ID A0A091NA03_9PASS Unreviewed; 737 AA.
AC A0A091NA03;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase {ECO:0000313|EMBL:KFP73432.1};
DE Flags: Fragment;
GN ORFNames=N310_05295 {ECO:0000313|EMBL:KFP73432.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP73432.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP73432.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP73432.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KK826890; KFP73432.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091NA03; -.
DR Proteomes; UP000053537; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IEA:InterPro.
DR CDD; cd03786; GTB_UDP-GlcNAc_2-Epimerase; 1.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000600; ROK.
DR InterPro; IPR020004; UDP-GlcNAc_Epase.
DR InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom.
DR NCBIfam; TIGR03568; NeuC_NnaA; 1.
DR PANTHER; PTHR18964:SF149; BIFUNCTIONAL UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE_N-ACETYLMANNOSAMINE KINASE; 1.
DR PANTHER; PTHR18964; ROK (REPRESSOR, ORF, KINASE) FAMILY; 1.
DR Pfam; PF02350; Epimerase_2; 1.
DR Pfam; PF00480; ROK; 1.
DR PRINTS; PR00475; HEXOKINASE.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KFP73432.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053537};
KW Transferase {ECO:0000313|EMBL:KFP73432.1}.
FT DOMAIN 52..390
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /evidence="ECO:0000259|Pfam:PF02350"
FT ACT_SITE 532
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-1"
FT BINDING 492
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 504
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 532
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 581
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 584
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT BINDING 584
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 594
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT BINDING 596
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT BINDING 601
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT BINDING 603
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP73432.1"
FT NON_TER 737
FT /evidence="ECO:0000313|EMBL:KFP73432.1"
SQ SEQUENCE 737 AA; 80868 MW; 5A52F001F56AF69C CRC64;
EVYFKNLSKQ KQKEVMEKNG NNHKLHVCVA TCNRADYSKL APIMFGIKAE PQSFELDVIV
LGSHLIDDYG NTYRMIEQDD FDIHTRLHTI VRGEDEAAMV ESVGLALVKL PDVLNRLKPD
IMIVHGDRFD ALALATSAAL MNIRILHIEG GEVSGTIDDS IRHAITKLAH YHVCCTRSAE
QHLIAMCEDH DRILLAGCPS YDKLLSAKNK DYMSIISMWL GEDVKTRDYI VALQHPVTTD
IKHSIKMFEL TLDALISFNK RTLVLFPNVD AGSKEMVRVM RKKGIEHHPN FRAVKHVPFD
QFIQLVAHAG CMIGNSSCGV REVGAFGTPV INLGTRQTGR ETGENVLHVR DADTQDKILH
ALQLQFGKQY PCSKIYGDGN AVPRILKFLK SIDLKEPLQK KFCFPPVKDN ISQDIDHILE
TQSALAVDLG GTNLRVAIVS MKGEIVKKYT QLNPKTYEDR LELILKMCIE AASEAVNVNC
RILGVGISTG GRVNPREGIV LHSTKLIQEW SSVDLRTPIS DALHLPVWVD NDGNCAALAE
RKFGHGKGIE NFVTLITGTG IGGGIIHQHE LIHGSSFCAA ELGHIVVSLE GPECLCGSQG
CIEAYASGIA LQREAKKLHD EDLLLVEGMS MKKEEVVSAA HLIQAAKLGN TKAESILRTA
GTALGLGVVN ILHTMNPSLV ILSGVLASHY VNAVKDVINR QALSSAKTVD VVVSNLADPA
LLGAASLVLD YTTRRIY
//
