ID A0A1Q7EY71_9CHLR Unreviewed; 1001 AA.
AC A0A1Q7EY71;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AUH33_05335 {ECO:0000313|EMBL:OLC19652.1};
OS Chloroflexi bacterium 13_1_40CM_68_21.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1805084 {ECO:0000313|EMBL:OLC19652.1, ECO:0000313|Proteomes:UP000185570};
RN [1] {ECO:0000313|EMBL:OLC19652.1, ECO:0000313|Proteomes:UP000185570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLC19652.1}.
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DR EMBL; MNEO01000070; OLC19652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7EY71; -.
DR Proteomes; UP000185570; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 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 InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
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; PF07748; Glyco_hydro_38C; 1.
DR Pfam; PF01074; Glyco_hydro_38N; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 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:ARBA00023295};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..180
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT DOMAIN 478..546
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1001 AA; 109627 MW; 7BE9399905672390 CRC64;
MNDILGALGA FDTQLYLALA AQRNVVTSVI AVSLTYLNWN GFFWWILAFL LLRSRGLTRR
GITATATAVI GLVDAWAFAE ILKLVVRRPR PFDAIPNAPG GLPAPETVVA HPSSFSFPSG
DAALAMGAAV AFAYVTPRFR VPILLLGVAA SLARLVVGVH YPFDVLGGMT IGIVSGLAAP
RAIALLRRRL RWRAFVIPHT HWDREWYERF EGYRARLVPM VSRLLDILER DTEFRSFTFD
GQTIAIQDYL EKRPADRPRV EALVKGERLL IGPWHVLADL LLVSGESILR NLQEGLRSAG
ELGRAARVAY VADPFGHPAQ LPQVLRGFGY DTYVFARGMG DEGESVGSEF WWEAPSGDRV
RAAHLVDHYS NALALVGPAD EAPASLRRRV AAQTARILDR LTPYANGDAL LLMVGDDHVD
AYPRLPEAVR AMREVFPNVD FRIASLEEYA TAMPPLQHAV SGEIASGRYR PILRGVNSTR
VWIKQENVAC ERLLLERCEP LDALTGGTAR DELRELWRML LQNHPHDSIC GCSIDAVHEI
DMAPRFAYVR QRGEALAARL AARLAGVGDV PMLWDPLPWP REAVIEVDGR PTRVQTGGLG
VAPVVRPAGA DVRVDGDGAI LNDHLRVEVE PDGSFVIVDR EMARRSGRMN VIISEGDRGD
EYTYSYAGPT MGSRGIVGSR SATVSGDRAT VTVDLVLRLP AGLRDDRLAR SPDLVDCPVR
AAISLDADEY RVDVSLTVRN QARDHRLRVL CETGTRALTH HAGAAFATIE RLNRFPVRRG
WIEPASAEAC LHDFVAVKGG TSGLAVGVDG LREYSVLHDG GTIAITLLRA VGFLSRGDLP
ERRGHAGPEL ATPSAQCIGE RIYRYTLVPL DEDLDIDSAA ATVREWLSPP WLVRGDGAPR
TLMSLADPYN TPVVLSALRA GPDGKLVIRL VNPHPKEARA EVRFARPILS SRPLDLREGE
TNLGNTGLDV MRTAAPLETE GDLARVQLQP FEIGTWLVQL G
//
