ID A0A085F8S5_9BURK Unreviewed; 613 AA.
AC A0A085F8S5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Pectin lyase fold-containing protein {ECO:0000313|EMBL:KFC67870.1};
GN ORFNames=FG94_03008 {ECO:0000313|EMBL:KFC67870.1};
OS Massilia sp. LC238.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1502852 {ECO:0000313|EMBL:KFC67870.1, ECO:0000313|Proteomes:UP000028601};
RN [1] {ECO:0000313|EMBL:KFC67870.1, ECO:0000313|Proteomes:UP000028601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC238 {ECO:0000313|EMBL:KFC67870.1,
RC ECO:0000313|Proteomes:UP000028601};
RA Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT isolate.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family.
CC {ECO:0000256|ARBA:ARBA00008834, ECO:0000256|RuleBase:RU361169}.
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:KFC67870.1}.
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DR EMBL; JNNN01000053; KFC67870.1; -; Genomic_DNA.
DR RefSeq; WP_036213139.1; NZ_JNNN01000053.1.
DR AlphaFoldDB; A0A085F8S5; -.
DR STRING; 1502852.FG94_03008; -.
DR PATRIC; fig|1502852.3.peg.2966; -.
DR eggNOG; COG5434; Bacteria.
DR OrthoDB; 9795222at2; -.
DR Proteomes; UP000028601; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR000743; Glyco_hydro_28.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR31339:SF71; PECTIN LYASE-LIKE SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR31339; PECTIN LYASE-RELATED; 1.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS00502; POLYGALACTURONASE; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361169};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361169};
KW Lyase {ECO:0000313|EMBL:KFC67870.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..613
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001789682"
SQ SEQUENCE 613 AA; 66183 MW; C15F43431E799123 CRC64;
MTKRHINPQR RSLLYAASAS VAGLAVGPAL AASGGTKVAQ DDPWARAQSI IDGFRKPLVF
PKRDFLITAY GAKPCEAVMV TGYVADHEEG KLSTPAPGAH DCYAAIAAAI AACSAAGGGR
VVIPAGNWLV KGPIVLKSNV NVHLAKGAHV YFSNDPEDFA KYGDYDCGPN GKLVISRWQS
NDCLNYSPMV YAYGQTNIAL TGEDWTSILD GQGGVPRADG ETWWDWKGKR KGVAGKAHNQ
QRTQIAVNPL NPTSIRTVAP NLNDAQVALM EGTNDKWRTD EAYLPTLSEA GVPAAKRVFG
RGHYLRPCMV EFIGCTNVLM QGYQLNQTPF WQHHPVNCSK VEIRGVHMDS MGPNSDGFDP
EACNTVLVDG CTFNSGDDCI AIKAGKNLDT QFGPTQNVVI QNCVMNSGHG GVTLGSEMAG
GIQHVYAQDI EFRNTHWASD PLNTAIRLKT NMNRGGFLRH FYVRNVTMPN GVNLKPQFYT
PLPGSPIKPK SVGAGAGAVI TFDCDYAPNA DNVRTRPPVV EHIHISGVRV GNVATENGPR
SCYQALLLLG PVAFDYNGDK PVDILPIRDV TITDCDFGTP VNADQPWFIY NVRNVKLSKV
TIAGKVYNTT LQA
//
