D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655373983   1 MAEAKQLRQWGRRVIDIEKQALDNLYQFVDsPEFAQACELILNCSGKVIVMGMGKSGHIGNKISATLASTGTPAFFVHPG 80
Cdd:COG0794    1 MTDAEDILESAREVLEIEAEALAALAERLD-ESFEKAVELILNCKGRVVVTGMGKSGHIARKIAATLASTGTPAFFLHPA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655373983  81 EASHGDLGVLSENDIVLAISNSGESSEILTLMPVIKRQGIPMISMTGKPESTMAKLAQLHLCIKVPEEACPLGLAPTSST 160
Cdd:COG0794   80 EASHGDLGMITPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVEREACPLNLAPTTST 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655373983 161 TATLVMGDALAVALLQAKGFTKDDFALSHPGGALGRKLLLKVSDVMHKGEELPLVTEDICITDALYEISKKGLGMTAVVN 240
Cdd:COG0794  160 TATLALGDALAVALLEARGFTAEDFARFHPGGSLGRRLLLRVSDLMMPGVEPPVVVPDALLEEALKELGMTGVGGGAVVD 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 655373983 241 QQKQLVGIFTDGDLRRVIDAGVNLRTTKISDVMTRDCITSGDNILAAQALKVMDENDINGLIVINGANEPIGALNMLD 318
Cdd:COG0794  240 DGGGLDGDLTDGDLRRRLLDDLDLTDVMTTTMTTPTTPPLAAAAAAAAAALLIEEIIVVVVVVVVVGVLVGGLLLLLL 317

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 655373983  46 GKVIVMGMGKSGHIGNKISATLASTGTPAFFVHPGEASHGDLGVLSENDIVLAISNSGESSEILTLMPVIKRQGIPMISM 125
Cdd:cd05014    1 GKVVVTGVGKSGHIARKIAATLSSTGTPAFFLHPTEALHGDLGMVTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 655373983 126 TGKPESTMAKLAQLHLCIKVPEEACPLGLAPTSSTTATLVMGDALAVA 173
Cdd:cd05014   81 TGNPNSTLAKLSDVVLDLPVEEEACPLGLAPTTSTTAMLALGDALAVA 128

D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655373983   1 MAEAKQLRQWGRRVIDIEKQALDNLYQFVDsPEFAQACELILNCSGKVIVMGMGKSGHIGNKISATLASTGTPAFFVHPG 80
Cdd:COG0794    1 MTDAEDILESAREVLEIEAEALAALAERLD-ESFEKAVELILNCKGRVVVTGMGKSGHIARKIAATLASTGTPAFFLHPA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655373983  81 EASHGDLGVLSENDIVLAISNSGESSEILTLMPVIKRQGIPMISMTGKPESTMAKLAQLHLCIKVPEEACPLGLAPTSST 160
Cdd:COG0794   80 EASHGDLGMITPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVEREACPLNLAPTTST 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655373983 161 TATLVMGDALAVALLQAKGFTKDDFALSHPGGALGRKLLLKVSDVMHKGEELPLVTEDICITDALYEISKKGLGMTAVVN 240
Cdd:COG0794  160 TATLALGDALAVALLEARGFTAEDFARFHPGGSLGRRLLLRVSDLMMPGVEPPVVVPDALLEEALKELGMTGVGGGAVVD 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 655373983 241 QQKQLVGIFTDGDLRRVIDAGVNLRTTKISDVMTRDCITSGDNILAAQALKVMDENDINGLIVINGANEPIGALNMLD 318
Cdd:COG0794  240 DGGGLDGDLTDGDLRRRLLDDLDLTDVMTTTMTTPTTPPLAAAAAAAAAALLIEEIIVVVVVVVVVGVLVGGLLLLLL 317

