ID A0A1V1UYY5_9CAUL Unreviewed; 402 AA.
AC A0A1V1UYY5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Rhamnogalacturonan acetylesterase RhgT {ECO:0000313|EMBL:GAW41093.1};
GN Name=rhgT {ECO:0000313|EMBL:GAW41093.1};
GN ORFNames=SH203_01496 {ECO:0000313|EMBL:GAW41093.1};
OS Brevundimonas sp. SH203.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=345167 {ECO:0000313|EMBL:GAW41093.1, ECO:0000313|Proteomes:UP000195546};
RN [1] {ECO:0000313|EMBL:GAW41093.1, ECO:0000313|Proteomes:UP000195546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH203 {ECO:0000313|EMBL:GAW41093.1,
RC ECO:0000313|Proteomes:UP000195546};
RA Suzuki T., Kikuchi M., Habu N., Konno N.;
RT "Draft Genome Sequence of Brevundimonas sp. SH203, producing Cellouronate
RT (beta-1,4-linked polyglucuronate) lyase.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000256|ARBA:ARBA00008668}.
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:GAW41093.1}.
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DR EMBL; BDMM01000003; GAW41093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V1UYY5; -.
DR OrthoDB; 191551at2; -.
DR Proteomes; UP000195546; Unassembled WGS sequence.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProt.
DR CDD; cd01821; Rhamnogalacturan_acetylesterase_like; 1.
DR Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
DR Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR037459; RhgT-like.
DR InterPro; IPR013830; SGNH_hydro.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR PANTHER; PTHR43695; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G17250)-RELATED; 1.
DR PANTHER; PTHR43695:SF1; RHAMNOGALACTURONAN ACETYLESTERASE; 1.
DR Pfam; PF13472; Lipase_GDSL_2; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52266; SGNH hydrolase; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000195546};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..402
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013341766"
FT DOMAIN 168..347
FT /note="SGNH hydrolase-type esterase"
FT /evidence="ECO:0000259|Pfam:PF13472"
FT REGION 376..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 402 AA; 43533 MW; EE1CBEB06CD03981 CRC64;
MLTAILMAAA ISTWRFDLAA QPTAPDRIAV QPGQTYQPNA YGFEPGAASD GYLFSAAVPE
GVYRVTVRFG GSQAGRTTVK AEARRLMVRD VVTAPGAYQT RSFLVHVRGP ALPPPPANAP
GGTAVVLTPQ ELASRTWDDR LTLEFLDRPQ VAAIDIEPVA APVVYLAGDS TVTDQPSEPA
ASWGQMLPAL LTPDVAVANY AQSGETLKSF LSELRLAKIL TTLKAGDWLL IQFGHNDQKT
QWLQTYVDPD TTYPAYLKVF IAEAKRRGAH PILVTSPERR NFRDGRIQDT LGTYAEAARR
VAREEDVPLI DLNDASRRIY EALGPDQAPR LFNDGGADHT HHDNAGAWLL ARAVAAQIAE
KAPDLAAHVA PDFRRFTPDA PPMAETAVAP SLTASRERPR GD
//