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Database: UniProt
Entry: B8D1Q1_HALOH
LinkDB: B8D1Q1_HALOH
Original site: B8D1Q1_HALOH 
ID   B8D1Q1_HALOH            Unreviewed;      1024 AA.
AC   B8D1Q1;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Glycoside hydrolase family 31 {ECO:0000313|EMBL:ACL69128.1};
GN   OrderedLocusNames=Hore_03670 {ECO:0000313|EMBL:ACL69128.1};
OS   Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halothermotrichaceae;
OC   Halothermothrix.
OX   NCBI_TaxID=373903 {ECO:0000313|EMBL:ACL69128.1, ECO:0000313|Proteomes:UP000000719};
RN   [1] {ECO:0000313|EMBL:ACL69128.1, ECO:0000313|Proteomes:UP000000719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H 168 / OCM 544 / DSM 9562 {ECO:0000313|Proteomes:UP000000719};
RX   PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA   Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA   Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT   "Genome analysis of the anaerobic thermohalophilic bacterium
RT   Halothermothrix orenii.";
RL   PLoS ONE 4:E4192-E4192(2009).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR   EMBL; CP001098; ACL69128.1; -; Genomic_DNA.
DR   RefSeq; WP_012635316.1; NC_011899.1.
DR   AlphaFoldDB; B8D1Q1; -.
DR   STRING; 373903.Hore_03670; -.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   KEGG; hor:Hore_03670; -.
DR   eggNOG; COG1501; Bacteria.
DR   HOGENOM; CLU_000631_7_3_9; -.
DR   OrthoDB; 176168at2; -.
DR   Proteomes; UP000000719; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd14752; GH31_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR   InterPro; IPR033403; DUF5110.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR43863; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G03140)-RELATED; 1.
DR   PANTHER; PTHR43863:SF2; MALTASE-GLUCOAMYLASE, INTESTINAL-LIKE; 1.
DR   Pfam; PF17137; DUF5110; 1.
DR   Pfam; PF13802; Gal_mutarotas_2; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361185};
KW   Hydrolase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:ACL69128.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000719}.
FT   DOMAIN          9..167
FT                   /note="Glycoside hydrolase family 31 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13802"
FT   DOMAIN          236..540
FT                   /note="Glycoside hydrolase family 31 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01055"
FT   DOMAIN          549..634
FT                   /note="Glycosyl hydrolase family 31 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21365"
FT   DOMAIN          651..714
FT                   /note="DUF5110"
FT                   /evidence="ECO:0000259|Pfam:PF17137"
SQ   SEQUENCE   1024 AA;  120060 MW;  908E96ED22FE1280 CRC64;
     MHLDNYNVVF NILEGEVLHI QIQDKNNKSP FLRVTGGEKV LKSIDYHQVD SREIIPVSER
     YNLEINKDRE SFKIFDKTRQ KIVLESYDSF FRKVDEKQKG LSLSIKENEL FTGLGQDVEG
     KLYIEDIERR CWNEWNGYDY LGSNSVPFYL SNQGYGLYLD TTYPSRFVFG KGEIQPKPIA
     HEVMAETPFD WEEKACVNAE DQLTILGWEE EQLDFYILLG DMAEIEQKYY QLTGKPSLLP
     KWSLGYIQCK NRYKSEEEIL HIARKMREKG IPCDVIVIDW LWFKEFGDLY WDGENYSEKM
     AETIKKLKDM GIKILLAVHP FVDYSSKNYK ELSEKGCLSK VPEGGRPYFD HTNPATKEAM
     WKFYQKLYDE GVAGWWTDMG EPESDLPGTQ GYAGKREVYH NVYTLLWSKN IMEAQRENTG
     SRNFCLARTN ALGIQNYNTA YWTGDIFATW EIYRRNIKAL QTVSVSGQPY VCTDIGGFHT
     DERFTPELYV RWLQWGVFAG LFRVHGVKPE NEPWSLGESN EKIIKKIIEF RYRFIPYIYE
     KMYQMQQNGE AFIRPLIYDY PQDEKAIERE YQYLFGDILV CPVVEPDVRE IDVYLPAGKW
     YDFYKGTMYY GGETYKAYAP IDRIPLYVKD GSIILTTEPE EDVKDIYDKY QLLIYGEGST
     TEYIYEDDGT SYGYEDGSYN LIKLEKKDNQ LTVSTLQHKY KEENTNRELE IVYYKNNKKY
     TRTVDYTIGE TINISLQEGK ESNIQVVNVE MDVDVTHSEY NGDFYANLSI KNNLNEPQNL
     RIRIEKPDHY YVKAQIDLPE SLDFSSNVKV EESAEYLYRK IQVEDTYTSV FPFKPFKDKM
     PQQEKIEVAI EDQRTGKVLD KKIITLGNGY LKNWRYAVSK YEEIDKDDLN FAPALDSNPW
     GYIYLYKYLN MQENGINPVD FIEIIQKIGY GYARVNILSP ENKKAYLRIR ADEGSTFYLN
     GEKIHENSRY TIEEDILIEL EKGVNLLEAN VQWKSPRPFT GREFGLSAQV LTLDKEIDET
     VKSF
//
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