KpsF/GutQ family protein; This model describes a number of closely related proteins with the phosphosugar-binding domain SIS (Sugar ISomerase) followed by two copies of the CBS (named after Cystathionine Beta Synthase) domain. One is GutQ, a protein of the glucitol operon. Another is KpsF, a virulence factor involved in capsular polysialic acid biosynthesis in some pathogenic strains of E. coli. [Energy metabolism, Sugars]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830   57 GHVILSGMGKSGHVGRKMSATLASTGTPSFFIHPAEAFHGDLGMITPYDLLILISASGETDEILKLVPSLKNFGNRIIAI 136
Cdd:TIGR00393   1 GKLVIVGIGKSGLIGKKIVATFASTGTPSFFLHPTEAMHGDLGMVEPNDVVLMISYSGESLELLNLIPHLKRLSHKIIAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830  137 TNNGNSTLAKNADAVLELHMANETCPNNLAPTTSTTLTMAIGDALAIAMIHQRKFMPNDFARYHPGGSLGRRLLTRVADV 216
Cdd:TIGR00393  81 TGSPNSSLARAADYVLDIKVEKEACPINLAPTTSTTLTLALGDALAVALMRARNFSQEDFASFHPGGALGRKLLVKVKDL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830  217 MQ-HDVPAVQLDASFKTVIQRITSGCQGMVMVEDAEGGLAGIITDGDLRRFMEKEDSLTfATAAQMMTREPLTLPEDTMI 295
Cdd:TIGR00393 161 MQtTDLPLIAPTTSFKDALLEMSEKRLGSAIVCDENNQLVGVFTDGDLRRALLGGGSLK-SEVRDFMTLGPKTFKLDALL 239

                         250       260
                  ....*....|....*....|....*...
gi 485703830  296 IEAEEKMQKHRVSTLLVTNKANKVTGLV 323
Cdd:TIGR00393 240 LEALEFLERRKITSLVVVDDHNKVLGVL 267

KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ISomerase) domains. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830  57 GHVILSGMGKSGHVGRKMSATLASTGTPSFFIHPAEAFHGDLGMITPYDLLILISASGETDEILKLVPSLKNFGNRIIAI 136
Cdd:cd05014    1 GKVVVTGVGKSGHIARKIAATLSSTGTPAFFLHPTEALHGDLGMVTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 485703830 137 TNNGNSTLAKNADAVLELHMANETCPNNLAPTTSTTLTMAIGDALAIA 184
Cdd:cd05014   81 TGNPNSTLAKLSDVVLDLPVEEEACPLGLAPTTSTTAMLALGDALAVA 128

Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 485703830   285 EPLTLPEDTMIIEAEEKMQKHRVSTLLVTNKANKVTGLVRIFD 327
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRD 43

KpsF/GutQ family protein; This model describes a number of closely related proteins with the phosphosugar-binding domain SIS (Sugar ISomerase) followed by two copies of the CBS (named after Cystathionine Beta Synthase) domain. One is GutQ, a protein of the glucitol operon. Another is KpsF, a virulence factor involved in capsular polysialic acid biosynthesis in some pathogenic strains of E. coli. [Energy metabolism, Sugars]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830   57 GHVILSGMGKSGHVGRKMSATLASTGTPSFFIHPAEAFHGDLGMITPYDLLILISASGETDEILKLVPSLKNFGNRIIAI 136
Cdd:TIGR00393   1 GKLVIVGIGKSGLIGKKIVATFASTGTPSFFLHPTEAMHGDLGMVEPNDVVLMISYSGESLELLNLIPHLKRLSHKIIAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830  137 TNNGNSTLAKNADAVLELHMANETCPNNLAPTTSTTLTMAIGDALAIAMIHQRKFMPNDFARYHPGGSLGRRLLTRVADV 216
Cdd:TIGR00393  81 TGSPNSSLARAADYVLDIKVEKEACPINLAPTTSTTLTLALGDALAVALMRARNFSQEDFASFHPGGALGRKLLVKVKDL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830  217 MQ-HDVPAVQLDASFKTVIQRITSGCQGMVMVEDAEGGLAGIITDGDLRRFMEKEDSLTfATAAQMMTREPLTLPEDTMI 295
Cdd:TIGR00393 161 MQtTDLPLIAPTTSFKDALLEMSEKRLGSAIVCDENNQLVGVFTDGDLRRALLGGGSLK-SEVRDFMTLGPKTFKLDALL 239

