ID   A0A1W2DPV6_9FLAO        Unreviewed;       591 AA.
AC   A0A1W2DPV6;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family {ECO:0000313|EMBL:SMC99439.1};
GN   ORFNames=SAMN02787074_4309 {ECO:0000313|EMBL:SMC99439.1};
OS   Chryseobacterium sp. YR221.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1500293 {ECO:0000313|EMBL:SMC99439.1, ECO:0000313|Proteomes:UP000192341};
RN   [1] {ECO:0000313|EMBL:SMC99439.1, ECO:0000313|Proteomes:UP000192341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR221 {ECO:0000313|EMBL:SMC99439.1,
RC   ECO:0000313|Proteomes:UP000192341};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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DR   EMBL; FWXM01000008; SMC99439.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W2DPV6; -.
DR   STRING; 1500293.SAMN02787074_4309; -.
DR   Proteomes; UP000192341; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd00616; AHBA_syn; 1.
DR   CDD; cd03360; LbH_AT_putative; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR020019; AcTrfase_PglD-like.
DR   InterPro; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR041561; PglD_N.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   NCBIfam; TIGR03570; NeuD_NnaD; 1.
DR   PANTHER; PTHR30244:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF17836; PglD_N; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:SMC99439.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:SMC99439.1}.
FT   DOMAIN          2..69
FT                   /note="PglD N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17836"
FT   ACT_SITE        123
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620019-1"
FT   BINDING         7..9
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620019-2"
FT   BINDING         58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620019-2"
FT   BINDING         132
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620019-2"
FT   SITE            124
FT                   /note="Increases basicity of active site His"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620019-1"
SQ   SEQUENCE   591 AA;  64691 MW;  C93383DF0FB1AA80 CRC64;
     MYLYGASGHG KVVAEVAEEC GYNIKAYIDE NLSKHKILNY PVIHEIPPFD IDVFISIGNN
     KLRKKIVSQN EQFNYATLLH PKAIISKRLQ IGEGTIVMPG VTINAAADIG KHCIINTNAS
     VDHDCIIEDF VHISPNAALA GNVIVGEGTH IGTGASVIQG IKIGEWCTIG AGAVIINDVP
     AGSTVVGNPG KIIKSRSLKI QNSKNMKSKI WLSSPHMGGN ELKYVKEAFD SNWVAPLGPN
     VDGFEQDLEI FLSEDVKIAA LSAGTAALHL ALIECNVSHG DEVICQSMTF SASANPIVYL
     GANPVFIDSE KDTWNMCPVA LQEAIEDRMA KGKKPKAIIV VNLYGMPAKM DEILSIANKY
     DIPLIEDGAE SLGSKYKGKA CGTFGRFGIL SFNGNKIITT SGGGALVCHT DEDKEKTVFL
     STQARDNAPH YQHSEIGYNY RMSNISAGVG RGQMEVLDDR IEGRRKMHDF YCEICKNIEG
     VKVFSEPNSD FYSNHWLSVI TIDETKTSKS YEDLRLAFLS ENIESRPIWK PMHLQPIFED
     APYYGGKVAE DLFGKSLCLP SGSNLSEDDK KRIAKVMVEV FSNKKEYSVL S
//