arabinose-5-phosphate isomerase KdsD;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501505096  10 ETISKEIEAVEGLKLLINEDFEKAIYVIHRSKGKVILTGVGKSGHIARKIASTMASVGTPAVFLHPNEALHGDLGIISKE 89
Cdd:PRK10892  16 EVLAIEREGLAELDQYINQDFTLACEKMFWCKGKVVVMGMGKSGHIGRKMAATFASTGTPSFFVHPGEAAHGDLGMVTPQ 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501505096  90 DVVLALSNSGESAEILYMIPYIKMMGCFLISVTNNKNSTLAKQSDISIVLNIEKEACPLNLAPTSSTTAMLVLGDAMAMS 169
Cdd:PRK10892  96 DVVIAISNSGESSEILALIPVLKRLHVPLICITGRPESSMARAADIHLCVKVPKEACPLGLAPTSSTTATLVMGDALAVA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501505096 170 LLRLSGFKEEDFALLHPAGFLGKK-LKQVKDVGHFGDELPIVKKDAKIYEAIIEITQKGFGATAVVDEAGKLVGILTDGD 248
Cdd:PRK10892 176 LLKARGFTAEDFALSHPGGALGRKlLLRVSDIMHTGDEIPHVSKTASLRDALLEITRKNLGMTVICDDNMKIEGIFTDGD 255

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501505096 249 IRRILESKVDINTTSVYEVCTKNPKTISKSDILAKALSLMESYKITVLIIEEDEKPIGIIHLHDILRSGI 318
Cdd:PRK10892 256 LRRVFDMGIDLRQASIADVMTPGGIRVRPGILAVDALNLMQSRHITSVLVADGDHLLGVLHMHDLLRAGV 325

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 501505096  42 GKVILTGVGKSGHIARKIASTMASVGTPAVFLHPNEALHGDLGIISKEDVVLALSNSGESAEILYMIPYIKMMGCFLISV 121
Cdd:cd05014    1 GKVVVTGVGKSGHIARKIAATLSSTGTPAFFLHPTEALHGDLGMVTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 501505096 122 TNNKNSTLAKQSDISIVLNIEKEACPLNLAPTSSTTAMLVLGDAMAMS 169
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 501505096   206 ELPIVKKDAKIYEAIIEITQKGFGATAVVDEAGKLVGILTDGDIRRILE 254
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49

arabinose-5-phosphate isomerase KdsD;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501505096  10 ETISKEIEAVEGLKLLINEDFEKAIYVIHRSKGKVILTGVGKSGHIARKIASTMASVGTPAVFLHPNEALHGDLGIISKE 89
Cdd:PRK10892  16 EVLAIEREGLAELDQYINQDFTLACEKMFWCKGKVVVMGMGKSGHIGRKMAATFASTGTPSFFVHPGEAAHGDLGMVTPQ 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501505096  90 DVVLALSNSGESAEILYMIPYIKMMGCFLISVTNNKNSTLAKQSDISIVLNIEKEACPLNLAPTSSTTAMLVLGDAMAMS 169
Cdd:PRK10892  96 DVVIAISNSGESSEILALIPVLKRLHVPLICITGRPESSMARAADIHLCVKVPKEACPLGLAPTSSTTATLVMGDALAVA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501505096 170 LLRLSGFKEEDFALLHPAGFLGKK-LKQVKDVGHFGDELPIVKKDAKIYEAIIEITQKGFGATAVVDEAGKLVGILTDGD 248
Cdd:PRK10892 176 LLKARGFTAEDFALSHPGGALGRKlLLRVSDIMHTGDEIPHVSKTASLRDALLEITRKNLGMTVICDDNMKIEGIFTDGD 255

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501505096 249 IRRILESKVDINTTSVYEVCTKNPKTISKSDILAKALSLMESYKITVLIIEEDEKPIGIIHLHDILRSGI 318
Cdd:PRK10892 256 LRRVFDMGIDLRQASIADVMTPGGIRVRPGILAVDALNLMQSRHITSVLVADGDHLLGVLHMHDLLRAGV 325

arabinose-5-phosphate isomerase GutQ;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501505096   7 TALETISKEIEAVEGLKLLINEDFEKAIYVIHRSKGKVILTGVGKSGHIARKIASTMASVGTPAVFLHPNEALHGDLGII 86
Cdd:PRK11543   8 AGRQTLMLELQEASRLPERLGDDFVRAANIILHCEGKVVVSGIGKSGHIGKKIAATLASTGTPAFFVHPAEALHGDLGMI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501505096  87 SKEDVVLALSNSGESAEILYMIPYIKMMGCFLISVTNNKNSTLAKQSDISIVLNIEKEACPLNLAPTSSTTAMLVLGDAM 166
Cdd:PRK11543  88 ESRDVMLFISYSGGAKELDLIIPRLEDKSIALLAMTGKPTSPLGLAAKAVLDISVEREACPMHLAPTSSTVNTLMMGDAL 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501505096 167 AMSLLRLSGFKEEDFALLHPAGFLGKKL-KQVKDVGHFGDELPIVKKDAKIYEAIIEITQKGFGATAVVDEAGKLVGILT 245
Cdd:PRK11543 168 AMAVMQARGFNEEDFARSHPAGALGARLlNKVHHLMRRDDAIPQVALTASVMDAMLELSRTGLGLVAVCDAQQQVQGVFT 247

