ID A0A3Q4GQP9_NEOBR Unreviewed; 743 AA.
AC A0A3Q4GQP9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase-like {ECO:0000313|Ensembl:ENSNBRP00000005737.1};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000005737.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000005737.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_006790889.1; XM_006790826.1.
DR AlphaFoldDB; A0A3Q4GQP9; -.
DR STRING; 32507.ENSNBRP00000005737; -.
DR Ensembl; ENSNBRT00000005915.1; ENSNBRP00000005737.1; ENSNBRG00000004501.1.
DR GeneTree; ENSGT00390000017246; -.
DR OMA; HELYFKK; -.
DR OrthoDB; 5489121at2759; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000004501; Expressed in liver and 7 other cell types or tissues.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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 SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000261580}.
FT DOMAIN 57..395
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /evidence="ECO:0000259|Pfam:PF02350"
FT ACT_SITE 538
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-1"
FT BINDING 498
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 510
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 538
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 587
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 590
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT BINDING 590
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 600
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT BINDING 602
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT BINDING 607
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT BINDING 609
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
SQ SEQUENCE 743 AA; 81813 MW; DAE339C614D7225C CRC64;
MEQYFLRMQR NKEKKSMEKM GESNQCKRKL RVCVATCNRA DYSKLAPIMS GIKSHPEDFE
LEVVVLGSHL IDDYGNTFRM IEQDDFDIGS KLHTIVRGED EAAMVESVGL ALVKLPDVIQ
RLKPDILVVH GDRFDALALA TAAALMNIRI LHLEGGEVSG TIDDSIRHAI SKLAHYHACC
TRMAEQHLIA MCEDHSRILL AGCPSYDKLL LSHHREDYMD IIKSWLGDKV QEGDYIVALQ
HPVTTDIQHS IKIYGLMLDA LISFNKKTLI LFPNIDAGSK EMVRVMRRKG IEQHPNFRAV
KHIPFEQFIQ LVSHAGCMIG NSSCGVREAG AFGTPVINLG TRQTGRETGE NVLHVRDADT
HNKIYHALEL QFGKRYPCSK IYGDGNAVPR ILKFLRSIDL DEPLQKTFCF PPVKDPISQD
IDHILETQSA LAVDLGGTNL RVAIVCMRGT IVKKYSQPNP KTFEARMELI LKMCNDAMRD
AVGLNCRILG VGVSTGGRVN PQDGVVLHST KLIQEWSSVD LRTPISDALH LPVWVDNDGN
CAALAERKFG HGKGLENFVT VITGTGIGGG IIHHNELVHG STFCAAELGH IMVSLEGPEC
MCGSRGCIEA YASGMALQRE AKKLHDEDLL KVEGMDMKLS EPITAAHLIS AAKMGNSKAD
AVLTKAATAL GVGIINILHI VNPSQVILSG VLASYYQAPV QHVISQRALF SVQNIKVVTS
DLEEPALLGA ASMVLDYATR RIY
//
