ID B0C9D3_ACAM1 Unreviewed; 761 AA.
AC B0C9D3;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Glycoside hydrolase family 2, sugar binding {ECO:0000313|EMBL:ABW27814.1};
GN OrderedLocusNames=AM1_2814 {ECO:0000313|EMBL:ABW27814.1};
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC Acaryochloridaceae; Acaryochloris.
OX NCBI_TaxID=329726 {ECO:0000313|EMBL:ABW27814.1, ECO:0000313|Proteomes:UP000000268};
RN [1] {ECO:0000313|EMBL:ABW27814.1, ECO:0000313|Proteomes:UP000000268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017 {ECO:0000313|Proteomes:UP000000268};
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; CP000828; ABW27814.1; -; Genomic_DNA.
DR AlphaFoldDB; B0C9D3; -.
DR STRING; 329726.AM1_2814; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR KEGG; amr:AM1_2814; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_005015_5_0_3; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000000268; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABW27814.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000268};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 73..160
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 217..331
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 343..540
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 761 AA; 88290 MW; AB8C3C355C4D108B CRC64;
MFLGCLTATH PRLIANPHLF HAQAYWTPTV TQTVNQTSLA GTWEFQADPQ PPADKLVLQP
SGPDLPPLPQ GQWQKITVPS NWYLQGQDAS GVVWYRHQFR ANDRWRRKIT RLVFSGVDYT
ADVWLNGQYL GFHEGYFQPF SFDVSKALMF TGQNELLVRV NSPLEPEGQD WSLRKRLIKG
IFSHHDTRPG GAWTDRGQEK NTGGIWAPVF LQVSDQVAIE TLQITPELDT DHQQATAKVD
LVVNSPGLGK TTLDAHMKLE PENFEGVPIG PIQVQRTLHQ GANHLKLEVP VDDPKLWWSW
EHGDPNLYRL TVQLADGNRL LDKASDVFGF RTIQFDPTEK IWRLNGRRLF LRGTNYIATQ
WLSEMTPDKY QTDIDLMKAV NINTVRVHAH VIGKEFYELC DRNGVFIWQD FPLQWGYEDT
PQFLKEATRQ AKDMIGYLYN HPSILAWSLH NEPPWDADWM KYKYESYNPE QNRELDAKLF
ANLQGEDPTR LLHPVSTVGE HPWWGWYSHT MYKYAEPTTE AIISEFGAQA LPHIDSLRRI
FTEDELWPDT EAEWDKWLYH NFQRHETFNI AKVPMGNTTQ EFIDNTQQYQ SQLIQFAAEA
YRRQRYQPVS SIFQFMFVED WPSMNWGIVD YWRQPKPGHE ALKWAYQPVL PSIAWPQLTW
TLGETVELEL WAINDLWKDY PEAIFTYALR QNQQRLKSGQ SRINLAADSS QPVDKIFFQP
QNLGSYTVTA TLKDRLGTVL GENQFVFDVI DRGDQTNEST S
//
