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Conserved domains on  [gi|489145391|ref|WP_003055144|]
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MULTISPECIES: L-serine ammonia-lyase, iron-sulfur-dependent subunit beta [Streptococcus]

Protein Classification

L-serine ammonia-lyase, iron-sulfur-dependent, subunit beta( domain architecture ID 11448350)

L-serine ammonia-lyase, iron-sulfur-dependent, subunit beta is part of the enzyme complex that catalyzes the deamination of serine to form pyruvate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
sda_beta super family cl31026
L-serine dehydratase, iron-sulfur-dependent, beta subunit; This enzyme is also called serine ...
 5-199 1.66e-62

L-serine dehydratase, iron-sulfur-dependent, beta subunit; This enzyme is also called serine deaminase. This model describes the beta chain of an iron-sulfur-dependent L-serine dehydratase, as in Bacillus subtilis. A fairly deep split in a UPGMA tree separates members of this family of beta chains from the homologous region of single chain forms such as found in E. coli. This family of enzymes is not homologous to the pyridoxal phosphate-dependent threonine deaminases and eukaryotic serine deaminases. [Energy metabolism, Amino acids and amines, Energy metabolism, Glycolysis/gluconeogenesis]


The actual alignment was detected with superfamily member TIGR00719:

Pssm-ID: 129802 [Multi-domain]  Cd Length: 208  Bit Score: 193.61  E-value: 1.66e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145391    5 KFQSVFDIIGPVMIGPSSSHTAGAVRIGKVVHSIFGEIPDEVTFHLYNSFAKTYKGHGTDKALVAGIMGMDTDNPDIKRS 84
Cdd:TIGR00719   2 KDRSAFDIIGPIMIGPSSSHTAGAAKIANVARSIFGNEPEQIEFQFHGSFAETFKGHGTDRAIIGGILDFDPDDDRIKTA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145391   85 LEIAHQKGIKIYWDILKDSNAPHPNTVKISVKKAD-KSMSVTGVSIGGGNIQVTELNGFSVSLSMNTPTIITVHQDIPGM 163
Cdd:TIGR00719  82 FEIAEAAGIDIEFRTEDAGDNVHPNSAKITFSDEKgEEEELIGISIGGGAIEITEINGFAIEFRGEHPAILLEHNDKFGT 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 489145391  164 IAKVTDILSSSNINIATMNVTRESAGEKAIMIIEVD 199
Cdd:TIGR00719 162 IAGVANLLAGFEINIEHLETAKKDIGNIALLTIEID 197
 
Name Accession Description Interval E-value
sda_beta TIGR00719
L-serine dehydratase, iron-sulfur-dependent, beta subunit; This enzyme is also called serine ...
 5-199 1.66e-62

L-serine dehydratase, iron-sulfur-dependent, beta subunit; This enzyme is also called serine deaminase. This model describes the beta chain of an iron-sulfur-dependent L-serine dehydratase, as in Bacillus subtilis. A fairly deep split in a UPGMA tree separates members of this family of beta chains from the homologous region of single chain forms such as found in E. coli. This family of enzymes is not homologous to the pyridoxal phosphate-dependent threonine deaminases and eukaryotic serine deaminases. [Energy metabolism, Amino acids and amines, Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 129802 [Multi-domain]  Cd Length: 208  Bit Score: 193.61  E-value: 1.66e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145391    5 KFQSVFDIIGPVMIGPSSSHTAGAVRIGKVVHSIFGEIPDEVTFHLYNSFAKTYKGHGTDKALVAGIMGMDTDNPDIKRS 84
Cdd:TIGR00719   2 KDRSAFDIIGPIMIGPSSSHTAGAAKIANVARSIFGNEPEQIEFQFHGSFAETFKGHGTDRAIIGGILDFDPDDDRIKTA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145391   85 LEIAHQKGIKIYWDILKDSNAPHPNTVKISVKKAD-KSMSVTGVSIGGGNIQVTELNGFSVSLSMNTPTIITVHQDIPGM 163
Cdd:TIGR00719  82 FEIAEAAGIDIEFRTEDAGDNVHPNSAKITFSDEKgEEEELIGISIGGGAIEITEINGFAIEFRGEHPAILLEHNDKFGT 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 489145391  164 IAKVTDILSSSNINIATMNVTRESAGEKAIMIIEVD 199
Cdd:TIGR00719 162 IAGVANLLAGFEINIEHLETAKKDIGNIALLTIEID 197
SdaA COG1760
L-serine deaminase [Amino acid transport and metabolism];
8-200 1.02e-33

L-serine deaminase [Amino acid transport and metabolism];


Pssm-ID: 441366 [Multi-domain]  Cd Length: 275  Bit Score: 121.85  E-value: 1.02e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145391   8 SVFDIIG--------------------PVM-----IGPS-SSHTAGAVRIGKVVHSIF--------GEIPDEVTFHLYNS 53
Cdd:COG1760   14 SIFDIIGenemalrpeeeiragldriwDVMkecveIGPStSSHTAGALRIGRRARKLLrygekplpGDVLDWVNIYALAS 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145391  54 FAKTYKGHGTDKALVAGIMGMDT------------DNPDIKRSLEIAHQKGIKIYwdilkdsnaphpNTVKISVKKA--- 118
Cdd:COG1760   94 FEENAAGGGTVTAPTAGALGVIPavllyyqeflgaDDERIRDALLTAAAIGILIK------------FTASISGAEGgcq 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145391 119 ---DKSMSVTGVSI----GGGNIQV--------TELNGFSVSLSMNTPTIITVHQDIpgmIAKVTdilsssNINIATMNV 183
Cdd:COG1760  162 aevGSASAMAAASLvellGGGPIQIenaaeialEHILGLTCDPVGGLVQIPCIERNA---LAAVK------AINIARMAL 232

