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Conserved domains on  [gi|2200029178|ref|WP_239940530|]
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pseudaminic acid synthase [Vibrio chagasii]

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 ...
18-343 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: 613.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178  18 PYIIAELSANHNGDINRAFQIMEEAKKAGADAIKLQTYTHETITMDCDSEEFQIHGGLWDGQTLYNLYKGAHMPWEWHKP 97
Cdd:TIGR03586   2 PFIIAELSANHNGSLERALAMIEAAKAAGADAIKLQTYTPDTITLDSDRPEFIIKGGLWDGRTLYDLYQEAHTPWEWHKE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178  98 LFEKAKELGITIFSSPFDFTAVDLLESLDAPAYKIASFEVVDLPLIKRVAQTGKPMIISTGMANEAEIEEAIKTARENGC 177
Cdd:TIGR03586  82 LFERAKELGLTIFSSPFDETAVDFLESLDVPAYKIASFEITDLPLIRYVAKTGKPIIMSTGIATLEEIQEAVEACREAGC 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178 178 KELVVLHCVSGYPAPAEQYNLKTIADIAERFNVLSGLSDHTIDNATAVASVTLGACLIEKHVTMDRNGGGADDSFSLEPH 257
Cdd:TIGR03586 162 KDLVLLKCTSSYPAPLEDANLRTIPDLAERFNVPVGLSDHTLGILAPVAAVALGACVIEKHFTLDRSDGGVDSAFSLEPD 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178 258 ELMALCKDTKTAWQAMGQVNYERTEAEKGNVKFRRSLYVVKDIARGESLTSENVRSIRPGFGLAPKHYEEVLGKAATVDI 337
Cdd:TIGR03586 242 EFKALVKEVRNAWLALGEVNYELSEKEKKSRQFRRSLYVVKDIKKGETFTEENVRSVRPGFGLHPKYLDEILGKKANQDI 321

                  ....*.
gi 2200029178 338 RRGTPL 343
Cdd:TIGR03586 322 KKGTPL 327
 
Name Accession Description Interval E-value
PseI TIGR03586
pseudaminic acid synthase; Members of this family are included within the larger pfam03102 ...
18-343 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: 613.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178  18 PYIIAELSANHNGDINRAFQIMEEAKKAGADAIKLQTYTHETITMDCDSEEFQIHGGLWDGQTLYNLYKGAHMPWEWHKP 97
Cdd:TIGR03586   2 PFIIAELSANHNGSLERALAMIEAAKAAGADAIKLQTYTPDTITLDSDRPEFIIKGGLWDGRTLYDLYQEAHTPWEWHKE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178  98 LFEKAKELGITIFSSPFDFTAVDLLESLDAPAYKIASFEVVDLPLIKRVAQTGKPMIISTGMANEAEIEEAIKTARENGC 177
Cdd:TIGR03586  82 LFERAKELGLTIFSSPFDETAVDFLESLDVPAYKIASFEITDLPLIRYVAKTGKPIIMSTGIATLEEIQEAVEACREAGC 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178 178 KELVVLHCVSGYPAPAEQYNLKTIADIAERFNVLSGLSDHTIDNATAVASVTLGACLIEKHVTMDRNGGGADDSFSLEPH 257
Cdd:TIGR03586 162 KDLVLLKCTSSYPAPLEDANLRTIPDLAERFNVPVGLSDHTLGILAPVAAVALGACVIEKHFTLDRSDGGVDSAFSLEPD 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178 258 ELMALCKDTKTAWQAMGQVNYERTEAEKGNVKFRRSLYVVKDIARGESLTSENVRSIRPGFGLAPKHYEEVLGKAATVDI 337
Cdd:TIGR03586 242 EFKALVKEVRNAWLALGEVNYELSEKEKKSRQFRRSLYVVKDIKKGETFTEENVRSVRPGFGLHPKYLDEILGKKANQDI 321