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501505096 246 DGDIRRILESKVDINtTSVYEVCTKNPKTISKSDILAKALSLMESYKITVL-IIEEDEKPIGIIHLHDILRSGI 318
Cdd:PRK11543 248 DGDLRRWLVGGGALT-TPVNEAMTRGGTTLQAQSRAIDAKEILMKRKITAApVVDENGKLTGAINLQDFYQAGI 320

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 501505096 194 LKQVKDVGHFGDELPIVKKDAKIYEAIIEITQKGFGATAVVDEAGKLVGILTDGDIRRILESKVDINTTSVYEVCTKNPK 273
Cdd:cd04604    2 LLRVSDLMHTGDELPLVSPDTSLKEALLEMTRKGLGCTAVVDEDGRLVGIITDGDLRRALEKGLDILNLPAKDVMTRNPK 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 501505096 274 TISKSDILAKALSLMESYKITVLII-EEDEKPIGIIHLHDILR 315
Cdd:cd04604   82 TISPDALAAEALELMEEHKITVLPVvDEDGKPVGILHLHDLLR 124

CBS domain [Signal transduction mechanisms];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501505096 196 QVKDVghFGDELPIVKKDAKIYEAIIEITQKGFGATAVVDEAGKLVGILTDGDIRRILESK-VDINTTSVYEVCTKNPKT 274
Cdd:COG0517    2 KVKDI--MTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEgKDLLDTPVSEVMTRPPVT 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 501505096 275 ISKSDILAKALSLMESYKITVL-IIEEDEKPIGIIHLHDILRSGIN 319
Cdd:COG0517   80 VSPDTSLEEAAELMEEHKIRRLpVVDDDGRLVGIITIKDLLKALLE 125

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 501505096 205 DELPIVKKDAKIYEAIIEITQKGFGATAVVDEAGKLVGILTDGDIRRILESKVDINTTSVYEVCTKNPKTISKSDILAKA 284
Cdd:cd02205    2 RDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVAEVMTPDVITVSPDTDLEEA 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 501505096 285 LSLMESYKIT-VLIIEEDEKPIGIIHLHDILR 315
Cdd:cd02205   82 LELMLEHGIRrLPVVDDDGKLVGIVTRRDILR 113

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 501505096  28 EDFEKAIYVIHRSKgKVILTGVGKSGHIARKIASTMASVGTPAVFLHPNEALHGDLGIISKEDVVLALSNSGESAEILYM 107
Cdd:cd05013    1 EALEKAVDLLAKAR-RIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501505096 108 IPYIKMMGCFLISVTNNKNSTLAKQSDISIVLNIEKEacPLNLAPTSSTTAMLVLGDAMAMS 169
Cdd:cd05013   80 AEIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEG--DFRSSAFSSRIAQLALIDALFLA 139

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501505096  12 ISKEIEAVEGLKLLIN-EDFEKAIYVIHRSKgKVILTGVGKSGHIARKIASTMASVGTPAVFLHPNEALHGD-LGIISKE 89
Cdd:COG1737  105 LEAEIANLEETLELLDeEALERAVDLLAKAR-RIYIFGVGASAPVAEDLAYKLLRLGKNVVLLDGDGHLQAEsAALLGPG 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501505096  90 DVVLALSNSGESAEILYMIPYIKMMGCFLISVTNNKNSTLAKQSDISIVLNIEKEacPLNLAPTSSTTAMLVLGDAMAMS 169
Cdd:COG1737  184 DVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEP--TLRSSAFSSRVAQLALIDALAAA 261

                 ....*.
gi 501505096 170 LLRLSG 175
Cdd:COG1737  262 VAQRDG 267

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 501505096 213 DAKIYEAIIEITQKGFGATAVVDEaGKLVGILTDGDIR-RILESKVDINTtSVYEVCTKNPKTISKSDILAKALSLMESY 291
Cdd:cd04587   12 DATIQEAAQLMSEERVSSLLVVDD-GRLVGIVTDRDLRnRVVAEGLDPDT-PVSEIMTPPPVTIDADALVFEALLLMLER 89

                         90       100
                 ....*....|....*....|....
gi 501505096 292 KITVLIIEEDEKPIGIIHLHDILR 315
Cdd:cd04587   90 NIHHLPVVDDGRVVGVVTATDLMR 113

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; 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 501505096 209 IVKKDAKIYEAIIEITQKGFGATAVVDEAGKLVGILTDGDIRRILESKVDiNTTSVYEVCTKNPKTISKSDILAKALSLM 288
Cdd:cd09836    7 TVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAVAEGID-LDTPVEEIMTKNLVTVSPDESIYEAAELM 85

                         90       100
                 ....*....|....*....|....*...
gi 501505096 289 ESYKIT-VLIIEEDEKPIGIIHLHDILR 315
Cdd:cd09836   86 REHNIRhLPVVDGGGKLVGVISIRDLAR 113