arabinose-5-phosphate isomerase GutQ;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655373983   7 LRQWGRRVIDIEKQALDNLYQFVDSpEFAQACELILNCSGKVIVMGMGKSGHIGNKISATLASTGTPAFFVHPGEASHGD 86
Cdd:PRK11543   5 LLNAGRQTLMLELQEASRLPERLGD-DFVRAANIILHCEGKVVVSGIGKSGHIGKKIAATLASTGTPAFFVHPAEALHGD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655373983  87 LGVLSENDIVLAISNSGESSEILTLMPVIKRQGIPMISMTGKPESTMAKLAQLHLCIKVPEEACPLGLAPTSSTTATLVM 166
Cdd:PRK11543  84 LGMIESRDVMLFISYSGGAKELDLIIPRLEDKSIALLAMTGKPTSPLGLAAKAVLDISVEREACPMHLAPTSSTVNTLMM 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655373983 167 GDALAVALLQAKGFTKDDFALSHPGGALGRKLLLKVSDVMHKGEELPLVTEDICITDALYEISKKGLGMTAVVNQQKQLV 246
Cdd:PRK11543 164 GDALAMAVMQARGFNEEDFARSHPAGALGARLLNKVHHLMRRDDAIPQVALTASVMDAMLELSRTGLGLVAVCDAQQQVQ 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655373983 247 GIFTDGDLRRVIDAGVNLrTTKISDVMTRDCITSGDNILAAQALKVMDENDINGLIVINGANEPIGALNMLDMVKAGVI 325
Cdd:PRK11543 244 GVFTDGDLRRWLVGGGAL-TTPVNEAMTRGGTTLQAQSRAIDAKEILMKRKITAAPVVDENGKLTGAINLQDFYQAGII 321

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 655373983 198 LLLKVSDVMHKGEELPLVTEDICITDALYEISKKGLGMTAVVNQQKQLVGIFTDGDLRRVIDAGVNLRTTKISDVMTRDC 277
Cdd:cd04604    1 LLLRVSDLMHTGDELPLVSPDTSLKEALLEMTRKGLGCTAVVDEDGRLVGIITDGDLRRALEKGLDILNLPAKDVMTRNP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 655373983 278 ITSGDNILAAQALKVMDENDINGLIVINGANEPIGALNMLDMVK 321
Cdd:cd04604   81 KTISPDALAAEALELMEEHKITVLPVVDEDGKPVGILHLHDLLR 124

Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655373983 202 VSDVMHKgeELPLVTEDICITDALYEISKKGLGMTAVVNQQKQLVGIFTDGDLR-RVIDAGVNLRTTKISDVMTRDCITS 280
Cdd:COG2905    1 VKDIMSR--DVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRrRVLAEGLDPLDTPVSEVMTRPPITV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 655373983 281 GDNILAAQALKVMDENDINGLIVINGaNEPIGALNMLDMVKA 322
Cdd:COG2905   79 SPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLLRA 119

DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655373983  12 RRVIDIEKQALDNLYQFVDSPEFAQACELILNcSGKVIVMGMGKSGHIGNKISATLASTGTPAFFVHPGEASHGD-LGVL 90
Cdd:COG1737  102 AKVLEAEIANLEETLELLDEEALERAVDLLAK-ARRIYIFGVGASAPVAEDLAYKLLRLGKNVVLLDGDGHLQAEsAALL 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655373983  91 SENDIVLAISNSGESSEILTLMPVIKRQGIPMISMTGKPESTMAKLAQLHLCIKVPEEacPLGLAPTSSTTATLVMGDAL 170
Cdd:COG1737  181 GPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEP--TLRSSAFSSRVAQLALIDAL 258

                 ....*....
gi 655373983 171 AVALLQAKG 179
Cdd:COG1737  259 AAAVAQRDG 267

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 655373983  33 EFAQACELILNcSGKVIVMGMGKSGHIGNKISATLASTGTPAFFVHPGEASHGDLGVLSENDIVLAISNSGESSEILTLM 112
Cdd:cd05013    2 ALEKAVDLLAK-ARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655373983 113 PVIKRQGIPMISMTGKPESTMAKLAQLHLCIKVPEEacPLGLAPTSSTTATLVMGDALAVA 173
Cdd:cd05013   81 EIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEG--DFRSSAFSSRIAQLALIDALFLA 139

