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Conserved domains on  [gi|522164509|ref|WP_020675717|]
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pseudaminic acid synthase [Geopsychrobacter electrodiphilus]

Protein Classification

pseudaminic acid synthase( domain architecture ID 11497184)

pseudaminic acid synthase catalyzes the condensation of phosphoenolpyruvate with 2,4-diacetamido-2,4,6-trideoxy-beta-l-altropyranose, forming pseudaminic acid

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PseI TIGR03586
pseudaminic acid synthase; Members of this family are included within the larger pfam03102 ...
16-344 0e+00

pseudaminic acid synthase; Members of this family are included within the larger pfam03102 (NeuB) family. NeuB itself (TIGR03569) is involved in the biosynthesis of neuraminic acid by the condensation of phosphoenolpyruvate (PEP) with N-Acetyl-D-Mannosamine. In an analagous reaction, this enzyme, PseI, condenses PEP with 6-deoxy-beta-L-AltNAc4NAc to generate pseudaminic acid.


:

Pssm-ID: 163337 [Multi-domain]  Cd Length: 327  Bit Score: 566.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509   16 PPFIIAEMSGNHNNSLERALEIVEAAAKSGAHALKLQTYTADTMTLDIAEGEFFIEDpnSLWQGRTLYDLYQEAHTPWEW 95
Cdd:TIGR03586   1 PPFIIAELSANHNGSLERALAMIEAAKAAGADAIKLQTYTPDTITLDSDRPEFIIKG--GLWDGRTLYDLYQEAHTPWEW 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509   96 HKPIFDRCKELGIICFSTPFDATSVDFLEGLDVPCYKIASFENTDIPLIRKVAATGKPMIISTGMATIAELDETVRAVRE 175
Cdd:TIGR03586  79 HKELFERAKELGLTIFSSPFDETAVDFLESLDVPAYKIASFEITDLPLIRYVAKTGKPIIMSTGIATLEEIQEAVEACRE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509  176 AGCKDLILLKCTSTYPATPENTNLLTIPHMRDLFGCEVGLSDHTMGIGGAVAAVALGASVIEKHFTLRRADGGVDSTFSL 255
Cdd:TIGR03586 159 AGCKDLVLLKCTSSYPAPLEDANLRTIPDLAERFNVPVGLSDHTLGILAPVAAVALGACVIEKHFTLDRSDGGVDSAFSL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509  256 EPQEIEALVIESERAWQSLGQISYGPTEKEKNSLVFRRSLYVVRDMMEGEFFTLENMRCIRPGLGLSPKVFDTLLGKRIK 335
Cdd:TIGR03586 239 EPDEFKALVKEVRNAWLALGEVNYELSEKEKKSRQFRRSLYVVKDIKKGETFTEENVRSVRPGFGLHPKYLDEILGKKAN 318

                  ....*....
gi 522164509  336 KSVKKGTPV 344
Cdd:TIGR03586 319 QDIKKGTPL 327
 
Name Accession Description Interval E-value
PseI TIGR03586
pseudaminic acid synthase; Members of this family are included within the larger pfam03102 ...
16-344 0e+00

pseudaminic acid synthase; Members of this family are included within the larger pfam03102 (NeuB) family. NeuB itself (TIGR03569) is involved in the biosynthesis of neuraminic acid by the condensation of phosphoenolpyruvate (PEP) with N-Acetyl-D-Mannosamine. In an analagous reaction, this enzyme, PseI, condenses PEP with 6-deoxy-beta-L-AltNAc4NAc to generate pseudaminic acid.


