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Database: UniProt
Entry: K6DA84_9BACI
LinkDB: K6DA84_9BACI
Original site: K6DA84_9BACI 
ID   K6DA84_9BACI            Unreviewed;       897 AA.
AC   K6DA84;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Glycoside hydrolase family protein {ECO:0000313|EMBL:EKN65229.1};
GN   ORFNames=BABA_21331 {ECO:0000313|EMBL:EKN65229.1};
OS   Neobacillus bataviensis LMG 21833.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX   NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN65229.1, ECO:0000313|Proteomes:UP000006316};
RN   [1] {ECO:0000313|EMBL:EKN65229.1, ECO:0000313|Proteomes:UP000006316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX   PubMed=23087684;
RA   Heylen K., Keltjens J.;
RT   "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT   reduction in Bacillus.";
RL   Front. Microbiol. 3:371-371(2012).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792}.
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:EKN65229.1}.
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DR   EMBL; AJLS01000137; EKN65229.1; -; Genomic_DNA.
DR   RefSeq; WP_007087258.1; NZ_AJLS01000137.1.
DR   AlphaFoldDB; K6DA84; -.
DR   STRING; 1117379.BABA_21331; -.
DR   PATRIC; fig|1117379.3.peg.4422; -.
DR   eggNOG; COG0383; Bacteria.
DR   OrthoDB; 9764050at2; -.
DR   Proteomes; UP000006316; Unassembled WGS sequence.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR   CDD; cd10814; GH38N_AMII_SpGH38_like; 1.
DR   Gene3D; 2.60.40.2210; -; 1.
DR   Gene3D; 2.60.40.2220; -; 1.
DR   Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR   Gene3D; 1.20.1270.50; Glycoside hydrolase family 38, central domain; 1.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR041509; GH38_beta-1.
DR   InterPro; IPR041147; GH38_C.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR011682; Glyco_hydro_38_C.
DR   InterPro; IPR015341; Glyco_hydro_38_cen.
DR   InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR   InterPro; IPR000602; Glyco_hydro_38_N.
DR   InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR   InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR   PANTHER; PTHR46017; ALPHA-MANNOSIDASE 2C1; 1.
DR   PANTHER; PTHR46017:SF2; MANNOSYLGLYCERATE HYDROLASE; 1.
DR   Pfam; PF09261; Alpha-mann_mid; 1.
DR   Pfam; PF17677; Glyco_hydro38C2; 1.
DR   Pfam; PF18438; Glyco_hydro_38; 1.
DR   Pfam; PF07748; Glyco_hydro_38C; 1.
DR   Pfam; PF01074; Glyco_hydro_38N; 1.
DR   SMART; SM00872; Alpha-mann_mid; 1.
DR   SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EKN65229.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006316}.
FT   DOMAIN          299..372
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   897 AA;  102586 MW;  09D5DD29EF99C411 CRC64;
     MSAKQSVHII SHTHWDREWY LPFEKHHVLL CKLMDQLMET LEADENYKSF HLDGQTIILD
     DYLQFRPEMK EKLQRLIDAG RIHIGPWYIL QDEFLTSSEA NLRNLQYGLK DAAKWSSNVS
     KLGYFPDSFG NMGQAPQILQ QAGIDTAVFG RGVKPTGFNN TVSDAEDYES PYSEMNWQAP
     DGSTVLGILF ANWYSNGNEI PVDRDQAQEF WKKKLADAEK YAATPHLLLM NGCDHQPAQT
     DLSEAIKVAR ELFPDYEFIH SDFDHYINQV KQSLPKDVKV VNGELRSQHT DGWGTLVNTA
     SSRIYLKQLN QKGQAMLEKV AEPLASLAYL AGEQYPHHLF SYAWKTLMQN HPHDSICGCS
     VDEVHREMVT RFDKSRHVAE MIIDDSTAAL TSRINTNAYR PYGEDAIPFT VFNTSGWMRT
     GVVTVELDLE RQYYAKGVNR LELLNICTDN RILIDEHGQE YPFALTDLGI QFGYDLPDDQ
     FRQPYMARKV RLTFEACEIP NLGYKTFAFV KAEKPSVADT LIHHPREMEN EFFIVHFEDN
     GSLTVTDKMS GNVFTKLCVY EDSGDIGNEY MYRQPDGEKA LTTEQIKAEI RIIEDTPFQA
     AFEIVHHWGL PSRASEQLDS EQSQLVWFTA RKSQRVQETT PFTIKTIVKL EKHGKGIDVT
     ASFDNQVTDH RLRVLFPTEI DTHCHYADSI FEVAKRDNQP SSEWKNPSNC QHQHAFVSVH
     NQEAGLTIAN KGLNEYEILR DGKNTIAITI LRAVRELGDW GYFPTPEAQC LGEQTVHFKI
     IPYGNGSYTD AYQFQIPWVV KQASLHDGDL PLTQTSLEWS GPKLAFSSMK VAEETGDVML
     RWYNLSDEQE TLAIPQPLTF YKSNVLEQES TKLENEISIN KYEIVTIGLK KKESSRP
//
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