                         250       260
                  ....*....|....*....|....*...
gi 485703830  296 IEAEEKMQKHRVSTLLVTNKANKVTGLV 323
Cdd:TIGR00393 240 LEALEFLERRKITSLVVVDDHNKVLGVL 267

arabinose-5-phosphate isomerase GutQ;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830  15 DPYLITSVRQTLAEQGAALQNLSKQLDSgQYQRVLNLIMNCKGHVILSGMGKSGHVGRKMSATLASTGTPSFFIHPAEAF 94
Cdd:PRK11543   2 SEALLNAGRQTLMLELQEASRLPERLGD-DFVRAANIILHCEGKVVVSGIGKSGHIGKKIAATLASTGTPAFFVHPAEAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830  95 HGDLGMITPYDLLILISASGETDEILKLVPSLKNFGNRIIAITNNGNSTLAKNADAVLELHMANETCPNNLAPTTSTTLT 174
Cdd:PRK11543  81 HGDLGMIESRDVMLFISYSGGAKELDLIIPRLEDKSIALLAMTGKPTSPLGLAAKAVLDISVEREACPMHLAPTSSTVNT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830 175 MAIGDALAIAMIHQRKFMPNDFARYHPGGSLGRRLLTRVADVMQHD--VPAVQLDASFKTVIQRITSGCQGMVMVEDAEG 252
Cdd:PRK11543 161 LMMGDALAMAVMQARGFNEEDFARSHPAGALGARLLNKVHHLMRRDdaIPQVALTASVMDAMLELSRTGLGLVAVCDAQQ 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 485703830 253 GLAGIITDGDLRRFMEKEDSLTfATAAQMMTREPLTLPEDTMIIEAEEKMQKHRVSTLLVTNKANKVTGLVRIFD 327
Cdd:PRK11543 241 QVQGVFTDGDLRRWLVGGGALT-TPVNEAMTRGGTTLQAQSRAIDAKEILMKRKITAAPVVDENGKLTGAINLQD 314

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the with the SIS (Sugar ISomerase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the SIS (Sugar ISomerase) domain in the API [A5P (D-arabinose 5-phosphate) isomerase] protein KpsF/GutQ. These APIs catalyze the conversion of the pentose pathway intermediate D-ribulose 5-phosphate into A5P, a precursor of 3-deoxy-D-manno-octulosonate, which is an integral carbohydrate component of various glycolipids coating the surface of the outer membrane of Gram-negative bacteria, including lipopolysaccharide and many group 2 K-antigen capsules. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830 209 LLTRVADVMQH--DVPAVQLDASFKTVIQRITSGCQGMVMVEDAEGGLAGIITDGDLRRFMEKEDSLTFATAAQMMTREP 286
Cdd:cd04604    1 LLLRVSDLMHTgdELPLVSPDTSLKEALLEMTRKGLGCTAVVDEDGRLVGIITDGDLRRALEKGLDILNLPAKDVMTRNP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 485703830 287 LTLPEDTMIIEAEEKMQKHRVSTLLVTNKANKVTGLVRIFD 327
Cdd:cd04604   81 KTISPDALAAEALELMEEHKITVLPVVDEDGKPVGILHLHD 121

CBS domain [Signal transduction mechanisms];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830 212 RVADVMQHDVPAVQLDASFKTVIQRITSGCQGMVMVEDAEGGLAGIITDGDLRRFMEKED-SLTFATAAQMMTREPLTLP 290
Cdd:COG0517    2 KVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGkDLLDTPVSEVMTRPPVTVS 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 485703830 291 EDTMIIEAEEKMQKHRVSTLLVTNKANKVTGLVRIFD 327
Cdd:COG0517   82 PDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKD 118

Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830 133 IIAITNNGNSTLAKNADAVLELHMANETCPNNLAPTTSTTLTMAIGDALAIAMIHQRKFMPNDFARYHPGGSLGRRLLT- 211
Cdd:COG2524    1 LLVLLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKEl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830 212 ------RVADVMQHDVPAVQLDASFKTVIQRIT-SGCQGMVMVEDaeGGLAGIITDGDLRRFMEKEDSLTFATAAQMMTR 284
Cdd:COG2524   81 glvlkmKVKDIMTKDVITVSPDTTLEEALELMLeKGISGLPVVDD--GKLVGIITERDLLKALAEGRDLLDAPVSDIMTR 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 485703830 285 EPLTLPEDTMIIEAEEKMQKHRVSTLLVTNKANKVTGLV 323
Cdd:COG2524  159 DVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGII 197

RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many phosphosugar isomerases and phosphosugar binding proteins. In E. coli, rpiR negatively regulates the expression of rpiB gene. Both rpiB and rpiA are ribose phosphate isomerases that catalyze the reversible reactions of ribose 5-phosphate into ribulose 5-phosphate.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830  44 QYQRVLNLIMNCKgHVILSGMGKSGHVGRKMSATLASTGTPSFFIHPAEAFHGDLGMITPYDLLILISASGETDEILKLV 123
Cdd:cd05013    2 ALEKAVDLLAKAR-RIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 485703830 124 PSLKNFGNRIIAITNNGNSTLAKNADAVLELHMANEtcPNNLAPTTSTTLTMAIGDALAIA 184
Cdd:cd05013   81 EIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEG--DFRSSAFSSRIAQLALIDALFLA 139

Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain [Cell wall/membrane/envelope biogenesis];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830  26 LAEQGAALQNLSKQLDSgQYQRVLNLIMNCKGH-VILSGMGKSGHVGRKMSATLAS-TGTPSFFIHPAEAFHGDLGMITP 103
Cdd:COG2222    4 IAQQPEAWRRALAALAA-AIAALLARLRAKPPRrVVLVGAGSSDHAAQAAAYLLERlLGIPVAALAPSELVVYPAYLKLE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830 104 YDLLILISASGETDEILKLVPSLKNFGNRIIAITNNGNSTLAKNADAVLELHMANEtcpNNLAPTTSTTLTMAIGDALAI 183
Cdd:COG2222   83 GTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPE---KSVAATKSFTTMLLALLALLA 159

                 ..
gi 485703830 184 AM 185
Cdd:COG2222  160 AW 161

Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) superfamily. In the ribulose monophosphate pathway of formaldehyde fixation, hexulose-6-phosphate synthase catalyzes the condensation of ribulose-5-phosphate with formadelhyde to become hexulose-6-phosphate, which is then isomerized to fructose-6-phosphate by PHI.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830  33 LQNLSKQLDSGQYQRVLNLIMNcKGHVILSGMGKSGHVGRKMSATLASTGTPSFFIhpaeafhGDlgMITPY----DLLI 108
Cdd:cd05005   11 IENVADKIDEEELDKLISAILN-AKRIFVYGAGRSGLVAKAFAMRLMHLGLNVYVV-------GE--TTTPAigpgDLLI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 485703830 109 LISASGETDEILKLVPSLKNFGNRIIAITNNGNSTLAKNADAVLELH 155
Cdd:cd05005   81 AISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIP 127

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830 212 RVADVMQHDVPAVQLDASFKTVIQ-----RItsgcqGMVMVEDaEGGLAGIITDGDLRRFM----------EKEDSLTFA 276
Cdd:cd04584    1 LVKDIMTKNVVTVTPDTSLAEARElmkehKI-----RHLPVVD-DGKLVGIVTDRDLLRASpskatslsiyELNYLLSKI 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 485703830 277 TAAQMMTREPLTLPEDTMIIEAEEKMQKHRVSTLLVTNKaNKVTGLV 323
Cdd:cd04584   75 PVKDIMTKDVITVSPDDTVEEAALLMLENKIGCLPVVDG-GKLVGII 120

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain downstream. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830 224 VQLDASFKTVIQRITSGCQGMVMVEDAEGGLAGIITDGDLRRFMEKEDSLTfATAAQMMTREPLTLPEDTMIIEAEEKMQ 303
Cdd:cd04607    7 VSPDTTIREAIEVIDKGALQIALVVDENRKLLGTVTDGDIRRGLLKGLSLD-APVEEVMNKNPITASPSTSREELLALMR 85

                         90
                 ....*....|....*....
gi 485703830 304 KHRVSTLLVTNKANKVTGL 322
Cdd:cd04607   86 AKKILQLPIVDEQGRVVGL 104

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain. Met2 is a key enzyme in the biosynthesis of methionine. It encodes a homoserine transacetylase involved in converting homoserine to O-acetyl homoserine. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830 213 VADVMQHDVPAVQLDASFKTVIQRITSGCQGMVMVEDAEGGLAGIITDGDLrrfmEKEDSLTFATAAQMMTREPLTLPED 292
Cdd:cd04605    2 VEDIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDI----SKAVALKKDSLEEIMTRNVITARPD 77

