA Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT York State patients.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SFA44152.1, ECO:0000313|Proteomes:UP000182312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6117 {ECO:0000313|EMBL:SFA44152.1,
RC ECO:0000313|Proteomes:UP000182312};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; JRKN01000007; KGJ05105.1; -; Genomic_DNA.
DR EMBL; FOJO01000003; SFA44152.1; -; Genomic_DNA.
DR RefSeq; WP_036739749.1; NZ_JRKN01000007.1.
DR AlphaFoldDB; A0A099F361; -.
DR STRING; 376733.SAMN04487972_103170; -.
DR eggNOG; COG0404; Bacteria.
DR eggNOG; COG0665; Bacteria.
DR OrthoDB; 7156675at2; -.
DR Proteomes; UP000029846; Unassembled WGS sequence.
DR Proteomes; UP000182312; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000029846}.
FT DOMAIN 7..379
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 384..436
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 440..718
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 740..820
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 830 AA; 91997 MW; 6C32CC7855D39835 CRC64;
MKTHVKALIV GGGAVGCGIA YHLARAGWDT MLVERDELTA GSTWHAAGLL PLFNMGYATS
HIHDYSVKLY AGLEAETGLN AGFTRCGNLR MAQTDARMDE YMLYSATAET VGIEHEFLTP
AQIRERWPLV RTEDLKGALF HPTDGYINPA DVTQAMAKGA RMAGCTIERK IQVNAYRWTG
SEWVVTVERM VEKGGNLIPS GEVFEITAEH VVTATGNHAQ RTARLLGIKI PAIPVEHQYI
VTEPDPALVK WRAEGNPEHP VLRDADAKWY VREERGGWIL GPYERNAPAR FHYDVPESFR
ADLFPLDLER IEEEYMSMIH RIPTSETVGL KDDFNGPICY TPDGNPLVGP APGLRNMWLA
EGFSFGITAA GGVGHYLSQI MTAGEAEIDM ASLDPRRFGG WMTTEYAAKK NEESYEHVFI
LHHPDEEREA ARPLRTAPAY DRQIAAGAQM GQVNGWERPN YYAPAGFDDH ASRSFRHGGW
WQYAADEARA IRETAGLIDA SAFAKHRVSG PGATAFLDWL TTNKLPKVGR INLTYALTAT
GTTHTEYTIV RLAEDDYYLI SAGAWTDYDG DNLRKLAEDR TGDFGAITVQ DISTQWGVFA
IAGPNSRAIL NEILRDADPA TVLGNKRFPW LSMRNIELGM CPVRAIRVAY TGELGWELHH
PVEFGRYLWD QLVAAGEKHG MKLVGARAQN WLRQEKSYRA FGTELGRDAT PLEAGLDRFV
DSDKDFRGKQ AMLDKGIRSK CVTLLIDGPE GADPWGREGL FLPDGTRIGR LTSGGRSVAF
GKSIGMGYVR PDLAAPGTKL KIRMFRELFD AEVAEDSPYD PTNARIRVDG
//
