ID W7YCG0_9BACT Unreviewed; 425 AA.
AC W7YCG0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Iota-carrageenase {ECO:0000313|EMBL:GAF02136.1};
GN ORFNames=JCM21142_2763 {ECO:0000313|EMBL:GAF02136.1};
OS Saccharicrinis fermentans DSM 9555 = JCM 21142.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC Saccharicrinis.
OX NCBI_TaxID=869213 {ECO:0000313|EMBL:GAF02136.1, ECO:0000313|Proteomes:UP000019402};
RN [1] {ECO:0000313|EMBL:GAF02136.1, ECO:0000313|Proteomes:UP000019402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 21142 {ECO:0000313|EMBL:GAF02136.1,
RC ECO:0000313|Proteomes:UP000019402};
RA Starns D., Oshima K., Suda W., Iino T., Yuki M., Inoue J., Kitamura K.,
RA Iida T., Darby A., Hattori M., Ohkuma M.;
RT "Draft Genome Sequence of Cytophaga fermentans JCM 21142T, a Facultative
RT Anaerobe Isolated from Marine Mud.";
RL Genome Announc. 2:e00206-14(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose
CC residues in alpha-D-galactosides, including galactose
CC oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
CC Evidence={ECO:0000256|ARBA:ARBA00001255};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing branched (1->3)-alpha-D-
CC galactosidic residues, producing free D-galactose.; EC=3.2.1.n1;
CC Evidence={ECO:0000256|ARBA:ARBA00001271};
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:GAF02136.1}.
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DR EMBL; BAMD01000006; GAF02136.1; -; Genomic_DNA.
DR RefSeq; WP_052342978.1; NZ_KI912107.1.
DR AlphaFoldDB; W7YCG0; -.
DR STRING; 869213.GCA_000517085_00790; -.
DR eggNOG; COG5434; Bacteria.
DR OrthoDB; 1115455at2; -.
DR Proteomes; UP000019402; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR024535; Pectate_lyase_SF_prot.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR PANTHER; PTHR31339; PECTIN LYASE-RELATED; 1.
DR PANTHER; PTHR31339:SF9; PLASMIN AND FIBRONECTIN-BINDING PROTEIN A; 1.
DR Pfam; PF12708; Pectate_lyase_3; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000019402};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 56..240
FT /note="Pectate lyase superfamily protein"
FT /evidence="ECO:0000259|Pfam:PF12708"
SQ SEQUENCE 425 AA; 46885 MW; D90622209888F70E CRC64;
MNFIFNYFKA KYICSARLCA VCFLNYILLV GITAQNTKES DFYTETNHLG VVKNFVNDYG
GNGNDALDDS EKLQEAIDEL SSLKNGGKII FPSGTYYLAE IQLRSNVHLV IDRETTIIPV
QRQNQKNYKI FQLDGQNEII KNVSIRGVGG AFKVDLRNLK NKNVGVFSCG NVENFLIANF
HVLDDYTKFS AVTFGVSAFK GGYNYASRGV IKNASIKNAN YGYGLIQTQA ARDILFENIS
GSGGVTLRFE TGYDKMNKLQ VGGVFNMVAR NVSCENGNAA LMISPHSMHN GSVNVDGVYA
KNCGFAVRIE KGYVKKGLKS LNLVPGIYEP SEVKNVTAIY GNSAQLKSKH FKYMRCHLRN
LITVDANHTL EKIYSGPSIA AVLNGAEGEG KGKFLVKVSN VSSSGFTEDQ KDILYEEDTY
LCSEN
//