                  ....*.
gi 2200029178 338 RRGTPL 343
Cdd:TIGR03586 322 KKGTPL 327
SpsE COG2089
Sialic acid synthase SpsE, contains C-terminal SAF domain [Cell wall/membrane/envelope ...
18-349 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: 569.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178  18 PYIIAELSANHNGDINRAFQIMEEAKKAGADAIKLQTYTHETITMDCDSEEFQIHGGLWDGQTLYNLYKGAHMPWEWHKP 97
Cdd:COG2089     3 PFIIAEIGVNHNGDLELAKELIDAAAEAGADAVKFQTYTADTLTSDSAPKAFYQSGSLWGGESLYELYKRLELPWEWHKE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178  98 LFEKAKELGITIFSSPFDFTAVDLLESLDAPAYKIASFEVVDLPLIKRVAQTGKPMIISTGMANEAEIEEAIKTARENGC 177
Cdd:COG2089    83 LKEYCKELGIIFFSTPFDEESVDFLEELGVPAYKIASGEITNLPLLRYIAKTGKPIILSTGMATLEEIEEAVEALREAGN 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178 178 KELVVLHCVSGYPAPAEQYNLKTIADIAERFNVLSGLSDHTIDNATAVASVTLGACLIEKHVTMDRNGGGADDSFSLEPH 257
Cdd:COG2089   163 DQIALLHCTSAYPAPPEDVNLRAIPTLKEAFGVPVGLSDHTLGIEVPIAAVALGASVIEKHFTLDRSLPGPDHAFSLEPD 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178 258 ELMALCKDTKTAWQAMGQVNYERTEAEKGN-VKFRRSLYVVKDIARGESLTSENVRSIRPGFGLAPKHYEEVLGKAATVD 336
Cdd:COG2089   243 ELKAMVEAIRNAEKALGSGIKGPTPSEKKNrRVARRSLVAARDIKAGEVITEENLRVKRPGTGLSPKYLDEVLGKKAKRD 322
                         330
                  ....*....|...
gi 2200029178 337 IRRGTPLSRDLFE 349
Cdd:COG2089   323 IKAGTPLTWDDLE 335
NeuB pfam03102
NeuB family; NeuB is the prokaryotic N-acetylneuraminic acid (Neu5Ac) synthase. It catalyzes ...
40-274 3.64e-119

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: 343.73  E-value: 3.64e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178  40 EEAKKAGADAIKLQTYTHETIT-MDCDSEEFQIHggLWDGQTLYNLYKGAHMPWEWHKPLFEKAKELGITIFSSPFDFTA 118
Cdd:pfam03102   2 DAAAEAGADAVKFQTFTAETLVsKEAPKADYQIT--TWGGESQYELLKKLELSEEWHKELFEYCREKGIIFLSTPFDLES 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178 119 VDLLESLDAPAYKIASFEVVDLPLIKRVAQTGKPMIISTGMANEAEIEEAIKTARENGCKELVVLHCVSGYPAPAEQYNL 198
Cdd:pfam03102  80 VDFLESLGVPAYKIASGEITNLPLLRYIAKTGKPVILSTGMATLGEIEEAVEVLRRAGNEDLTLLHCTSEYPAPFEDVNL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2200029178 199 KTIADIAERFNVLSGLSDHTIDNATAVASVTLGACLIEKHVTMDRNGGGADDSFSLEPHELMALCKDTKTAWQAMG 274
Cdd:pfam03102 160 RAIPTLKEAFGVPVGYSDHTLGIAAPIAAVALGAKVIEKHFTLDRNLPGPDHAASLEPDELKEMVRAIRNVEKALG 235
SAF_NeuB_like cd11615
C-terminal SAF domain of sialic acid synthetase; Sialic acid synthetase (N-acetylneuraminate ...
291-348 1.10e-23

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: 92.02  E-value: 1.10e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2200029178 291 RRSLYVVKDIARGESLTSENVRSIRPGFGLAPKHYEEVLGKAATVDIRRGTPLSRDLF 348
Cdd:cd11615     1 RRSLVAARDIKAGEVLTEENLRVKRPGGGLSPKYLDEVLGKKAKRDIKAGEPLTWDDL 58
SAF smart00858
This domain family includes a range of different proteins. Such as antifreeze proteins and ...
291-349 3.57e-09

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: 52.57  E-value: 3.57e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2200029178  291 RRSLYVVKDIARGESLTSENVRSIR------PGFGLAPkhYEEVLGKAATVDIRRGTPLSRDLFE 349
Cdd:smart00858   1 DNVVVAARDLPAGEVITAEDLRLGHvalrdlPGGGLTP--YGQVIGRVARRDIAAGEPITASNLE 63
 
