ID Q4A6K4_MYCS5 Unreviewed; 296 AA.
AC Q4A6K4;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 2.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Acylneuraminate lyase {ECO:0000313|EMBL:AAZ43617.2};
DE EC=4.1.3.3 {ECO:0000313|EMBL:AAZ43617.2};
GN Name=nanA {ECO:0000313|EMBL:AAZ43617.2};
GN OrderedLocusNames=MS53_0198 {ECO:0000313|EMBL:AAZ43617.2};
OS Mycoplasmopsis synoviae (strain 53) (Mycoplasma synoviae).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Metamycoplasmataceae;
OC Mycoplasmopsis.
OX NCBI_TaxID=262723 {ECO:0000313|EMBL:AAZ43617.2, ECO:0000313|Proteomes:UP000000549};
RN [1] {ECO:0000313|EMBL:AAZ43617.2, ECO:0000313|Proteomes:UP000000549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=53 {ECO:0000313|EMBL:AAZ43617.2,
RC ECO:0000313|Proteomes:UP000000549};
RX PubMed=16077101; DOI=10.1128/JB.187.16.5568-5577.2005;
RA Vasconcelos A.T., Ferreira H.B., Bizarro C.V., Bonatto S.L., Carvalho M.O.,
RA Pinto P.M., Almeida D.F., Almeida L.G., Almeida R., Alves-Filho L.,
RA Assuncao E.N., Azevedo V.A., Bogo M.R., Brigido M.M., Brocchi M.,
RA Burity H.A., Camargo A.A., Camargo S.S., Carepo M.S., Carraro D.M.,
RA de Mattos Cascardo J.C., Castro L.A., Cavalcanti G., Chemale G.,
RA Collevatti R.G., Cunha C.W., Dallagiovanna B., Dambros B.P.,
RA Dellagostin O.A., Falcao C., Fantinatti-Garboggini F., Felipe M.S.,
RA Fiorentin L., Franco G.R., Freitas N.S., Frias D., Grangeiro T.B.,
RA Grisard E.C., Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A.,
RA Laurino J.P., Lima L.F., Lopes M.I., Loreto E.L., Madeira H.M.,
RA Manfio G.P., Maranhao A.Q., Martinkovics C.T., Medeiros S.R., Moreira M.A.,
RA Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C., Paixao R.F.,
RA Pedrosa F.O., Pena S.D., Pereira M., Pereira-Ferrari L., Piffer I.,
RA Pinto L.S., Potrich D.P., Salim A.C., Santos F.R., Schmitt R.,
RA Schneider M.P., Schrank A., Schrank I.S., Schuck A.F., Seuanez H.N.,
RA Silva D.W., Silva R., Silva S.C., Soares C.M., Souza K.R., Souza R.C.,
RA Staats C.C., Steffens M.B., Teixeira S.M., Urmenyi T.P., Vainstein M.H.,
RA Zuccherato L.W., Simpson A.J., Zaha A.;
RT "Swine and poultry pathogens: the complete genome sequences of two strains
RT of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae.";
RL J. Bacteriol. 187:5568-5577(2005).
RN [2] {ECO:0007829|PDB:4N4P, ECO:0007829|PDB:4N4Q}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
RX PubMed=24813614; DOI=10.1016/j.cell.2014.03.038;
RA Georgescauld F., Popova K., Gupta A.J., Bracher A., Engen J.R.,
RA Hayer-Hartl M., Hartl F.U.;
RT "GroEL/ES chaperonin modulates the mechanism and accelerates the rate of
RT TIM-barrel domain folding.";
RL Cell 157:922-934(2014).
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; AE017245; AAZ43617.2; -; Genomic_DNA.
DR RefSeq; WP_041351880.1; NC_007294.1.
DR PDB; 4N4P; X-ray; 1.80 A; A/B/C/D=1-296.
DR PDB; 4N4Q; X-ray; 2.00 A; A/B/C/D=1-296.
DR PDBsum; 4N4P; -.
DR PDBsum; 4N4Q; -.
DR AlphaFoldDB; Q4A6K4; -.
DR SMR; Q4A6K4; -.
DR STRING; 262723.MS53_0198; -.
DR KEGG; msy:MS53_0198; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_6_0_14; -.
DR OrthoDB; 9782828at2; -.
DR Proteomes; UP000000549; Chromosome.
DR GO; GO:0008747; F:N-acetylneuraminate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR PANTHER; PTHR42849; N-ACETYLNEURAMINATE LYASE; 1.
DR PANTHER; PTHR42849:SF1; N-ACETYLNEURAMINATE LYASE; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4N4P, ECO:0007829|PDB:4N4Q};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW Reference proteome {ECO:0000313|Proteomes:UP000000549}.
FT ACT_SITE 139
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 167
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 51
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT BINDING 208
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 296 AA; 33607 MW; C6ADA4F3D1F3991A CRC64;
MHNFDKFKGL FPAMVTPFTK DGKLHKAGVK EVVNFLVEKQ KVDGIYITGS TGEFLLLSFE
DKKEVMKLVA EANAGRVTLI AQIGSLNIEE TKELAKLAKE LKYDAISAIT PYYYNFSFNE
THHYYEEISK AADIPMLIYY LPQLAGQKVS TDQFGKLLEI KNVIGSKYGA TDLFAFERLM
SKYPDKLFMF AWDEALAMGL TMGAKGFIGS TYNVNAKGAN AIIKAWEAND KEAVMKLTHT
YNDYVLDLIS KGLMQSLKAI MRLHGVDAGY TRKPFWRYED EEIKKHAEFI TDKYLK
//
