ID A0A091G5Z3_9AVES Unreviewed; 737 AA.
AC A0A091G5Z3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase {ECO:0000313|EMBL:KFO76736.1};
DE Flags: Fragment;
GN ORFNames=N303_06762 {ECO:0000313|EMBL:KFO76736.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO76736.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO76736.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO76736.1};
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; KL447750; KFO76736.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091G5Z3; -.
DR STRING; 55661.A0A091G5Z3; -.
DR Proteomes; UP000053760; 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:KFO76736.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW Transferase {ECO:0000313|EMBL:KFO76736.1}.
FT DOMAIN 53..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:KFO76736.1"
FT NON_TER 737
FT /evidence="ECO:0000313|EMBL:KFO76736.1"
SQ SEQUENCE 737 AA; 80913 MW; 3B9C280DB305E1B5 CRC64;
EVYFKNLSKQ KQKEIMEKNG NNHKLRVCVA TCNRADYSKL APIMFGIKAE PQFFELDVVV
LGSHLIDDYG NTYRMIEQDD FDIHTRLHTI VRGEDEAAMV ESVGLALVKL PDVLNRLKPD
IMIVHGDRFD ALALATSAAL MNIRILHIEG GEVSGTIDDS IRHAITKLAH YHVCCTRSAE
QHLIAMCEDH DRILLAGCPS YDKLLSAKNK DYMSIIRVWL GEDVKTRDYI VALQHPVTTD
IKHSIKMFEL TLDALISFNK RTLVLFPNVD AGSKEMVRVM RKKGIEHHPN FRAVKHVPFD
QFIQLVAHAG CMIGNSSCGV REVGAFGTPV INLGTRQTGR ETGENVLHVR DADTQDKILH
ALQLQFGKQY PCSKIYGDGN AVPRILKFLK SINLKEPLQK KFCFPPVKDN ISQDIDHILE
TQSALAVDLG GTNLRVAIVS MKGEIVKKYT QLNPKTYEDR LELILKMCIE AASEAVNVNC
RILGVGISTG GRVNPREGIV LHSTKLIQEW SSVDLRTPIS DALHLPVWVD NDGNCAALAE
RKFGHGKGVE NFVTLITGTG IGGGIVHQHE LIHGSSFCAA ELGHIVVSLD GPECLCGSQG
CIEAYASGIA LQREAKKLHD EDLLLVEGMS VKKEEAVSAA HLIQAAKLGN TKADSILRTA
GTALGLGVVN ILHTMNPSLV ILSGVLASHY VNTVKDVINR QALSSVKTVD VVVSNLADPA
LLGAASLVLD YTTRRTY
//