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 655373983  22 LDNLYQFVDSPEFAQACELILNcSGKVIVMGMGKSG-----------HIGnKISATLASTGTPAFfvhpgeashgdlgvl 90
Cdd:cd05005   11 IENVADKIDEEELDKLISAILN-AKRIFVYGAGRSGlvakafamrlmHLG-LNVYVVGETTTPAI--------------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655373983  91 SENDIVLAISNSGESSEILTLMPVIKRQGIPMISMTGKPESTMAKLAQLHLCIKVPEEACPLG----LAPTSST--TATL 164
Cdd:cd05005   74 GPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIPAATKDDHGGehksIQPLGTLfeQSAL 153

                        170       180
                 ....*....|....*....|
gi 655373983 165 VMGDALAVALLQAKGFTKDD 184
Cdd:cd05005  154 VFLDAVIAKLMEELGVSEEE 173

CBS-domain-containing membrane protein [Signal transduction mechanisms];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655373983 200 LKVSDVMHKgeELPLVTEDICITDALYEISKKGLGMTAVVNQQKQLVGIFTDGDLRRVI------DAGVNLRTTKISDVM 273
Cdd:COG3448    2 MTVRDIMTR--DVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALlpdrldELEERLLDLPVEDVM 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 655373983 274 TRDCITSGDNILAAQALKVMDENDINGLIVINGANEPIGALNMLDMVKA 322
Cdd:COG3448   80 TRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRA 128

SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655373983  47 KVIVMGMGKSGHIGNKISATLASTGTPAFFVHPGEASHGDLGVLSENDIVLAISNSGESSEILTLMPVIKRQGIPMISMT 126
Cdd:cd05008    1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 655373983 127 GKPESTMAKLAQLHLCIKV-PEEACplglAPTSSTTATLVMGDALAVAL 174
Cdd:cd05008   81 NVVGSTLAREADYVLYLRAgPEISV----AATKAFTSQLLALLLLALAL 125

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 655373983 201 KVSDVMHKgeELPLVTEDICITDALYEISKKGLGMTAVVNQQKqLVGIFTDGDLRRVI----------DAGVNLRTTKIS 270
Cdd:cd04584    1 LVKDIMTK--NVVTVTPDTSLAEARELMKEHKIRHLPVVDDGK-LVGIVTDRDLLRASpskatslsiyELNYLLSKIPVK 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 655373983 271 DVMTRDCITSGDNILAAQALKVMDENDINGLIVINGaNEPIGALNMLDMVKA 322
Cdd:cd04584   78 DIMTKDVITVSPDDTVEEAALLMLENKIGCLPVVDG-GKLVGIITETDILRA 128

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and associated with helix turn helix domain; 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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655373983 210 EELPLVTEDICITDALYEISKKGLGMTAVVNQQKqLVGIFTDGDLRRVIDAGvnLRTTKISDVMTRDCITSGDNILAAQA 289
Cdd:cd04588    2 KDLITLKPDATIKDAAKLLSENNIHGAPVVDDGK-LVGIVTLTDIAKALAEG--KENAKVKDIMTKDVITIDKDEKIYDA 78

                         90       100       110
                 ....*....|....*....|....*....|..
gi 655373983 290 LKVMDENDINGLIVINGANEPIGALNMLDMVK 321
Cdd:cd04588   79 IRLMNKHNIGRLIVVDDNGKPVGIITRTDILK 110

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 655373983 238 VVNQQKQLVGIFTDGDLR-RVIDAGVNLrTTKISDVMTRDCITSGDNILAAQALKVMDENDINGLIVINGaNEPIGALNM 316
Cdd:cd04587   31 LVVDDGRLVGIVTDRDLRnRVVAEGLDP-DTPVSEIMTPPPVTIDADALVFEALLLMLERNIHHLPVVDD-GRVVGVVTA 108

