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 38704115    43 GKVVVSGIGKSGHIGKKIAATLASTGTPAFFVHPAEALHGDLGMIESRDVMLFISYSGGAKELDLIIPRLEDKSIALLAM 122
Cdd:TIGR00393   1 GKLVIVGIGKSGLIGKKIVATFASTGTPSFFLHPTEAMHGDLGMVEPNDVVLMISYSGESLELLNLIPHLKRLSHKIIAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704115   123 TGKPTSPLGLAAKAVLDISVEREACPMHLAPTSSTVNTLMMGDALAMAVMQARGFNEEDFARSHPAGALGARLLNKVHHL 202
Cdd:TIGR00393  81 TGSPNSSLARAADYVLDIKVEKEACPINLAPTTSTTLTLALGDALAVALMRARNFSQEDFASFHPGGALGRKLLVKVKDL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704115   203 MRRDDaIPQVALTASVMDAMLELSRTGLGLVAVCDAQQQVQGVFTDGDLRRWLVGGGALTTPVNEAMTVGGTTLQSQSRA 282
Cdd:TIGR00393 161 MQTTD-LPLIAPTTSFKDALLEMSEKRLGSAIVCDENNQLVGVFTDGDLRRALLGGGSLKSEVRDFMTLGPKTFKLDALL 239

                         250       260
                  ....*....|....*....|....*....
gi 38704115   283 IDAKEILMKRKITAAPVVDENGKLTGAIN 311
Cdd:TIGR00393 240 LEALEFLERRKITSLVVVDDHNKVLGVLH 268

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 38704115  43 GKVVVSGIGKSGHIGKKIAATLASTGTPAFFVHPAEALHGDLGMIESRDVMLFISYSGGAKELDLIIPRLEDKSIALLAM 122
Cdd:cd05014   1 GKVVVTGVGKSGHIARKIAATLSSTGTPAFFLHPTEALHGDLGMVTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAI 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 38704115 123 TGKPTSPLGLAAKAVLDISVEREACPMHLAPTSSTVNTLMMGDALAMA 170
Cdd:cd05014  81 TGNPNSTLAKLSDVVLDLPVEEEACPLGLAPTTSTTAMLALGDALAVA 128

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 38704115    43 GKVVVSGIGKSGHIGKKIAATLASTGTPAFFVHPAEALHGDLGMIESRDVMLFISYSGGAKELDLIIPRLEDKSIALLAM 122
Cdd:TIGR00393   1 GKLVIVGIGKSGLIGKKIVATFASTGTPSFFLHPTEAMHGDLGMVEPNDVVLMISYSGESLELLNLIPHLKRLSHKIIAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704115   123 TGKPTSPLGLAAKAVLDISVEREACPMHLAPTSSTVNTLMMGDALAMAVMQARGFNEEDFARSHPAGALGARLLNKVHHL 202
Cdd:TIGR00393  81 TGSPNSSLARAADYVLDIKVEKEACPINLAPTTSTTLTLALGDALAVALMRARNFSQEDFASFHPGGALGRKLLVKVKDL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704115   203 MRRDDaIPQVALTASVMDAMLELSRTGLGLVAVCDAQQQVQGVFTDGDLRRWLVGGGALTTPVNEAMTVGGTTLQSQSRA 282
Cdd:TIGR00393 161 MQTTD-LPLIAPTTSFKDALLEMSEKRLGSAIVCDENNQLVGVFTDGDLRRALLGGGSLKSEVRDFMTLGPKTFKLDALL 239

                         250       260
                  ....*....|....*....|....*....
gi 38704115   283 IDAKEILMKRKITAAPVVDENGKLTGAIN 311
Cdd:TIGR00393 240 LEALEFLERRKITSLVVVDDHNKVLGVLH 268

arabinose-5-phosphate isomerase KdsD;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704115    8 AGRQTLMLELQEASRLPERLGDDFVRAANIILHCEGKVVVSGIGKSGHIGKKIAATLASTGTPAFFVHPAEALHGDLGMI 87
Cdd:PRK10892  13 AGKEVLAIEREGLAELDQYINQDFTLACEKMFWCKGKVVVMGMGKSGHIGRKMAATFASTGTPSFFVHPGEAAHGDLGMV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704115   88 ESRDVMLFISYSGGAKELDLIIPRLEDKSIALLAMTGKPTSPLGLAAKAVLDISVEREACPMHLAPTSSTVNTLMMGDAL 167
Cdd:PRK10892  93 TPQDVVIAISNSGESSEILALIPVLKRLHVPLICITGRPESSMARAADIHLCVKVPKEACPLGLAPTSSTTATLVMGDAL 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704115  168 AMAVMQARGFNEEDFARSHPAGALGARLLNKVHHLMRRDDAIPQVALTASVMDAMLELSRTGLGLVAVCDAQQQVQGVFT 247
Cdd:PRK10892 173 AVALLKARGFTAEDFALSHPGGALGRKLLLRVSDIMHTGDEIPHVSKTASLRDALLEITRKNLGMTVICDDNMKIEGIFT 252

