ID K7SNW6_ACIA4 Unreviewed; 1034 AA.
AC K7SNW6;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Glycosyl hydrolase family 38 N-terminal domain-containing protein {ECO:0000313|EMBL:AFV90875.1};
GN OrderedLocusNames=PACID_31150 {ECO:0000313|EMBL:AFV90875.1};
OS Acidipropionibacterium acidipropionici (strain ATCC 4875 / DSM 20272 / JCM
OS 6432 / NBRC 12425 / NCIMB 8070 / 4) (Propionibacterium acidipropionici).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Acidipropionibacterium.
OX NCBI_TaxID=1171373 {ECO:0000313|EMBL:AFV90875.1, ECO:0000313|Proteomes:UP000000214};
RN [1] {ECO:0000313|EMBL:AFV90875.1, ECO:0000313|Proteomes:UP000000214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 4875 / DSM 20272 / JCM 6432 / NBRC 12425 / NCIMB 8070
RC {ECO:0000313|Proteomes:UP000000214};
RX PubMed=23083487; DOI=10.1186/1471-2164-13-562;
RA Parizzi L.P., Grassi M.C., Llerena L.A., Carazzolle M.F., Queiroz V.L.,
RA Lunardi I., Zeidler A.F., Teixeira P.J., Mieczkowski P., Rincones J.,
RA Pereira G.A.;
RT "The genome sequence of Propionibacterium acidipropionici provides insights
RT into its biotechnological and industrial potential.";
RL BMC Genomics 13:562-562(2012).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
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DR EMBL; CP003493; AFV90875.1; -; Genomic_DNA.
DR RefSeq; WP_015071769.1; NC_019395.1.
DR AlphaFoldDB; K7SNW6; -.
DR STRING; 1171373.PACID_31150; -.
DR KEGG; pbo:PACID_31150; -.
DR PATRIC; fig|1171373.8.peg.3060; -.
DR eggNOG; COG0383; Bacteria.
DR HOGENOM; CLU_003442_0_1_11; -.
DR Proteomes; UP000000214; Chromosome.
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; cd10789; GH38N_AMII_ER_cytosolic; 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; 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:SF1; ALPHA-MANNOSIDASE 2C1; 1.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF17677; Glyco_hydro38C2; 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:AFV90875.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 534..612
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
FT REGION 38..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1034 AA; 113078 MW; E0329D606EE61B85 CRC64;
MHDSAAVLDA RVRRHLAEKI RPAETTVVGG LDVARAQVTD PAGSTNPSAR PGAVGQGEPI
SPAEGLALDY EPFETGRSWG PPWGTTWLRL RATVPPEVRG EHLELVLDLG GEYDSPGFQC
EGLVFRPDGS VVKGLNPRNT WIPAEPDGDG RIEIYVEAAS NPVLLGTPPF QPTEDGDKLT
ASQAPYYVLR RADLVIVHDQ VRELIADVVT LSGLARELPE DSERAWEIRR ALDRALDRLD
LWDIPATASA SRAQLAAMLA RPAAASAQLM GAVGHAHIDS AWLWPLRETR RKVARTVANQ
LNLIADHPEH IFAFPAAQHW TWLQADHPEL FARLIDAVEA GNVVPVGGMW VESDANLPGG
EAMCRQLLYG QRYFIDNVGR PCEEVWLPDS FGYSGALPQL AKLAGARWFL TQKISWNQVD
RFPHHSFWWE GIDGTRIFTH FPPADTYGSD LSAHDLEHAR SNFADKGRSS TSLLLFGYGD
GGGGPTREML AQAARTADLD GLPRVRIETP QDFFARAELQ HENPAVWAGE LYLELHRGTF
TNQARVKAAN RRNEHLLREA ELWCATAAVR GLMPYPGQRL AEIWREVCLY QFHDILPGTA
IAWVYREVIA AHAAISTELE TMIDEAQRLL ARSGDAGVSG DAVVFDASPV TRADMTSTPM
GASVVSPVAG EVRLEPLETG FAVDNGLIRL IVDTQGKVEH LVDLASGRDV IPPGVLGNTL
EIHPDFPNQW DGWDIDIFAT DTTVMSGPGR ARASRADDGS VEIATTVEFD RSTAVQTLTV
RPGEPRLGCH VHVDWHERDA LLKLSWPLDV HTDHASYEIE MGHLTRPTHT NTSWDAYRFE
VHAHRWVHVG EPGFGVAIAN AQTYGWSVDR HERRGGGTYS TARASLLKGA RYPDPRGDEG
EHDLDFTIHP GAGIREAVAD GYALNLPVRV VPGGPVEPLI RVDGDVAVEA VKLAEDGSGD
VVVRLYEPYG ARASADLRLG FEADEAVETD LLEEPLAGNP HAQVAPTAVT GALSGGRVQV
ALRPFQVATI RFRR
//
