ID A0A074TEQ1_9RHOB Unreviewed; 833 AA.
AC A0A074TEQ1;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Diguanylate cyclase {ECO:0000313|EMBL:KEP70149.1};
GN ORFNames=DL1_18630 {ECO:0000313|EMBL:KEP70149.1};
OS Thioclava dalianensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1185766 {ECO:0000313|EMBL:KEP70149.1, ECO:0000313|Proteomes:UP000027725};
RN [1] {ECO:0000313|EMBL:KEP70149.1, ECO:0000313|Proteomes:UP000027725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DLFJ1-1 {ECO:0000313|EMBL:KEP70149.1,
RC ECO:0000313|Proteomes:UP000027725};
RA Lai Q., Shao Z.;
RT "The draft genome sequence of Thioclava dalianensis DLFJ1-1.";
RL Submitted (MAR-2014) 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:KEP70149.1}.
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DR EMBL; JHEH01000007; KEP70149.1; -; Genomic_DNA.
DR RefSeq; WP_038064558.1; NZ_JHEH01000007.1.
DR AlphaFoldDB; A0A074TEQ1; -.
DR STRING; 1185766.SAMN05216224_101386; -.
DR eggNOG; COG0404; Bacteria.
DR eggNOG; COG0665; Bacteria.
DR OrthoDB; 7156675at2; -.
DR Proteomes; UP000027725; 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:UP000027725}.
FT DOMAIN 6..380
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..722
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 744..818
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 833 AA; 93169 MW; 65077CA4DED50C59 CRC64;
MKTHVKVLVV GGGAVGCGVA YHLAKAGWDT LLVERDELTS GSTWHAAGLL PLFNMSYATT
HIHKYSVDFY KSLEAETGLN AGFAVVGNLR MAQTEARMDE YRLYSSVAET AEVHHEFLTP
AQMKERWPLL RTDDLKGALF HPQDGYINPA DVTQAMAKGA RQHGAEIARK LQVNAYRWTG
SEWVVTLEKM VERGNRLVPS GEEIEIRAEH VVTCTGNHAQ RTARLLGIKI PAIPVEHQFI
VTEPDPALMK WRAEGNPEHP VLRDADAKWY VREERGGWIL GPYERNAPAR FEYEVPDSFR
ADLFQLDLDR IEEEYMSMIH RLPTSEEVGL KDDFNGPICY TPDGNPLVGP APGLRNMWLA
EGFSFGITAA GGTGHYLAQL MTQGEAEIDM ASLDPRRYGA WMTTEYAARK NEEAYEHVFI
LHHPDEEREA CRPLRTAPNY DRQIAEGAQM GQVNGWERPN YYGPKDAPAS FDHDSRSFRR
GAWWDYAKAE AEAVRETAGL IDATAFTKHL VRGPGATAFL DLFTCNKLPK VGRINLTYAL
TKAGTTRTEY TIVRLSEDEY YLISAGAWTD YDSDFLKQSI EDFRADGGDY VDCHDITTQW
GVFALAGPNA RAILAEIVKD ADPATVLSNK RFPWLSMRNI ELGMCPVRAI RVAYTGELGW
ELHHPIEMSR YLWDLLIAAG EKHGMKLVGA RAQNWLRQEK SYRAFGTELG RDATPQEAGL
DRFIDLSKEF TGKQAMLDTG IRAKCVTLLI DGPEDSDPWG KEAIFDQGRK VGRLTSGGWS
VAFGKQIGMG YVPPELSEPG TKLKVKIQLE EWDAVVAEDS PHDPSNARIR VDG
//