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38704115  248 DGDLRRWLVGGGAL-TTPVNEAMTVGGTTLQSQSRAIDAKEILMKRKITAApVVDENGKLTGAINLQDFYQAGII 321
Cdd:PRK10892 253 DGDLRRVFDMGIDLrQASIADVMTPGGIRVRPGILAVDALNLMQSRHITSV-LVADGDHLLGVLHMHDLLRAGVV 326

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 38704115 195 LLNKVHHLMRRDDAIPQVALTASVMDAMLELSRTGLGLVAVCDAQQQVQGVFTDGDLRRWLVGGG-ALTTPVNEAMTVGG 273
Cdd:cd04604   1 LLLRVSDLMHTGDELPLVSPDTSLKEALLEMTRKGLGCTAVVDEDGRLVGIITDGDLRRALEKGLdILNLPAKDVMTRNP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 38704115 274 TTLQSQSRAIDAKEILMKRKITAAPVVDENGKLTGAINLQD 314
Cdd:cd04604  81 KTISPDALAAEALELMEEHKITVLPVVDEDGKPVGILHLHD 121

CBS domain [Signal transduction mechanisms];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704115 198 KVHHLMRRDdaIPQVALTASVMDAMLELSRTGLGLVAVCDAQQQVQGVFTDGDLRRWLV--GGGALTTPVNEAMTVGGTT 275
Cdd:COG0517   2 KVKDIMTTD--VVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAaeGKDLLDTPVSEVMTRPPVT 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 38704115 276 LQSQSRAIDAKEILMKRKITAAPVVDENGKLTGAINLQDFYQAGI 320
Cdd:COG0517  80 VSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; 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 38704115 212 VALTASVMDAMLELSRTGLGLVAVCDAQQQVQGVFTDGDLRRWLVGGG-ALTTPVNEAMTVGGTTLQSQSRAIDAKEILM 290
Cdd:cd02205   7 VDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGlALDTPVAEVMTPDVITVSPDTDLEEALELML 86

                        90       100
                ....*....|....*....|....
gi 38704115 291 KRKITAAPVVDENGKLTGAINLQD 314
Cdd:cd02205  87 EHGIRRLPVVDDDGKLVGIVTRRD 110

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704115 128 SPLGLAAKAVLDISVEREACPMHLAPTSSTVNTLMMGDALAMAVMQARGFNEEDFARSHPAGALGARLLN-------KVH 200
Cdd:COG2524  10 SLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKElglvlkmKVK 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704115 201 HLMRRDdaIPQVALTASVMDAMLELSRTGLGLVAVCDaQQQVQGVFTDGDLRRWL-VGGGALTTPVNEAMTVGGTTLQSQ 279
Cdd:COG2524  90 DIMTKD--VITVSPDTTLEEALELMLEKGISGLPVVD-DGKLVGIITERDLLKALaEGRDLLDAPVSDIMTRDVVTVSED 166

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 38704115 280 SRAIDAKEILMKRKITAAPVVDENGKLTGAINLQDFYQA 318
Cdd:COG2524 167 DSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRA 205

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 38704115  29 DDFVRAANIILHCEgKVVVSGIGKSGHIGKKIAATLASTGTPAFFVHPAEALHGDLGMIESRDVMLFISYSGGAKELDLI 108
Cdd:cd05013   1 EALEKAVDLLAKAR-RIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEA 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38704115 109 IPRLEDKSIALLAMTGKPTSPLGLAAKAVLDISVEREacPMHLAPTSSTVNTLMMGDALAMA 170
Cdd:cd05013  80 AEIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEG--DFRSSAFSSRIAQLALIDALFLA 139

Predicted transcriptional regulator containing CBS domains [Transcription];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704115 198 KVHHLMRRDDAIPqVALTASVMDAMLELSRTGLGLVAVCDAQQQVQGVFTDGDLRRWLVgggalTTPVNEAMTVGGTTLQ 277
Cdd:COG4109  17 LVEDIMTLEDVAT-LSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGKDD-----DTPIEDVMTKNPITVT 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 38704115 278 SQSRAIDAKEILMKRKITAAPVVDENGKLTGAINLQDFYQA 318
Cdd:COG4109  91 PDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKA 131