Name Accession Description Interval E-value
PseI TIGR03586
pseudaminic acid synthase; Members of this family are included within the larger pfam03102 ...
18-343 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: 613.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178  18 PYIIAELSANHNGDINRAFQIMEEAKKAGADAIKLQTYTHETITMDCDSEEFQIHGGLWDGQTLYNLYKGAHMPWEWHKP 97
Cdd:TIGR03586   2 PFIIAELSANHNGSLERALAMIEAAKAAGADAIKLQTYTPDTITLDSDRPEFIIKGGLWDGRTLYDLYQEAHTPWEWHKE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178  98 LFEKAKELGITIFSSPFDFTAVDLLESLDAPAYKIASFEVVDLPLIKRVAQTGKPMIISTGMANEAEIEEAIKTARENGC 177
Cdd:TIGR03586  82 LFERAKELGLTIFSSPFDETAVDFLESLDVPAYKIASFEITDLPLIRYVAKTGKPIIMSTGIATLEEIQEAVEACREAGC 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178 178 KELVVLHCVSGYPAPAEQYNLKTIADIAERFNVLSGLSDHTIDNATAVASVTLGACLIEKHVTMDRNGGGADDSFSLEPH 257
Cdd:TIGR03586 162 KDLVLLKCTSSYPAPLEDANLRTIPDLAERFNVPVGLSDHTLGILAPVAAVALGACVIEKHFTLDRSDGGVDSAFSLEPD 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178 258 ELMALCKDTKTAWQAMGQVNYERTEAEKGNVKFRRSLYVVKDIARGESLTSENVRSIRPGFGLAPKHYEEVLGKAATVDI 337
Cdd:TIGR03586 242 EFKALVKEVRNAWLALGEVNYELSEKEKKSRQFRRSLYVVKDIKKGETFTEENVRSVRPGFGLHPKYLDEILGKKANQDI 321

                  ....*.
gi 2200029178 338 RRGTPL 343
Cdd:TIGR03586 322 KKGTPL 327
SpsE COG2089
Sialic acid synthase SpsE, contains C-terminal SAF domain [Cell wall/membrane/envelope ...
18-349 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: 569.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178  18 PYIIAELSANHNGDINRAFQIMEEAKKAGADAIKLQTYTHETITMDCDSEEFQIHGGLWDGQTLYNLYKGAHMPWEWHKP 97
Cdd:COG2089     3 PFIIAEIGVNHNGDLELAKELIDAAAEAGADAVKFQTYTADTLTSDSAPKAFYQSGSLWGGESLYELYKRLELPWEWHKE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178  98 LFEKAKELGITIFSSPFDFTAVDLLESLDAPAYKIASFEVVDLPLIKRVAQTGKPMIISTGMANEAEIEEAIKTARENGC 177
Cdd:COG2089    83 LKEYCKELGIIFFSTPFDEESVDFLEELGVPAYKIASGEITNLPLLRYIAKTGKPIILSTGMATLEEIEEAVEALREAGN 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178 178 KELVVLHCVSGYPAPAEQYNLKTIADIAERFNVLSGLSDHTIDNATAVASVTLGACLIEKHVTMDRNGGGADDSFSLEPH 257
Cdd:COG2089   163 DQIALLHCTSAYPAPPEDVNLRAIPTLKEAFGVPVGLSDHTLGIEVPIAAVALGASVIEKHFTLDRSLPGPDHAFSLEPD 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178 258 ELMALCKDTKTAWQAMGQVNYERTEAEKGN-VKFRRSLYVVKDIARGESLTSENVRSIRPGFGLAPKHYEEVLGKAATVD 336
Cdd:COG2089   243 ELKAMVEAIRNAEKALGSGIKGPTPSEKKNrRVARRSLVAARDIKAGEVITEENLRVKRPGTGLSPKYLDEVLGKKAKRD 322
                         330
                  ....*....|...
gi 2200029178 337 IRRGTPLSRDLFE 349
Cdd:COG2089   323 IKAGTPLTWDDLE 335
NeuB pfam03102
NeuB family; NeuB is the prokaryotic N-acetylneuraminic acid (Neu5Ac) synthase. It catalyzes ...
40-274 3.64e-119

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: 343.73  E-value: 3.64e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178  40 EEAKKAGADAIKLQTYTHETIT-MDCDSEEFQIHggLWDGQTLYNLYKGAHMPWEWHKPLFEKAKELGITIFSSPFDFTA 118
Cdd:pfam03102   2 DAAAEAGADAVKFQTFTAETLVsKEAPKADYQIT--TWGGESQYELLKKLELSEEWHKELFEYCREKGIIFLSTPFDLES 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178 119 VDLLESLDAPAYKIASFEVVDLPLIKRVAQTGKPMIISTGMANEAEIEEAIKTARENGCKELVVLHCVSGYPAPAEQYNL 198
Cdd:pfam03102  80 VDFLESLGVPAYKIASGEITNLPLLRYIAKTGKPVILSTGMATLGEIEEAVEVLRRAGNEDLTLLHCTSEYPAPFEDVNL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2200029178 199 KTIADIAERFNVLSGLSDHTIDNATAVASVTLGACLIEKHVTMDRNGGGADDSFSLEPHELMALCKDTKTAWQAMG 274
Cdd:pfam03102 160 RAIPTLKEAFGVPVGYSDHTLGIAAPIAAVALGAKVIEKHFTLDRNLPGPDHAASLEPDELKEMVRAIRNVEKALG 235
NeuB_NnaB TIGR03569
N-acetylneuraminate synthase; This family is a subset of the pfam03102 and is believed to ...
18-341 6.99e-112

