ID D4IKB7_9BACT Unreviewed; 858 AA.
AC D4IKB7;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=DUF4955 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AL1_08240 {ECO:0000313|EMBL:CBK63379.1};
OS Alistipes shahii WAL 8301.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=717959 {ECO:0000313|EMBL:CBK63379.1, ECO:0000313|Proteomes:UP000008794};
RN [1] {ECO:0000313|EMBL:CBK63379.1, ECO:0000313|Proteomes:UP000008794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAL 8301 {ECO:0000313|EMBL:CBK63379.1,
RC ECO:0000313|Proteomes:UP000008794};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J.;
RT "The genome sequence of Alistipes shahii WAL 8301.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK63379.1, ECO:0000313|Proteomes:UP000008794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAL 8301 {ECO:0000313|EMBL:CBK63379.1,
RC ECO:0000313|Proteomes:UP000008794};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; FP929032; CBK63379.1; -; Genomic_DNA.
DR RefSeq; WP_015546314.1; NZ_CP102253.1.
DR AlphaFoldDB; D4IKB7; -.
DR STRING; 717959.AL1_08240; -.
DR KEGG; ash:AL1_08240; -.
DR PATRIC; fig|717959.3.peg.2415; -.
DR HOGENOM; CLU_336401_0_0_10; -.
DR OrthoDB; 188639at2; -.
DR Proteomes; UP000008794; Chromosome.
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; IPR032532; DUF4955.
DR InterPro; IPR032149; DUF4988.
DR InterPro; IPR024535; Pectate_lyase_SF_prot.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF16315; DUF4955; 1.
DR Pfam; PF16378; DUF4988; 1.
DR Pfam; PF12708; Pectate_lyase_3; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008794}.
FT DOMAIN 25..215
FT /note="DUF4988"
FT /evidence="ECO:0000259|Pfam:PF16378"
FT DOMAIN 355..495
FT /note="Pectate lyase superfamily protein"
FT /evidence="ECO:0000259|Pfam:PF12708"
FT DOMAIN 705..857
FT /note="DUF4955"
FT /evidence="ECO:0000259|Pfam:PF16315"
SQ SEQUENCE 858 AA; 93157 MW; 87D10087DAE0F453 CRC64;
MNKLFLWIAA ASAFVLQSCE NTDGIRDEIG SLRDRVIALE AKIGSVNTSI VALHKLMDES
TIIVGIEPNA KGYEIELSDG TRLPVILGEK IEALVPVMGI DAEGYWTVSL DGGATSERLK
VGGEYVSAWP VSGGDHKPGA EGVTPQLKVS ADGEWLVSLD GGVTYAPLLQ NGQPVNALGD
KVVVSYSSAF KSVTYDATTG LLAVELLDGE KLTLPVFDDF GLTVTASDNE TFRLGETRAF
EVVQNNVAEA VIDAPAGWTA VLGETTLTVK APATFDAASQ QAAVSVTVYS DRKYRKLVTL
NVTLLDEQVD VNAALAWRNF KAGTADNVLL DYSYAGYKHG EEAPADVWGL GYKVYNVVDY
GADPTGVRSS RGALAALLKE LKLSGRSDAG ANLANANARA VIYFPEGRFV LHNDDDNVVD
PTSANQKYTD SKGNNRSEEI FIRGGYFVLK GAGRGKTTLV MDTPNLPNNS EQMWSSPMMI
NIKHNSGLSD LTTVTGDAAR GTFSVEVASA AGIGKGDWVC LSLSNNDPTL VAQELAPHRV
EGNMTDIQTI TVEDYHQVAS VSGNRVTFAE PIMYAVEAKW GWKIRKYPHY EHVGVEDLTF
EGRSKENFGH HASWEDDGAY KPLNMMRLTD SWIRRVDFRG VSEALSIVSS ANCSAYDIEI
SGNRGHSGVR SQSSSRIFIG KVCDRSRGQA VSPPYTSTGY FENAGQYHAS GVSNTSLGAV
LWNNTWGDDA FFESHSRQPR ATLVDRCTGG FVQWRFGGDE TNVPNHLGDL TIWNLNATRA
AHDFGAEPFK WWLSSDKWWK TMPPIIVGFH GAAVTFDESA EQVKYLESNG AAVEPLSLYE
AQLRQRLGYV PAWLNSLK
//