Pssm-ID: 163337 [Multi-domain]  Cd Length: 327  Bit Score: 566.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509   16 PPFIIAEMSGNHNNSLERALEIVEAAAKSGAHALKLQTYTADTMTLDIAEGEFFIEDpnSLWQGRTLYDLYQEAHTPWEW 95
Cdd:TIGR03586   1 PPFIIAELSANHNGSLERALAMIEAAKAAGADAIKLQTYTPDTITLDSDRPEFIIKG--GLWDGRTLYDLYQEAHTPWEW 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509   96 HKPIFDRCKELGIICFSTPFDATSVDFLEGLDVPCYKIASFENTDIPLIRKVAATGKPMIISTGMATIAELDETVRAVRE 175
Cdd:TIGR03586  79 HKELFERAKELGLTIFSSPFDETAVDFLESLDVPAYKIASFEITDLPLIRYVAKTGKPIIMSTGIATLEEIQEAVEACRE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509  176 AGCKDLILLKCTSTYPATPENTNLLTIPHMRDLFGCEVGLSDHTMGIGGAVAAVALGASVIEKHFTLRRADGGVDSTFSL 255
Cdd:TIGR03586 159 AGCKDLVLLKCTSSYPAPLEDANLRTIPDLAERFNVPVGLSDHTLGILAPVAAVALGACVIEKHFTLDRSDGGVDSAFSL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509  256 EPQEIEALVIESERAWQSLGQISYGPTEKEKNSLVFRRSLYVVRDMMEGEFFTLENMRCIRPGLGLSPKVFDTLLGKRIK 335
Cdd:TIGR03586 239 EPDEFKALVKEVRNAWLALGEVNYELSEKEKKSRQFRRSLYVVKDIKKGETFTEENVRSVRPGFGLHPKYLDEILGKKAN 318

                  ....*....
gi 522164509  336 KSVKKGTPV 344
Cdd:TIGR03586 319 QDIKKGTPL 327
SpsE COG2089
Sialic acid synthase SpsE, contains C-terminal SAF domain [Cell wall/membrane/envelope ...
15-350 0e+00

Sialic acid synthase SpsE, contains C-terminal SAF domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441692 [Multi-domain]  Cd Length: 335  Bit Score: 547.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509  15 HPPFIIAEMSGNHNNSLERALEIVEAAAKSGAHALKLQTYTADTMTLDIAEGEFFIEDpnSLWQGRTLYDLYQEAHTPWE 94
Cdd:COG2089    1 HPPFIIAEIGVNHNGDLELAKELIDAAAEAGADAVKFQTYTADTLTSDSAPKAFYQSG--SLWGGESLYELYKRLELPWE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509  95 WHKPIFDRCKELGIICFSTPFDATSVDFLEGLDVPCYKIASFENTDIPLIRKVAATGKPMIISTGMATIAELDETVRAVR 174
Cdd:COG2089   79 WHKELKEYCKELGIIFFSTPFDEESVDFLEELGVPAYKIASGEITNLPLLRYIAKTGKPIILSTGMATLEEIEEAVEALR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509 175 EAGCKDLILLKCTSTYPATPENTNLLTIPHMRDLFGCEVGLSDHTMGIGGAVAAVALGASVIEKHFTLRRADGGVDSTFS 254
Cdd:COG2089  159 EAGNDQIALLHCTSAYPAPPEDVNLRAIPTLKEAFGVPVGLSDHTLGIEVPIAAVALGASVIEKHFTLDRSLPGPDHAFS 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509 255 LEPQEIEALVIESERAWQSLGQISYGPTEKE-KNSLVFRRSLYVVRDMMEGEFFTLENMRCIRPGLGLSPKVFDTLLGKR 333
Cdd:COG2089  239 LEPDELKAMVEAIRNAEKALGSGIKGPTPSEkKNRRVARRSLVAARDIKAGEVITEENLRVKRPGTGLSPKYLDEVLGKK 318
                        330
                 ....*....|....*..
gi 522164509 334 IKKSVKKGTPVSWDLIG 350
Cdd:COG2089  319 AKRDIKAGTPLTWDDLE 335
NeuB pfam03102
NeuB family; NeuB is the prokaryotic N-acetylneuraminic acid (Neu5Ac) synthase. It catalyzes ...
38-279 1.10e-115

NeuB family; NeuB is the prokaryotic N-acetylneuraminic acid (Neu5Ac) synthase. It catalyzes the direct formation of Neu5Ac (the most common sialic acid) by condensation of phosphoenolpyruvate (PEP) and N-acetylmannosamine (ManNAc). This reaction has only been observed in prokaryotes; eukaryotes synthesize the 9-phosphate form, Neu5Ac-9-P, and utilize ManNAc-6-P instead of ManNAc. Such eukaryotic enzymes are not present in this family. This family also contains SpsE spore coat polysaccharide biosynthesis proteins.