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: 328.77  E-value: 6.99e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178  18 PYIIAELSANHNGDINRAFQIMEEAKKAGADAIKLQTY-THETITMDCDSEEFQIHGGlWDGQTLYNLYKGAHMPWEWHK 96
Cdd:TIGR03569   1 TFIIAEAGVNHNGDLELAKKLVDAAAEAGADAVKFQTFkAEDLVSKNAPKAEYQKINT-GAEESQLEMLKKLELSEEDHR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178  97 PLFEKAKELGITIFSSPFDFTAVDLLESLDAPAYKIASFEVVDLPLIKRVAQTGKPMIISTGMANEAEIEEAIKTARENG 176
Cdd:TIGR03569  80 ELKEYCESKGIEFLSTPFDLESADFLEDLGVPRFKIPSGEITNAPLLKKIARFGKPVILSTGMATLEEIEAALGVLRDAG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178 177 CKE--LVVLHCVSGYPAPAEQYNLKTIADIAERFNVLSGLSDHTIDNATAVASVTLGACLIEKHVTMDRNGGGADDSFSL 254
Cdd:TIGR03569 160 TPDsnITLLHCTTEYPAPFEDVNLNAMDTLKEAFDLPVGYSDHTLGIEAPIAAVALGATVIEKHFTLDKNLPGPDHKASL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178 255 EPHELMALCKDTKTAWQAMGQVNYERTEAEKGNVKF-RRSLYVVKDIARGESLTSENVRSIRPGFGLAPKHYEEVLGKAA 333
Cdd:TIGR03569 240 EPDELKEMVQGIRNVEKALGDGVKRPTPSEQKNRDVaRKSLVAAKDIKKGEIFTEDNLTVKRPGNGISPMEYWEVIGKKA 319

                  ....*...
gi 2200029178 334 TVDIRRGT 341
Cdd:TIGR03569 320 SRDYEEDE 327
SAF_NeuB_like cd11615
C-terminal SAF domain of sialic acid synthetase; Sialic acid synthetase (N-acetylneuraminate ...
291-348 1.10e-23

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: 92.02  E-value: 1.10e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2200029178 291 RRSLYVVKDIARGESLTSENVRSIRPGFGLAPKHYEEVLGKAATVDIRRGTPLSRDLF 348
Cdd:cd11615     1 RRSLVAARDIKAGEVLTEENLRVKRPGGGLSPKYLDEVLGKKAKRDIKAGEPLTWDDL 58
SAF pfam08666
SAF domain; This domain family includes a range of different proteins. Such as antifreeze ...
291-349 2.23e-10

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: 55.64  E-value: 2.23e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2200029178 291 RRSLYVVKDIARGESLTSENVRSIRPG----FGLAPKHYEEVLGKAATVDIRRGTPLSRDLFE 349
Cdd:pfam08666   1 DNVVVAARDLPAGEVITADDLTLVRPPlalpPGLFPIAYGEVIGKVARRDIAAGEPLTASDLE 63
SAF smart00858
This domain family includes a range of different proteins. Such as antifreeze proteins and ...
291-349 3.57e-09

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: 52.57  E-value: 3.57e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2200029178  291 RRSLYVVKDIARGESLTSENVRSIR------PGFGLAPkhYEEVLGKAATVDIRRGTPLSRDLFE 349
Cdd:smart00858   1 DNVVVAARDLPAGEVITAEDLRLGHvalrdlPGGGLTP--YGQVIGRVARRDIAAGEPITASNLE 63
SAF_CpaB_FlgA_like cd11614
SAF domains of the flagella basal body P-ring formation protein FlgA and the flp pilus ...
295-348 6.21e-05

SAF domains of the flagella basal body P-ring formation protein FlgA and the flp pilus assembly CpaB; FlgA is a putative periplasmic chaperone that assists in the formation of the flagellar P ring; CpaB is a protein invoved in the assembly of the flp pili, which are bacterial virulence factors mediating non-specific adherence to surfaces; these proteins appear to contain a single SAF domain. This intermediate family also contains the SAF domains of sialic acid synthetases and type III antifreeze proteins, which also share the same extensive core structure.


Pssm-ID: 212159 [Multi-domain]  Cd Length: 61  Bit Score: 40.15  E-value: 6.21e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2200029178 295 YVV--KDIARGESLTSENVRSIR-PGFGLAPKHY---EEVLGKAATVDIRRGTPLSRDLF 348
Cdd:cd11614     2 VVVaaRDLPAGTVITADDLTLVEvPLSLLPPGALtdpDDVVGRVARRPLRAGEPITASML 61
 
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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