KDNA_SHEON
ID KDNA_SHEON Reviewed; 395 AA.
AC Q8EEB1;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=8-amino-3,8-dideoxy-alpha-D-manno-octulosonate transaminase {ECO:0000305};
DE EC=2.6.1.109 {ECO:0000269|PubMed:23413030};
GN Name=kdnA {ECO:0000303|PubMed:23413030};
GN OrderedLocusNames=SO_2476 {ECO:0000312|EMBL:AAN55507.1};
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=MR-1;
RX PubMed=23413030; DOI=10.1074/jbc.m113.453324;
RA Gattis S.G., Chung H.S., Trent M.S., Raetz C.R.;
RT "The origin of 8-amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N) in the
RT lipopolysaccharide of Shewanella oneidensis.";
RL J. Biol. Chem. 288:9216-9225(2013).
CC -!- FUNCTION: Catalyzes the second (last) step of the biosynthesis of Kdo8N
CC (8-amino-3,8-dideoxy-D-manno-octulosonate) from Kdo (3-deoxy-D-manno-
CC octulosonate). {ECO:0000269|PubMed:23413030}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 8-amino-3,8-dideoxy-alpha-D-manno-
CC octulosonate = 3,8-dideoxy-8-oxo-alpha-D-manno-octulosonate + L-
CC glutamate; Xref=Rhea:RHEA:46892, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:87090, ChEBI:CHEBI:87091;
CC EC=2.6.1.109; Evidence={ECO:0000269|PubMed:23413030};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:23413030};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000269|PubMed:23413030}.
CC -!- DISRUPTION PHENOTYPE: A double kdnA/kdnB deletion mutant shows
CC increased sensitivity to polymyxin B and bile salts.
CC {ECO:0000269|PubMed:23413030}.
CC -!- MISCELLANEOUS: Kdo8N is found in lipopolysaccharides of members of the
CC Shewanella genus. {ECO:0000305|PubMed:23413030}.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. {ECO:0000305}.
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DR EMBL; AE014299; AAN55507.1; -; Genomic_DNA.
DR RefSeq; NP_718063.1; NC_004347.2.
DR RefSeq; WP_011072442.1; NZ_CP053946.1.
DR PDB; 5K8B; X-ray; 2.15 A; A/B/C/D=1-395.
DR PDBsum; 5K8B; -.
DR AlphaFoldDB; Q8EEB1; -.
DR SMR; Q8EEB1; -.
DR STRING; 211586.SO_2476; -.
DR PaxDb; Q8EEB1; -.
DR KEGG; son:SO_2476; -.
DR PATRIC; fig|211586.12.peg.2385; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_7_2_6; -.
DR OMA; IMGLNFR; -.
DR OrthoDB; 1722208at2; -.
DR PhylomeDB; Q8EEB1; -.
DR BioCyc; MetaCyc:MON-19349; -.
DR BioCyc; SONE211586:G1GMP-2262-MON; -.
DR BRENDA; 2.6.1.109; 5706.
DR UniPathway; UPA00030; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IBA:GO_Central.
DR CDD; cd00616; AHBA_syn; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244; PTHR30244; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Lipopolysaccharide biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..395
FT /note="8-amino-3,8-dideoxy-alpha-D-manno-octulosonate
FT transaminase"
FT /id="PRO_0000434590"
FT MOD_RES 186
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q8ZNF3"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:5K8B"
FT HELIX 9..20
FT /evidence="ECO:0007829|PDB:5K8B"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:5K8B"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:5K8B"
FT HELIX 38..50
FT /evidence="ECO:0007829|PDB:5K8B"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:5K8B"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:5K8B"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:5K8B"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:5K8B"
FT HELIX 89..96
FT /evidence="ECO:0007829|PDB:5K8B"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:5K8B"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:5K8B"
FT HELIX 114..120
FT /evidence="ECO:0007829|PDB:5K8B"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:5K8B"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:5K8B"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:5K8B"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:5K8B"
FT STRAND 173..181
FT /evidence="ECO:0007829|PDB:5K8B"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:5K8B"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:5K8B"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:5K8B"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:5K8B"
FT HELIX 238..248
FT /evidence="ECO:0007829|PDB:5K8B"
FT HELIX 251..269
FT /evidence="ECO:0007829|PDB:5K8B"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:5K8B"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:5K8B"
FT HELIX 298..310
FT /evidence="ECO:0007829|PDB:5K8B"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:5K8B"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:5K8B"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:5K8B"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:5K8B"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:5K8B"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:5K8B"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:5K8B"
FT HELIX 359..365
FT /evidence="ECO:0007829|PDB:5K8B"
FT STRAND 368..372
FT /evidence="ECO:0007829|PDB:5K8B"
FT HELIX 379..393
FT /evidence="ECO:0007829|PDB:5K8B"
SQ SEQUENCE 395 AA; 43644 MW; 9AE9475E326D240C CRC64;
MPGFELFGPE EKQEVADVME HGFTFRYNFD HMRNDRWKTR DMEQLLCEKM NVKHAHLLSS
GTAALQTAMM AAGIGAGDEV IVPPFTFVAS VEAIFMAGAV PIFAEIDETL CLSPEGIEAV
ITPRTKAINL VHMCGSMAKM DEIKAICKKH NLVLLEDACQ AIGGSYKGQA LGTIGDVGCY
SFDSVKTITC GEGGAVITNN TEIYDNAHMF SDHGHDHIGK DRGAESHPIM GLNFRISEMN
AALGLAQLRK LDTIIDIQRK NKKAIKDAMA SIPEVSFREI PDPEGDSAGF LSFMLPTEAR
TQEISKKLAA NGVDGCFYWY VNNWHYLKNW KHIQELKAPA ALPITLIADR PDYTQISVPK
SDAIMSRTIS MLIKLSWTDA QIAERIENIK KAFAQ
