ID A0A1F1E7U6_9PORP Unreviewed; 474 AA.
AC A0A1F1E7U6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Glycosyl hydrolase {ECO:0000313|EMBL:OFR38398.1};
GN ORFNames=HMPREF2890_02750 {ECO:0000313|EMBL:OFR38398.1};
OS Porphyromonas sp. HMSC065F10.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1739394 {ECO:0000313|EMBL:OFR38398.1, ECO:0000313|Proteomes:UP000177035};
RN [1] {ECO:0000313|EMBL:OFR38398.1, ECO:0000313|Proteomes:UP000177035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC065F10 {ECO:0000313|EMBL:OFR38398.1,
RC ECO:0000313|Proteomes:UP000177035};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911};
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. Glycosyl hydrolase 109
CC subfamily. {ECO:0000256|ARBA:ARBA00009329}.
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:OFR38398.1}.
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DR EMBL; LTXH01000092; OFR38398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F1E7U6; -.
DR STRING; 1739394.HMPREF2890_02750; -.
DR OrthoDB; 9771072at2; -.
DR Proteomes; UP000177035; Unassembled WGS sequence.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR049303; Glyco_hydro_109_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43818; BCDNA.GH03377; 1.
DR PANTHER; PTHR43818:SF1; GLYCOSYL HYDROLASE FAMILY 109 PROTEIN; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF21252; Glyco_hydro_109_C; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OFR38398.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000177035};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..474
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009468477"
FT DOMAIN 63..189
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 200..343
FT /note="Glycosyl hydrolase 109 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21252"
SQ SEQUENCE 474 AA; 53851 MW; 31BCE72ABB18CE60 CRC64;
MMKYLAAALL SALMISPAMA QNCCAKKGGQ EKSCSRMIQT NVPERPAGQQ DMLAFRAPKL
QTVRIGIIGL GMRGVSAVDR LSVIEGTDVV ALCDLHQDRA EKSNAILEKN GRHSAALYYG
SEDAWKKLVE RPDLDLIYIV TDWQTHVEMA KYAMEQGKHV AVEVPAAFSM DDIWTLIDTS
ERTRKHCMML ENCVYDFFEM TTLNMKNKGL LGDIVYAEGG YIHNLEEFWP YYEGDWRMDY
NIKHRGDVYP THGMGPAAQI LDLHRGDKMN VLVSMDTTPR NLPAYLEEVR GVKDAKVANG
QHTMTMIRTE KGRTIFIHHD VTTHRPYSRQ YNVAGTKGYA SKYPAEHYAF AGTDLKEAGM
PAVDDLSTHS WVSPEMQKEL YEKYKHPITR ELEKRAKEVG GHGGMDFIMD YRLIYCLRNG
LPLDMDVYDM AEWCSLIPLS QISLEHGFAP VEVPDFTRGA WQRLQGYHHY MIGD
//