Pssm-ID: 427137  Cd Length: 239  Bit Score: 334.87  E-value: 1.10e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509   38 VEAAAKSGAHALKLQTYTADTMTLDIA-EGEFFIEdpnsLWQGRTLYDLYQEAHTPWEWHKPIFDRCKELGIICFSTPFD 116
Cdd:pfam03102   1 IDAAAEAGADAVKFQTFTAETLVSKEApKADYQIT----TWGGESQYELLKKLELSEEWHKELFEYCREKGIIFLSTPFD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509  117 ATSVDFLEGLDVPCYKIASFENTDIPLIRKVAATGKPMIISTGMATIAELDETVRAVREAGCKDLILLKCTSTYPATPEN 196
Cdd:pfam03102  77 LESVDFLESLGVPAYKIASGEITNLPLLRYIAKTGKPVILSTGMATLGEIEEAVEVLRRAGNEDLTLLHCTSEYPAPFED 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509  197 TNLLTIPHMRDLFGCEVGLSDHTMGIGGAVAAVALGASVIEKHFTLRRADGGVDSTFSLEPQEIEALVIESERAWQSLGQ 276
Cdd:pfam03102 157 VNLRAIPTLKEAFGVPVGYSDHTLGIAAPIAAVALGAKVIEKHFTLDRNLPGPDHAASLEPDELKEMVRAIRNVEKALGD 236

                  ...
gi 522164509  277 ISY 279
Cdd:pfam03102 237 GIK 239
SAF_NeuB_like cd11615
C-terminal SAF domain of sialic acid synthetase; Sialic acid synthetase (N-acetylneuraminate ...
292-349 2.69e-21

C-terminal SAF domain of sialic acid synthetase; Sialic acid synthetase (N-acetylneuraminate synthase or N-acetylneuraminate-9-phosphate synthase) catalyzes the condensation of phosphoenolpyruvate with N-acetylmannosamine (ManNAc, in bacteria) or N-acetylmannosamine-6-phosphate (ManNAc-6P, in mammals), to yield N-acetylneuramic acid (NeuNAc) or N-acetylneuramic acid-9-phosphate (NeuNAc-9P), respectively. The N-terminal NeuB domain, a TIM-barrel-like structure, contains the catalytic site, the function of the SAF domain is not as clear. It may participate in domain-swapped dimerization and play a role in binding the substrate, in either domain-swapped dimers or by directly interacting with the N-terminal domain. Also included in the family are PEP-sugar pyruvyltransferases known as spore coat polysaccharide biosynthesis proteins (SpsE).


Pssm-ID: 212160 [Multi-domain]  Cd Length: 58  Bit Score: 85.85  E-value: 2.69e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 522164509 292 RRSLYVVRDMMEGEFFTLENMRCIRPGLGLSPKVFDTLLGKRIKKSVKKGTPVSWDLI 349
Cdd:cd11615    1 RRSLVAARDIKAGEVLTEENLRVKRPGGGLSPKYLDEVLGKKAKRDIKAGEPLTWDDL 58
SAF smart00858
This domain family includes a range of different proteins. Such as antifreeze proteins and ...
292-349 1.75e-04

This domain family includes a range of different proteins. Such as antifreeze proteins and flagellar FlgA proteins, and CpaB pilus proteins;


Pssm-ID: 214862 [Multi-domain]  Cd Length: 63  Bit Score: 39.09  E-value: 1.75e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522164509   292 RRSLYVVRDMMEGEFFTLENMRCIR------PGLGLSPKvfDTLLGKRIKKSVKKGTPVSWDLI 349
Cdd:smart00858   1 DNVVVAARDLPAGEVITAEDLRLGHvalrdlPGGGLTPY--GQVIGRVARRDIAAGEPITASNL 62
 
Name Accession Description Interval E-value
PseI TIGR03586
pseudaminic acid synthase; Members of this family are included within the larger pfam03102 ...
16-344 0e+00

pseudaminic acid synthase; Members of this family are included within the larger pfam03102 (NeuB) family. NeuB itself (TIGR03569) is involved in the biosynthesis of neuraminic acid by the condensation of phosphoenolpyruvate (PEP) with N-Acetyl-D-Mannosamine. In an analagous reaction, this enzyme, PseI, condenses PEP with 6-deoxy-beta-L-AltNAc4NAc to generate pseudaminic acid.