                 ....*.
gi 655373983 317 LDMVKA 322
Cdd:cd04587  109 TDLMRL 114

2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins, repeat 1; This cd contains 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins. Two-component regulation is the predominant form of signal recognition and response coupling mechanism used by bacteria to sense and respond to diverse environmental stresses and cues ranging from common environmental stimuli to host signals recognized by pathogens and bacterial cell-cell communication signals. The structures of both sensors and regulators are modular, and numerous variations in domain architecture and composition have evolved to tailor to specific needs in signal perception and signal transduction. The simplest histidine kinase sensors consists of only sensing and kinase domains. The more complex hybrid sensors contain an additional REC domain typical of two-component regulators and in some cases a C-terminal histidine phosphotransferase (HPT) 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
                 ....*....|....*....|....*....|....*....|...
gi 655373983 237 AVVNQQKQLVGIFTDGDLRRVIDAGVNLRTTKISDVMTRDCIT 279
Cdd:cd04620   49 VLVVENQQLVGIFTERDVVRLTASGIDLSGVTIAEVMTQPVIT 91

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 655373983 215 VTEDICITDALYEISKKGLGMTAVVNQQKQLVGIFTDGD-LRRVIDAGVNLRTTKISDVMTRD--CITSGDNIlaAQALK 291
Cdd:cd04623    7 VSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDyVRKLALRGASSLDTPVSEIMTRDvvTCTPDDTV--EECMA 84

                         90       100       110
                 ....*....|....*....|....*....|
gi 655373983 292 VMDENDINGLIVINGaNEPIGALNMLDMVK 321
Cdd:cd04623   85 LMTERRIRHLPVVED-GKLVGIVSIGDVVK 113

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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655373983 215 VTEDICIT------DALYEISKKGLGMTAVVNQQKQLVGIFTDGDLRRVIDagvnlRTTKISDVMTRDC--ITSGDNILA 286
Cdd:cd04601    1 ITDPVTLSpdatvaDVLELKAEYGISGVPVTEDGGKLVGIVTSRDIRFETD-----LSTPVSEVMTPDErlVTAPEGITL 75

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 655373983 287 AQALKVMDENDINGLIVINGANEPIGALNMLDMVK 321
Cdd:cd04601   76 EEAKEILHKHKIEKLPIVDDNGELVGLITRKDIEK 110

SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655373983  48 VIVMGMGKSGHIGNKISATLAS-TGTPAFFVHPGEASHGDLGVL-SENDIVLAISNSGESSEILTLMPVIKRQGIPMISM 125
Cdd:cd04795    1 IFVIGIGGSGAIAAYFALELLElTGIEVVALIATELEHASLLSLlRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80

                 .
gi 655373983 126 T 126
Cdd:cd04795   81 T 81

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat2; 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 655373983 209 GEELPLVTedicITDALYEISK--KGLGMTAVV--NQQKQLVGIFTDGD-LRRVIDAGVNLRTTKISDVMTR--DCITSG 281
Cdd:cd17782    1 GTPPPLVS----PKTTVREAARlmKENRTTAVLvmDNSGKVIGIFTSKDvVLRVLAAGLDPATTSVVRVMTPnpETAPPS 76

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 655373983 282 DNILaaQALKVMDENDINGLIVINGANEPIGALNML 317
Cdd:cd17782   77 TTIL--DALHKMHEGKFLNLPVVDDEGEIVGLVDVL 110

Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose isomerase catalyzes the isomerization of sedoheptulose 7-phosphate into D-glycero-D-mannoheptose 7-phosphate. This is the first step of the biosynthesis of gram-negative bacteria inner core lipopolysaccharide precursor, L-glycero-D-mannoheptose (Gmh).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655373983  19 KQALDNLyqfvDSPEFAQACELILNC---SGKVIVMGMGKSGHIGNKISATLAS---TGTPAFfvhPGEASHGDLGVLS- 91
Cdd:cd05006    8 KEALLEL----LAEAIEQAAQLLAEAllnGGKILICGNGGSAADAQHFAAELVKrfeKERPGL---PAIALTTDTSILTa 80