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 38704115 210 PQVALT----ASVMDAMLELSRTGLGLVAVCDAQQQVQGVFTDGDLRRWLVGGG--ALTTPVNEAMTVGGTTLQSQSRAI 283
Cdd:cd17781   1 PSPALTvpetTTVAEAAQLMAAKRTDAVLVVDDDGGLSGIFTDKDLARRVVASGldPRSTLVSSVMTPNPLCVTMDTSAT 80

                        90       100
                ....*....|....*....|....*...
gi 38704115 284 DAKEILMKRKITAAPVVDENGKLTGAIN 311
Cdd:cd17781  81 DALDLMVEGKFRHLPVVDDDGDVVGVLD 108

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 (Nucleotidyltransferase) Pol-beta-like domain, and the DUF294 dom; 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 38704115 202 LMRRDDAIpqVALTASVMDAMLELSRTGLGLVAVCDAQQqVQGVFTDGDLR-RWLVGGGALTTPVNEAMTVGGTTLQSQS 280
Cdd:cd04587   1 LMSRPPVT--VPPDATIQEAAQLMSEERVSSLLVVDDGR-LVGIVTDRDLRnRVVAEGLDPDTPVSEIMTPPPVTIDADA 77

                        90       100       110
                ....*....|....*....|....*....|....
gi 38704115 281 RAIDAKEILMKRKITAAPVVDEnGKLTGAINLQD 314
Cdd:cd04587  78 LVFEALLLMLERNIHHLPVVDD-GRVVGVVTATD 110

MurR/RpiR family transcriptional regulator;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704115   44 KVVVSGIGKSGHIGKKIAATLASTGTPAFFVHPAEALHGDLGMIESRDVMLFISYSGGAKELDLIIPRLEDKSIALLAMT 123
Cdd:PRK11557 130 RIILTGIGASGLVAQNFAWKLMKIGINAVAERDMHALLATVQALSPDDLLLAISYSGERRELNLAADEALRVGAKVLAIT 209

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 38704115  124 GkpTSPLGLAAKAVLDISVEREACPMHLAPTSSTVNTLMMGDALAMAVMQ 173
Cdd:PRK11557 210 G--FTPNALQQRASHCLYTIAEEQATRSAAISSTHAQGMLTDLLFMALIQ 257

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and eukaryotes; 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 38704115 212 VALTASVMDAMLELSRTGLGLVAVCDAQQQVQGVFTDGDLRRWLV--GGGALTTPVNEAMTVGGTTLQSQSRAIDAKEIL 289
Cdd:cd04623   7 VSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDYVRKLAlrGASSLDTPVSEIMTRDVVTCTPDDTVEECMALM 86

                        90       100
                ....*....|....*....|.
gi 38704115 290 MKRKITAAPVVDeNGKLTGAI 310
Cdd:cd04623  87 TERRIRHLPVVE-DGKLVGIV 106

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. 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
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38704115 261 LTTPVNEAMT------VG--GTTLQsqsraiDAKEILMKRKITAAPVVDENGKLTGAINLQDF 315
Cdd:cd04601  52 LSTPVSEVMTpderlvTApeGITLE------EAKEILHKHKIEKLPIVDDNGELVGLITRKDI 108

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 38704115  22 RLPERLGDDFVRAANIILHCEG-KVVVSGIGKSGHIGKKIAATLAS-TGTPAFFVHPAEALHGDLGMIESRDVMLFISYS 99
Cdd:COG2222  13 RALAALAAAIAALLARLRAKPPrRVVLVGAGSSDHAAQAAAYLLERlLGIPVAALAPSELVVYPAYLKLEGTLVVAISRS 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704115 100 GGAKELDLIIPRLEDKSIALLAMTGKPTSPLGLAAKAVLDISVEREACpmhLAPTSSTVNTLmmgdALAMAVMQARGFNE 179
Cdd:COG2222  93 GNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKS---VAATKSFTTML----LALLALLAAWGGDD 165

                       170
                ....*....|....*...
gi 38704115 180 EDFARSHPAGALGARLLN 197
Cdd:COG2222 166 ALLAALDALPAALEAALA 183

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in archaea; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in archaea. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. 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
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704115 259 GALTTPVNEAMTVGGTTLQSQSRAIDAKEILMKRKITAAPVVDeNGKLTGAINLQDFYQA 318
Cdd:cd04594  48 NKSPGKVGKYVVRGSPYVTPTSSLEEAWEIMMRNKSRWVAVVE-KGKFLGIITLDDLLEA 106