Pssm-ID: 163337 [Multi-domain]  Cd Length: 327  Bit Score: 566.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509   16 PPFIIAEMSGNHNNSLERALEIVEAAAKSGAHALKLQTYTADTMTLDIAEGEFFIEDpnSLWQGRTLYDLYQEAHTPWEW 95
Cdd:TIGR03586   1 PPFIIAELSANHNGSLERALAMIEAAKAAGADAIKLQTYTPDTITLDSDRPEFIIKG--GLWDGRTLYDLYQEAHTPWEW 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509   96 HKPIFDRCKELGIICFSTPFDATSVDFLEGLDVPCYKIASFENTDIPLIRKVAATGKPMIISTGMATIAELDETVRAVRE 175
Cdd:TIGR03586  79 HKELFERAKELGLTIFSSPFDETAVDFLESLDVPAYKIASFEITDLPLIRYVAKTGKPIIMSTGIATLEEIQEAVEACRE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509  176 AGCKDLILLKCTSTYPATPENTNLLTIPHMRDLFGCEVGLSDHTMGIGGAVAAVALGASVIEKHFTLRRADGGVDSTFSL 255
Cdd:TIGR03586 159 AGCKDLVLLKCTSSYPAPLEDANLRTIPDLAERFNVPVGLSDHTLGILAPVAAVALGACVIEKHFTLDRSDGGVDSAFSL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509  256 EPQEIEALVIESERAWQSLGQISYGPTEKEKNSLVFRRSLYVVRDMMEGEFFTLENMRCIRPGLGLSPKVFDTLLGKRIK 335
Cdd:TIGR03586 239 EPDEFKALVKEVRNAWLALGEVNYELSEKEKKSRQFRRSLYVVKDIKKGETFTEENVRSVRPGFGLHPKYLDEILGKKAN 318

                  ....*....
gi 522164509  336 KSVKKGTPV 344
Cdd:TIGR03586 319 QDIKKGTPL 327
SpsE COG2089
Sialic acid synthase SpsE, contains C-terminal SAF domain [Cell wall/membrane/envelope ...
15-350 0e+00

Sialic acid synthase SpsE, contains C-terminal SAF domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441692 [Multi-domain]  Cd Length: 335  Bit Score: 547.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509  15 HPPFIIAEMSGNHNNSLERALEIVEAAAKSGAHALKLQTYTADTMTLDIAEGEFFIEDpnSLWQGRTLYDLYQEAHTPWE 94
Cdd:COG2089    1 HPPFIIAEIGVNHNGDLELAKELIDAAAEAGADAVKFQTYTADTLTSDSAPKAFYQSG--SLWGGESLYELYKRLELPWE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509  95 WHKPIFDRCKELGIICFSTPFDATSVDFLEGLDVPCYKIASFENTDIPLIRKVAATGKPMIISTGMATIAELDETVRAVR 174
Cdd:COG2089   79 WHKELKEYCKELGIIFFSTPFDEESVDFLEELGVPAYKIASGEITNLPLLRYIAKTGKPIILSTGMATLEEIEEAVEALR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509 175 EAGCKDLILLKCTSTYPATPENTNLLTIPHMRDLFGCEVGLSDHTMGIGGAVAAVALGASVIEKHFTLRRADGGVDSTFS 254
Cdd:COG2089  159 EAGNDQIALLHCTSAYPAPPEDVNLRAIPTLKEAFGVPVGLSDHTLGIEVPIAAVALGASVIEKHFTLDRSLPGPDHAFS 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509 255 LEPQEIEALVIESERAWQSLGQISYGPTEKE-KNSLVFRRSLYVVRDMMEGEFFTLENMRCIRPGLGLSPKVFDTLLGKR 333
Cdd:COG2089  239 LEPDELKAMVEAIRNAEKALGSGIKGPTPSEkKNRRVARRSLVAARDIKAGEVITEENLRVKRPGTGLSPKYLDEVLGKK 318
                        330
                 ....*....|....*..
gi 522164509 334 IKKSVKKGTPVSWDLIG 350
Cdd:COG2089  319 AKRDIKAGTPLTWDDLE 335
NeuB pfam03102
NeuB family; NeuB is the prokaryotic N-acetylneuraminic acid (Neu5Ac) synthase. It catalyzes ...
38-279 1.10e-115

