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Database: UniProt
Entry: K2NSH1_9LACT
LinkDB: K2NSH1_9LACT
Original site: K2NSH1_9LACT 
ID   K2NSH1_9LACT            Unreviewed;       869 AA.
AC   K2NSH1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Glycosyl hydrolase, family 38 {ECO:0000313|EMBL:EKF50513.1};
GN   ORFNames=C426_2088 {ECO:0000313|EMBL:EKF50513.1};
OS   Lactococcus garvieae DCC43.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1231377 {ECO:0000313|EMBL:EKF50513.1, ECO:0000313|Proteomes:UP000006787};
RN   [1] {ECO:0000313|EMBL:EKF50513.1, ECO:0000313|Proteomes:UP000006787}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DCC43 {ECO:0000313|EMBL:EKF50513.1,
RC   ECO:0000313|Proteomes:UP000006787};
RX   PubMed=23209230; DOI=10.1128/JB.01864-12;
RA   Gabrielsen C., Brede D.A., Hernandez P.E., Nes I.F., Diep D.B.;
RT   "Genome Sequence of the Bacteriocin-Producing Strain Lactococcus garvieae
RT   DCC43.";
RL   J. Bacteriol. 194:6976-6977(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:EKF50513.1}.
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DR   EMBL; AMQS01000041; EKF50513.1; -; Genomic_DNA.
DR   RefSeq; WP_003136720.1; NZ_AMQS01000041.1.
DR   AlphaFoldDB; K2NSH1; -.
DR   PATRIC; fig|1231377.3.peg.2070; -.
DR   eggNOG; COG0383; Bacteria.
DR   Proteomes; UP000006787; 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   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; 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; 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:0000313|EMBL:EKF50513.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          274..352
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   869 AA;  99335 MW;  C67903C5DAB11BE3 CRC64;
     MKKKVHIVNH THWDREWYFT TMDAFLLSDN LFNNVIEELL ENPEAKFCLD GQSSILDDYM
     RLNPHQLENV KNLVANKQLS IGPWYTQTDA FFVDEESFIR NMIIGIRDSR KYGKEMEIGY
     LPDTFGHNAQ WPTILQHCGL DNIVFWRGLN IEKHTKSPYF KWKGLGDKTI TAMNLVDGYG
     AVAFLKDEPE YIEERLIPAV KRTEKWTDLD EMLLTSGGDQ TEIIKGLPQT LREISKKTDY
     DFIESSYEDY LEILKSKANL PEYRGEFREP CTTRAHKSIG SVRYDIKRTN FIIEQKLLKR
     VEPLLAIGKA HGITLSTETL VIAWKKILEG HAHDSMGGCV SDDVAVDILH RMKEAEELAD
     GMENYIVKRL SEKFGLSDKE VLVFNTTSKD FKGYKQIDFL APNKNVTLSG VNEMVIIGEE
     HFAGKDNLLL ETPEGNKYIN EDPYYRLYAL ANVSIPSMGF KIFTIEDTDK EAESLIAATD
     VAIMNEFYTI VNEGGQLNLI TQDGVHLENF IEFEDMGNDG DTYDFSPLKD DKPIILNLTD
     SQVKKSSLVE QMILTGKFQL PKTLENRLET RVHGTLDMQL TLSLRKDSEL IDGQLTINNQ
     VLSHRLRLKI NTGVENTRTI ASLPYGFINR EALTKEIPNW FKSYVEYPID LEPFDKSVSV
     ENEQYHISAF GKGLKEYQFQ EGSLYLTLIA TTSQLGKPNL AYRPGRASGD TTKKGHVMMP
     TPMAELLGEQ NFEFALVLSS QAFDEHKASE QWAEYTSANI AYQNQVLNKF IHRLDNKIQA
     NDERLARVEE FSLLKIEGQA FDTTFMPSLY DNEAEVLRLA NPTAKPLAIG HLDFTKYAKY
     EFVNAQETIV DSSTVIAPYD MVSIKLWRK
//
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