ID A0A384BCN5_BALAS Unreviewed; 722 AA.
AC A0A384BCN5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase {ECO:0000313|RefSeq:XP_007197054.1};
GN Name=GNE {ECO:0000313|RefSeq:XP_007197054.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007197054.1};
RN [1] {ECO:0000313|RefSeq:XP_007197054.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007197054.1};
RG RefSeq;
RL Submitted (JAN-2023) to UniProtKB.
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DR RefSeq; XP_007197054.1; XM_007196992.1.
DR AlphaFoldDB; A0A384BCN5; -.
DR SMR; A0A384BCN5; -.
DR STRING; 310752.A0A384BCN5; -.
DR KEGG; bacu:103005913; -.
DR CTD; 10020; -.
DR InParanoid; A0A384BCN5; -.
DR OrthoDB; 5489121at2759; -.
DR Proteomes; UP000261681; Unplaced.
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|RefSeq:XP_007197054.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW Transferase {ECO:0000313|RefSeq:XP_007197054.1}.
FT DOMAIN 38..375
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /evidence="ECO:0000259|Pfam:PF02350"
FT ACT_SITE 517
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-1"
FT BINDING 477
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 489
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 517
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 566
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT BINDING 569
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 579
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT BINDING 581
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT BINDING 586
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT BINDING 588
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
SQ SEQUENCE 722 AA; 79394 MW; EEBD70EC15D43009 CRC64;
MEKKENNRKL RVCVATCNRA DYSKLAPIMF GIKMEPEFFE LDVVVLGSHL IDDYGNTYRM
IEQDDFDINT RLHTIVRGED EAAMVESVGL ALVKLPDVLN RLKPDIMIVH GDRFDALALA
TSAALMNIRI LHIEGGEVSG TIDDSIRHAI TKLAHYHVCC TRSAEQHLIS MCEDHDRILL
AGCPSYDKLL SAKNKDYMSI IRMWLGDDVK SKDYIVALQH PVTTDIKHSI KMFELTLDAL
ISFNKRTLVL FPNIDAGSKE MVRVMRKKGI EHHPNFRAVK HVPFDQFIQL VAHAGCMIGN
SSCGVREVGA FGTPVINLGT RQIGRETGEN VLHVRDADTQ DKILQALHLQ FGKQYPCSKI
YGDGNAVPRI LKFLKSIDLQ EPLQKKFCFP PVKDNISQDI DHILETLSAL AVDLGGTNLR
VAIVSMKGEI VKKYTQFNPK TYEERINLIL QMCVEAAAEA VKLNCRILGV GISTGGRVNP
REGIVLHSTK LIQEWNSVDL RTPLSDTLHL PVWVDNDGNC AALAERKFGQ GKGLENFVTL
ITGTGIGGGI IHQHELIHGS SFCAAELGHI VVSLDGPDCS CGSHGCIEAY ASGMALQREA
KKLHDEDQLL VEGMSVPKDE AVGALHLIQA AKLGNAKAQS ILRTAGTALG LGVVNILHTM
NPSLVILSGV LASHYIHTVK DVIRQQALSS VQDVDVVVSD LVEPALLGAA SMVLDYTTRR
IY
//