NeuB family; NeuB is the prokaryotic N-acetylneuraminic acid (Neu5Ac) synthase. It catalyzes the direct formation of Neu5Ac (the most common sialic acid) by condensation of phosphoenolpyruvate (PEP) and N-acetylmannosamine (ManNAc). This reaction has only been observed in prokaryotes; eukaryotes synthesize the 9-phosphate form, Neu5Ac-9-P, and utilize ManNAc-6-P instead of ManNAc. Such eukaryotic enzymes are not present in this family. This family also contains SpsE spore coat polysaccharide biosynthesis proteins.


Pssm-ID: 427137  Cd Length: 239  Bit Score: 334.87  E-value: 1.10e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509   38 VEAAAKSGAHALKLQTYTADTMTLDIA-EGEFFIEdpnsLWQGRTLYDLYQEAHTPWEWHKPIFDRCKELGIICFSTPFD 116
Cdd:pfam03102   1 IDAAAEAGADAVKFQTFTAETLVSKEApKADYQIT----TWGGESQYELLKKLELSEEWHKELFEYCREKGIIFLSTPFD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509  117 ATSVDFLEGLDVPCYKIASFENTDIPLIRKVAATGKPMIISTGMATIAELDETVRAVREAGCKDLILLKCTSTYPATPEN 196
Cdd:pfam03102  77 LESVDFLESLGVPAYKIASGEITNLPLLRYIAKTGKPVILSTGMATLGEIEEAVEVLRRAGNEDLTLLHCTSEYPAPFED 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509  197 TNLLTIPHMRDLFGCEVGLSDHTMGIGGAVAAVALGASVIEKHFTLRRADGGVDSTFSLEPQEIEALVIESERAWQSLGQ 276
Cdd:pfam03102 157 VNLRAIPTLKEAFGVPVGYSDHTLGIAAPIAAVALGAKVIEKHFTLDRNLPGPDHAASLEPDELKEMVRAIRNVEKALGD 236

                  ...
gi 522164509  277 ISY 279
Cdd:pfam03102 237 GIK 239
NeuB_NnaB TIGR03569
N-acetylneuraminate synthase; This family is a subset of the pfam03102 and is believed to ...
17-342 5.75e-99

N-acetylneuraminate synthase; This family is a subset of the pfam03102 and is believed to include only authentic NeuB N-acetylneuraminate (sialic acid) synthase enzymes. The majority of the genes identified by this model are observed adjacent to both the NeuA and NeuC genes which together effect the biosynthesis of CMP-N-acetylneuraminate from UDP-N-acetylglucosamine.


