ID A0A1Q7QK39_9CHLR Unreviewed; 1011 AA.
AC A0A1Q7QK39;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AUI58_04375 {ECO:0000313|EMBL:OLD52121.1};
OS Chloroflexi bacterium 13_1_40CM_2_70_6.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1805070 {ECO:0000313|EMBL:OLD52121.1, ECO:0000313|Proteomes:UP000185765};
RN [1] {ECO:0000313|EMBL:OLD52121.1, ECO:0000313|Proteomes:UP000185765}
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:OLD52121.1}.
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DR EMBL; MNHK01000059; OLD52121.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7QK39; -.
DR Proteomes; UP000185765; 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 CDD; cd01610; PAP2_like; 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 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 29..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..191
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT DOMAIN 489..557
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1011 AA; 110536 MW; C7708F0C6489F7C7 CRC64;
MDELLRALGS IDTQLYLGIV RARNPALDAL AVAVYLLNWN GFVWWVAGLL VARARGFGRR
GLWAALTIYL GLVDGWIVAE LAKLVFRRAR PFDVLVLPPR DLTPPYDIRV PPAIAPDTLI
PHPTSFSFPS GDAAFAFGAA VALASVAPRF RVLALLFAVA ASLSRVVVGA HYPFDVLAGA
AVGIASGLLA PRAVAAVRRR QRWRAFVIPH THWDREWYER FEGYRARLVP MVSKLLDLLE
RDPAFRSFTF DGQTIAIQDH LEKRPADRSR VEQLVRAERL FIGPWHVLAD LILVSGESIV
RNLQEGLRSA GELGRASRVA YVADPFGHPA QIPQILRGFG YETYVFARGM GDETEDVGAE
FQWEGPSGDR VRATHLIDHY SNGLRIVGPA DEPPESLRRR LTRELPGILD RTTSYANGDA
LLFMVGDDHV EAYPRLPEAV AAMRALAPRV DARIASLEEY AAAAPVPRGV VRGEIVRGRY
RPILRGVNST RVWIKQENVA CERLLLERCE PLDALTGGTA REELRELWRM LLQNHPHDSI
CGCSIDAVHD IDMPPRFAFV RERGTALAER LVVRLSGAGD VAMTWNALPW ERDAVVEAAG
RRVRVRCAAL GLAPAEALPV GGARMAGEGI VENEHLRVEV DRDGSFVVVD RATGERSGRQ
NWLLDEGDRG DEYTYSYAGP TLGSRDVPGQ RTTSAAAERA AVSVSLVLRL PAALRGDRLA
RSPELVDCPV RMTISLDSGA RRVDVAVTVD NRARDHRLRV LCETGTRTLT HRAGAAFALI
ERANRPPIGR GWIEPATYDA CVHDLVAVSG ATRGLAVGVD GLREYAVLHD GRTIAITLLR
AVGFLSRGDL PERRIHAGPE LATPSAQCEG ERAYRYCLVP LDARTGLADA ERAIREWLSP
PLVLHGDGAT RSYLSFVDAR TPLVLSALRA GPDGALVVRV ANPTGEAASN GLRFARDVRA
ARAVDLREGD LTLGNTGLDV IRTAAPAEVE GAVMTVRLQP YEIGTWLVDL A
//