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 501505096  43 KVILTGVGKSGHIARKIASTMASV-GTPAVFLHPNEALHGDLgIISKEDVVLALSNSGESAEILYMIPYIKMMGCFLISV 121
Cdd:cd05008    1 RILIVGCGTSYHAALVAKYLLERLaGIPVEVEAASEFRYRRP-LLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAI 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 501505096 122 TNNKNSTLAKQSDISIVLNIEKE-ACPLNLAPTSSTTAMLVLGDAMA 167
Cdd:cd05008   80 TNVVGSTLAREADYVLYLRAGPEiSVAATKAFTSQLLALLLLALALA 126

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 501505096 210 VKKDAKIYEAIIEITQKGFGATAVVDEaGKLVGILTDGDIRRILESKVD----------INTTSVYEVCTKNPKTISKSD 279
Cdd:cd04584   13 VTPDTSLAEARELMKEHKIRHLPVVDD-GKLVGIVTDRDLLRASPSKATslsiyelnylLSKIPVKDIMTKDVITVSPDD 91

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 501505096 280 ILAKALSLMESYKITVLIIEEDEKPIGIIHLHDILR 315
Cdd:cd04584   92 TVEEAALLMLENKIGCLPVVDGGKLVGIITETDILR 127

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 501505096 210 VKKDAKIYEAIIEITQKGFGATAVVDEAGKLVGILTDGDI-RRILESKVDINTTSVYEVCTKNPKTISKSDILAKALSLM 288
Cdd:cd04623    7 VSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDYvRKLALRGASSLDTPVSEIMTRDVVTCTPDDTVEECMALM 86

                         90       100
                 ....*....|....*....|....*..
gi 501505096 289 ESYKITVLIIEEDEKPIGIIHLHDILR 315
Cdd:cd04623   87 TERRIRHLPVVEDGKLVGIVSIGDVVK 113

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 501505096   8 ALETISKEIEAVegLKLLINEDFEKAIYVIhRSKGKVILTGVGKSGHIARKIAstM---------ASVG---TPAvflhp 75
Cdd:cd05005    3 YLSLILEEIENV--ADKIDEEELDKLISAI-LNAKRIFVYGAGRSGLVAKAFA--MrlmhlglnvYVVGettTPA----- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501505096  76 nealhgdlgiISKEDVVLALSNSGESAEILYMIPYIKMMGCFLISVTNNKNSTLAKQSDISIVLNIEKEACPL----NLA 151
Cdd:cd05005   73 ----------IGPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIPAATKDDHGgehkSIQ 142

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 501505096 152 PTSST--TAMLVLGDAMAMSLLRLSGFKEEDFALLH 185
Cdd:cd05005  143 PLGTLfeQSALVFLDAVIAKLMEELGVSEEEMKKRH 178

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 501505096 206 ELPIVKKDAKIYEAIIEITQKG-FGATaVVDEAGKLVGILTDGD-IRRILESKV-DINTTSVYEVCTKNPKTISKSDILA 282
Cdd:cd04629    4 NPVTLTPDTSILEAVELLLEHKiSGAP-VVDEQGRLVGFLSEQDcLKALLEASYhCEPGGTVADYMSTEVLTVSPDTSIV 82

                         90       100       110
                 ....*....|....*....|....*....|...
gi 501505096 283 KALSLMESYKITVLIIEEDEKPIGIIHLHDILR 315
Cdd:cd04629   83 DLAQLFLKNKPRRYPVVEDGKLVGQISRRDVLR 115

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain upstream. Cystathionine beta-synthase (CBS ) contains, besides the C-terminal regulatory CBS-pair, an N-terminal heme-binding module, followed by a pyridoxal phosphate (PLP) domain, which houses the active site. It is the first enzyme in the transsulfuration pathway, catalyzing the conversion of serine and homocysteine to cystathionine and water. In general, 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 501505096 210 VKKDAKIYEAIIEITQKGFGATAVVDEAGKLVGILTDGDIRRILESKVDINTTSVYEVCTKNPKTISKSDILAKALSLME 289
Cdd:cd04608   15 VLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSLLAGRAQPSDPVSKAMYKQFKQVDLDTPLGALSRILE 94

                         90       100
                 ....*....|....*....|....*
gi 501505096 290 sYKITVLIIEEDEKPIGIIHLHDIL 314
Cdd:cd04608   95 -RDHFALVVDGQGKVLGIVTRIDLL 118

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 501505096 209 IVKKDAKIYEAIIEITQKGFGATAVVDEAGKLVGILTDGDI-RRILESKVDINTTSVYEVCTKNPKTISKSDILAKALSL 287
Cdd:cd17775    7 TASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDIvVEVVAKGLDPKDVTVGDIMSADLITAREDDGLFEALER 86

                         90       100
                 ....*....|....*....|....*....
gi 501505096 288 MESYKITVL-IIEEDEKPIGIIHLHDILR 315
Cdd:cd17775   87 MREKGVRRLpVVDDDGELVGIVTLDDILE 115