Pssm-ID: 274655 [Multi-domain]  Cd Length: 329  Bit Score: 295.65  E-value: 5.75e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509   17 PFIIAEMSGNHNNSLERALEIVEAAAKSGAHALKLQTYTADT-MTLDIAEGEFFIEDPNSlwqGRTLYDLYQEAHTPWEW 95
Cdd:TIGR03569   1 TFIIAEAGVNHNGDLELAKKLVDAAAEAGADAVKFQTFKAEDlVSKNAPKAEYQKINTGA---EESQLEMLKKLELSEED 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509   96 HKPIFDRCKELGIICFSTPFDATSVDFLEGLDVPCYKIASFENTDIPLIRKVAATGKPMIISTGMATIAELDETVRAVRE 175
Cdd:TIGR03569  78 HRELKEYCESKGIEFLSTPFDLESADFLEDLGVPRFKIPSGEITNAPLLKKIARFGKPVILSTGMATLEEIEAALGVLRD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509  176 AGCKD--LILLKCTSTYPATPENTNLLTIPHMRDLFGCEVGLSDHTMGIGGAVAAVALGASVIEKHFTLRRADGGVDSTF 253
Cdd:TIGR03569 158 AGTPDsnITLLHCTTEYPAPFEDVNLNAMDTLKEAFDLPVGYSDHTLGIEAPIAAVALGATVIEKHFTLDKNLPGPDHKA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522164509  254 SLEPQEIEALVIESERAWQSLGQISYGPTEKE-KNSLVFRRSLYVVRDMMEGEFFTLENMRCIRPGLGLSPKVFDTLLGK 332
Cdd:TIGR03569 238 SLEPDELKEMVQGIRNVEKALGDGVKRPTPSEqKNRDVARKSLVAAKDIKKGEIFTEDNLTVKRPGNGISPMEYWEVIGK 317
                         330
                  ....*....|
gi 522164509  333 RIKKSVKKGT 342
Cdd:TIGR03569 318 KASRDYEEDE 327
SAF_NeuB_like cd11615
C-terminal SAF domain of sialic acid synthetase; Sialic acid synthetase (N-acetylneuraminate ...
292-349 2.69e-21

C-terminal SAF domain of sialic acid synthetase; Sialic acid synthetase (N-acetylneuraminate synthase or N-acetylneuraminate-9-phosphate synthase) catalyzes the condensation of phosphoenolpyruvate with N-acetylmannosamine (ManNAc, in bacteria) or N-acetylmannosamine-6-phosphate (ManNAc-6P, in mammals), to yield N-acetylneuramic acid (NeuNAc) or N-acetylneuramic acid-9-phosphate (NeuNAc-9P), respectively. The N-terminal NeuB domain, a TIM-barrel-like structure, contains the catalytic site, the function of the SAF domain is not as clear. It may participate in domain-swapped dimerization and play a role in binding the substrate, in either domain-swapped dimers or by directly interacting with the N-terminal domain. Also included in the family are PEP-sugar pyruvyltransferases known as spore coat polysaccharide biosynthesis proteins (SpsE).


Pssm-ID: 212160 [Multi-domain]  Cd Length: 58  Bit Score: 85.85  E-value: 2.69e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 522164509 292 RRSLYVVRDMMEGEFFTLENMRCIRPGLGLSPKVFDTLLGKRIKKSVKKGTPVSWDLI 349
Cdd:cd11615    1 RRSLVAARDIKAGEVLTEENLRVKRPGGGLSPKYLDEVLGKKAKRDIKAGEPLTWDDL 58
SAF pfam08666
SAF domain; This domain family includes a range of different proteins. Such as antifreeze ...
292-349 5.97e-08

SAF domain; This domain family includes a range of different proteins. Such as antifreeze proteins and flagellar FlgA proteins, and CpaB pilus proteins.


Pssm-ID: 430140 [Multi-domain]  Cd Length: 63  Bit Score: 49.09  E-value: 5.97e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522164509  292 RRSLYVVRDMMEGEFFTLENMRCIRPGL----GLSPKVFDTLLGKRIKKSVKKGTPVSWDLI 349
Cdd:pfam08666   1 DNVVVAARDLPAGEVITADDLTLVRPPLalppGLFPIAYGEVIGKVARRDIAAGEPLTASDL 62
SAF smart00858
This domain family includes a range of different proteins. Such as antifreeze proteins and ...
292-349 1.75e-04

This domain family includes a range of different proteins. Such as antifreeze proteins and flagellar FlgA proteins, and CpaB pilus proteins;


Pssm-ID: 214862 [Multi-domain]  Cd Length: 63  Bit Score: 39.09  E-value: 1.75e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522164509   292 RRSLYVVRDMMEGEFFTLENMRCIR------PGLGLSPKvfDTLLGKRIKKSVKKGTPVSWDLI 349
Cdd:smart00858   1 DNVVVAARDLPAGEVITAEDLRLGHvalrdlPGGGLTPY--GQVIGRVARRDIAAGEPITASNL 62
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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