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 38704115 203 MRRDDAIpqVALTASVMDAMLELSRTGLGLVAVCDAQQQVQGVFTDGDLRRWLVGGGAL--TTPVNEAMTVGGTTLQSQS 280
Cdd:cd17775   1 CRREVVT--ASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDIVVEVVAKGLDpkDVTVGDIMSADLITAREDD 78

                        90       100       110
                ....*....|....*....|....*....|....*
gi 38704115 281 RAIDAKEILMKRKITAAPVVDENGKLTGAINLQDF 315
Cdd:cd17775  79 GLFEALERMREKGVRRLPVVDDDGELVGIVTLDDI 113

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in Euryarchaeota; 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
                ....*....|....*....|....*....|....*....|.
gi 38704115 274 TTLQSQSRAIDAKEILMKRKITAAPVVDENGKLTGAINLQD 314
Cdd:cd17784   5 ITAKPNEGVVEAFEKMLKHKISALPVVDDEGKLIGIVTATD 45

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. 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 38704115 235 VCDAQQQVQGVFTDGDLRRWLVGGGAlTTPVNEAMTVGG--TTLQSQSRAIDAKEILMKRKITAAPVVDENGKLTGAINL 312
Cdd:cd04639  35 VTDEAGRLVGLITVDDLRAIPTSQWP-DTPVRELMKPLEeiPTVAADQSLLEVVKLLEEQQLPALAVVSENGTLVGLIEK 113

                ..
gi 38704115 313 QD 314
Cdd:cd04639 114 ED 115

putative manganese-dependent inorganic diphosphatase;

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 38704115  261 LTTPVNEAMTVGG-TTLQSQSRAIDAKEILMKRKITAAPVVDENGKLTGAIN 311
Cdd:PRK14869 244 QSIPVSYIMTTEDlVTFSKDDYLEDVKEVMLKSRYRSYPVVDEDGKVVGVIS 295

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with family II inorganic pyrophosphatase; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a subgroup of family II inorganic pyrophosphatases (PPases) that also contain a DRTGG domain. The homolog from Clostridium has been shown to be inhibited by AMP and activated by a novel effector, diadenosine 5',5-P1,P4-tetraphosphate (AP(4)A), which has been shown to bind to the CBS 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704115 207 DAIPQVALTASVMDAMLELSRTGLGLVAVCDAQQQVQGVFTDGDLrrwlvgggalTTPVNEAMTVGGTTLQSQSRAID-A 285
Cdd:cd04597   5 DKVEPLSPETSIKDAWNLMDENNLKTLPVTDDNGKLIGLLSISDI----------ARTVDYIMTKDNLIVFKEDDYLDeV 74

                        90       100
                ....*....|....*....|....*.
gi 38704115 286 KEILMKRKITAAPVVDENGKLTGAIN 311
Cdd:cd04597  75 KEIMLNTNFRNYPVVDENNKFLGTIS 100

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of CcpN repressor; 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 38704115 215 TASVMDAMLELSRTGLGLVAVCDAQQQVQGVFTDGDLRRWLVGGGAL-TTPVNEAMT----VggTTLQSQSRAIDAKEIL 289
Cdd:cd04617  12 TTSVYDAIVTLFLEDVGSLFVVDEEGYLVGVVSRKDLLKATLGGQDLeKTPVSMIMTrmpnI--VTVTPDDSVLEAARKL 89

                        90
                ....*....|....*.
gi 38704115 290 MKRKITAAPVVDENGK 305
Cdd:cd04617  90 IEHEIDSLPVVEKEDG 105

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 38704115  17 LQEASRLPERLGDDFV-RAANIILHcEGKVVVSGIGKSGHIGKKIAATLASTGTPAFFV----HPAealhgdlgmIESRD 91
Cdd:cd05005   8 LEEIENVADKIDEEELdKLISAILN-AKRIFVYGAGRSGLVAKAFAMRLMHLGLNVYVVgettTPA---------IGPGD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704115  92 VMLFISYSGGAKELDLIIPRLEDKSIALLAMTGKPTSPLGLAAKAVLDISVEREACPMH----LAPTSST--VNTLMMGD 165
Cdd:cd05005  78 LLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIPAATKDDHGGehksIQPLGTLfeQSALVFLD 157

                       170       180
                ....*....|....*....|.
gi 38704115 166 ALAMAVMQARGFNEEDFARSH 186
Cdd:cd05005 158 AVIAKLMEELGVSEEEMKKRH 178

GuaB1 family IMP dehydrogenase-related protein;