SACA_NEIMA
ID SACA_NEIMA Reviewed; 372 AA.
AC A0A0U1RGY0;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=UDP-N-acetylglucosamine 2-epimerase {ECO:0000305};
DE Short=UDP-GlcNAc 2-epimerase {ECO:0000303|PubMed:26598987};
DE EC=5.1.3.14 {ECO:0000269|PubMed:26598987};
GN Name=sacA {ECO:0000303|PubMed:26598987};
GN OrderedLocusNames=NMA0199 {ECO:0000312|EMBL:CAM07513.1};
OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS Z2491).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=10761919; DOI=10.1038/35006655;
RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA Barrell B.G.;
RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT Z2491.";
RL Nature 404:502-506(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PATHWAY.
RC STRAIN=M1027 / Serogroup A;
RX PubMed=26598987; DOI=10.1016/j.carres.2015.10.016;
RA Zhang L., Muthana M.M., Yu H., McArthur J.B., Qu J., Chen X.;
RT "Characterizing non-hydrolyzing Neisseria meningitidis serogroup A UDP-N-
RT acetylglucosamine (UDP-GlcNAc) 2-epimerase using UDP-N-acetylmannosamine
RT (UDP-ManNAc) and derivatives.";
RL Carbohydr. Res. 419:18-28(2016).
CC -!- FUNCTION: Catalyzes the interconversion between UDP-N-acetylglucosamine
CC (UDP-GlcNAc) and UDP-N-acetylmannosamine (UDP-ManNAc). Involved in the
CC biosynthesis of the capsular polysaccharides. In vitro, can also use
CC several chemoenzymatically synthesized UDP-ManNAc derivatives as
CC substrates, with lower efficiency. {ECO:0000269|PubMed:26598987}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-
CC mannosamine; Xref=Rhea:RHEA:17213, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:68623; EC=5.1.3.14;
CC Evidence={ECO:0000269|PubMed:26598987};
CC -!- ACTIVITY REGULATION: Activated by UDP-GlcNAc and inhibited by 2-
CC acetamidoglucal and UDP. Activity is strongly decreased in the presence
CC of Co(2+) and abolished in the presence of Mn(2+) or Zn(2+).
CC {ECO:0000269|PubMed:26598987}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.6 mM for UDP-GlcNAc {ECO:0000269|PubMed:26598987};
CC KM=5.2 mM for UDP-ManNAc {ECO:0000269|PubMed:26598987};
CC KM=20 mM for UDP-ManNGc {ECO:0000269|PubMed:26598987};
CC KM=51 mM for UDP-ManNPr {ECO:0000269|PubMed:26598987};
CC KM=63 mM for rUDP-ManNAc {ECO:0000269|PubMed:26598987};
CC Note=kcat is 31 sec(-1) with UDP-GlcNAc as substrate. kcat is 52
CC sec(-1) with UDP-ManNAc as substrate. kcat is 4.2 sec(-1) with UDP-
CC ManNGc as substrate. kcat is 7.8 sec(-1) with UDP-ManNPr as
CC substrate. kcat is 6.7 sec(-1) with rUDP-ManNAc as substrate.
CC {ECO:0000269|PubMed:26598987};
CC pH dependence:
CC Optimum pH is 8-0-9.0. {ECO:0000269|PubMed:26598987};
CC -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC {ECO:0000269|PubMed:26598987}.
CC -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
CC {ECO:0000305}.
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DR EMBL; AL157959; CAM07513.1; -; Genomic_DNA.
DR RefSeq; WP_002236579.1; NC_003116.1.
DR PDB; 6VLB; X-ray; 1.85 A; A/B=1-372.
DR PDB; 6VLC; X-ray; 2.15 A; A/B/C/D=1-372.
DR PDBsum; 6VLB; -.
DR PDBsum; 6VLC; -.
DR AlphaFoldDB; A0A0U1RGY0; -.
DR SMR; A0A0U1RGY0; -.
DR EnsemblBacteria; CAM07513; CAM07513; NMA0199.
DR KEGG; nma:NMA0199; -.
DR HOGENOM; CLU_041674_1_0_4; -.
DR OMA; RYNTERP; -.
DR BioCyc; NMEN122587:NMA_RS01025-MON; -.
DR BRENDA; 5.1.3.14; 16120.
DR UniPathway; UPA00934; -.
DR Proteomes; UP000000626; Chromosome.
DR GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom.
DR InterPro; IPR029767; WecB-like.
DR PANTHER; PTHR43174; PTHR43174; 1.
DR Pfam; PF02350; Epimerase_2; 1.
DR TIGRFAMs; TIGR00236; wecB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsule biogenesis/degradation; Isomerase.
FT CHAIN 1..372
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /id="PRO_0000442460"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27828"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27828"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27828"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27828"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27828"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27828"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27828"
FT BINDING 289..291
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27828"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27828"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27828"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:6VLB"
FT HELIX 10..23
FT /evidence="ECO:0007829|PDB:6VLB"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:6VLB"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:6VLB"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:6VLB"
FT HELIX 67..85
FT /evidence="ECO:0007829|PDB:6VLB"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:6VLB"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:6VLB"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:6VLB"
FT TURN 125..130
FT /evidence="ECO:0007829|PDB:6VLC"
FT HELIX 131..141
FT /evidence="ECO:0007829|PDB:6VLB"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:6VLB"
FT HELIX 150..157
FT /evidence="ECO:0007829|PDB:6VLB"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:6VLB"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:6VLB"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:6VLB"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:6VLB"
FT HELIX 187..196
FT /evidence="ECO:0007829|PDB:6VLB"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:6VLB"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:6VLB"
FT HELIX 219..234
FT /evidence="ECO:0007829|PDB:6VLB"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:6VLB"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:6VLB"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:6VLB"
FT HELIX 272..281
FT /evidence="ECO:0007829|PDB:6VLB"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:6VLB"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:6VLB"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:6VLB"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:6VLB"
FT HELIX 313..318
FT /evidence="ECO:0007829|PDB:6VLB"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:6VLB"
FT HELIX 328..340
FT /evidence="ECO:0007829|PDB:6VLB"
FT HELIX 342..349
FT /evidence="ECO:0007829|PDB:6VLB"
FT HELIX 360..370
FT /evidence="ECO:0007829|PDB:6VLB"
SQ SEQUENCE 372 AA; 41731 MW; E3F9DDBEE6E8821A CRC64;
MKVLTVFGTR PEAIKMAPVI LELQKHNTIT SKVCITAQHR EMLDQVLSLF EIKADYDLNI
MKPNQSLQEI TTNIISSLTD VLEDFKPDCV LVHGDTTTTF AASLAAFYQK IPVGHIEAGL
RTYNLYSPWP EEANRRLTSV LSQWHFAPTE DSKNNLLSES IPSDKVIVTG NTVIDALMVS
LEKLKITTIK KQMEQAFPFI QDNSKVILIT AHRRENHGEG IKNIGLSILE LAKKYPTFSF
VIPLHLNPNV RKPIQDLLSS VHNVHLIEPQ EYLPFVYLMS KSHIILSDSG GIQEEAPSLG
KPVLVLRDTT ERPEAVAAGT VKLVGSETQN IIESFTQLIE YPEYYEKMAN IENPYGIGNA
SKIIVETLLK NR