                         90       100       110
                 ....*....|....*....|....*....|.
gi 485703830 293 TMIIEAEEKMQKHRVSTLLVTNKANKVTGLV 323
Cdd:cd04605   78 EPIELAARKMEKHNISALPVVDDDRRVIGII 108

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and archaea; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830 217 MQHDVPAVQLDASFKTVIQRITSGCQGMVMVEDAEGGLAGIITDGDL-RRFMEKEDSLTFATAAQMMTREPLTLPEDTMI 295
Cdd:cd17775    1 CRREVVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDIvVEVVAKGLDPKDVTVGDIMSADLITAREDDGL 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 485703830 296 IEAEEKMQKHRVSTLLVTNKANKVTGLVRIFD 327
Cdd:cd17775   81 FEALERMREKGVRRLPVVDDDGELVGIVTLDD 112

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830  243 GMVMVEDaeGGLAGIITDGDLRrFMEKEDSltfaTAAQMMTREPL-TLPEDTMIIEAEEKMQKHRVSTLLVTNKANKVTG 321
Cdd:pfam00478 113 GVPVVDD--GKLVGIVTNRDLR-FETDLSQ----PVSEVMTKENLvTAPEGTTLEEAKEILHKHKIEKLPVVDDNGRLVG 185

                  ....*.
gi 485703830  322 LVRIFD 327
Cdd:pfam00478 186 LITIKD 191

CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal proteins that contain 2 repeats. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830 212 RVADVMQHDVPAVQLDASFKTVIQR-ITSGCQGMVMVEDaeGGLAGIITDGDLRRFMEKEDSLTFATAAQ---------- 280
Cdd:cd17778    1 KVKEFMTTPVVTIYPDDTLKEAMELmVTRGFRRLPVVSG--GKLVGIVTAMDIVKYFGSHEAKKRLTTGDideaystpve 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 485703830 281 -MMTREPLTLPEDTMIIEAEEKMQKHRVSTLLVTNKANKVTGLV 323
Cdd:cd17778   79 eIMSKEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGII 122

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830 237 ITSGCQGM-------VMVEDAEGGLAGIITDGDL-RRFMEKEDSLTFATAAQMMTREPLTLPEDTMIIEAEEKMQKHRVS 308
Cdd:cd17781   13 VAEAAQLMaakrtdaVLVVDDDGGLSGIFTDKDLaRRVVASGLDPRSTLVSSVMTPNPLCVTMDTSATDALDLMVEGKFR 92

                         90
                 ....*....|....*..
gi 485703830 309 TLLVTNKANKVTGLVRI 325
Cdd:cd17781   93 HLPVVDDDGDVVGVLDI 109

Predicted transcriptional regulator containing CBS domains [Transcription];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830 212 RVADVMQ-HDVPAVQLDASFKTVIQRITSGCQGMVMVEDAEGGLAGIITDGDLRRFMEkedsltFATAAQMMTREPLTLP 290
Cdd:COG4109   17 LVEDIMTlEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGKDD------DTPIEDVMTKNPITVT 90

                         90       100       110
                 ....*....|....*....|....*....|....
gi 485703830 291 EDTMIIEAEEKMQKHRVSTLLVTNKANKVTGLVR 324
Cdd:COG4109   91 PDTSLASAAHKMIWEGIELLPVVDDDGRLLGIIS 124

CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830 243 GMVMVEDAEGGLAGIITDGDLRRFMEKEDSLTFATAAQMMTREPLTLPEDTMIIEAEEKMQKHRVSTLLVTNkANKVTGL 322
Cdd:cd17771   28 GSMVVVDANRRPVGIFTLRDLLSRVALPQIDLDAPISEVMTPDPVRLPPSASAFEAALLMAEHGFRHVCVVD-NGRLVGV 106

                 .
gi 485703830 323 V 323
Cdd:cd17771  107 V 107

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485703830 217 MQHDVPAVQLDASFKTVIQ-----RITSGCqgmvmVEDAEGGLAGIITDGD-LRRFME-KEDSLTFATAAQMMTREPLTL 289
Cdd:cd04629    1 MTRNPVTLTPDTSILEAVElllehKISGAP-----VVDEQGRLVGFLSEQDcLKALLEaSYHCEPGGTVADYMSTEVLTV 75