                        250
                 ....*....|....*..
gi 489145391 184 TRESagekaIMIIEVDS 200
Cdd:COG1760  233 ARDG-----LMVIELDE 244
ACT_LSD cd04903
C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit; ...
 152-222 4.92e-28

C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit; The C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit, found in various bacterial anaerobes such as Clostridium, Bacillis, and Treponema species. These enzymes catalyze the deamination of L-serine, producing pyruvate and ammonia. Unlike the eukaryotic L-serine dehydratase, which requires the pyridoxal-5'-phosphate (PLP) cofactor, the prokaryotic L-serine dehydratase contains an [4Fe-4S] cluster instead of a PLP active site. The LSD alpha and beta subunits of the 'clostridial' enzyme are encoded by the sdhA and sdhB genes. The single subunit bacterial homologs of L-serine dehydratase (LSD1, LSD2, TdcG) present in Escherichia coli, and other enterobacterials, lack the ACT domain described here. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153175  Cd Length: 71  Bit Score: 101.07  E-value: 4.92e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489145391 152 TIITVHQDIPGMIAKVTDILSSSNINIATMNVTRESAGEKAIMIIEVDSRECQDAVKSIAKIPNIHNVNFF 222
Cdd:cd04903    1 TLIVVHKDKPGAIAKVTSVLADHEINIAFMRVSRKEKGDQALMVIEVDQPIDEEVIEEIKKIPNIHQVILI 71
SDH_beta pfam03315
Serine dehydratase beta chain; L-serine dehydratase (EC:4.2.1.13) is a found as a heterodimer ...
 18-138 1.05e-15

Serine dehydratase beta chain; L-serine dehydratase (EC:4.2.1.13) is a found as a heterodimer of alpha and beta chain or as a fusion of the two chains in a single protein. This enzyme catalyzes the deamination of serine to form pyruvate. This enzyme is part of the gluconeogenesis pathway.


Pssm-ID: 427239 [Multi-domain]  Cd Length: 146  Bit Score: 71.28  E-value: 1.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145391   18 IGPSSSHTAGAVRIGKvvhsIF-------GEIPD--EVTFHLYNSFAKTYKGHGTDKALVAGIMGMDTDN--PDIKRSL- 85
Cdd:pfam03315   1 IGPSSSHTVGPMRAAA----RFldelrekGLLDRvaRVRVELYGSLAATGKGHGTDRAVLLGLEGEDPETvdPDAIDARl 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489145391   86 -EIAHQKGIKIY----------WDIL--KDSNAP-HPNTVKISVKKADKSMSVTGV--SIGGGNIqVTE 138
Cdd:pfam03315  77 aAIRATGRLPLGgeheipfdpdRDIVfhRRESLPfHPNGMRFTAFDADGELLLERTyySIGGGFV-VDE 144
PRK15040 PRK15040
L-serine ammonia-lyase;
8-157 1.41e-09

L-serine ammonia-lyase;


Pssm-ID: 185000 [Multi-domain]  Cd Length: 454  Bit Score: 56.98  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145391   8 SVFDIIgPVMIGPSSSHTAGAVRIGK-----VVHSifGEIP--DEVTFHLYNSFAKTYKGHGTDKALVAGIMGMDTDN-- 78
Cdd:PRK15040   3 SAFDIF-KIGIGPSSSHTVGPMNAGKsfidrLESS--GLLTatSHIVVDLYGSLSLTGKGHATDVAIIMGLAGNSPQDvv 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145391  79 --------PDIKRSLEIAHQKGIKIYWDILKDSNAPHP-------NTVKISVKKADKS-MSVTGVSIGGGNIqvTELNGF 142
Cdd:PRK15040  80 ideipafiELVTRSGRLPVASGAHIVDFPVAKNIIFHPemlprheNGMRITAWKGQEElLSKTYYSVGGGFI--VEEEHF 157

                        170
                 ....*....|....*
gi 489145391 143 SVSLSMNTPTIITVH 157
Cdd:PRK15040 158 GLSHDVETSVPYDFH 172
 
Name Accession Description Interval E-value
sda_beta TIGR00719
L-serine dehydratase, iron-sulfur-dependent, beta subunit; This enzyme is also called serine ...
 5-199 1.66e-62

L-serine dehydratase, iron-sulfur-dependent, beta subunit; This enzyme is also called serine deaminase. This model describes the beta chain of an iron-sulfur-dependent L-serine dehydratase, as in Bacillus subtilis. A fairly deep split in a UPGMA tree separates members of this family of beta chains from the homologous region of single chain forms such as found in E. coli. This family of enzymes is not homologous to the pyridoxal phosphate-dependent threonine deaminases and eukaryotic serine deaminases. [Energy metabolism, Amino acids and amines, Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 129802 [Multi-domain]  Cd Length: 208  Bit Score: 193.61  E-value: 1.66e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145391    5 KFQSVFDIIGPVMIGPSSSHTAGAVRIGKVVHSIFGEIPDEVTFHLYNSFAKTYKGHGTDKALVAGIMGMDTDNPDIKRS 84
Cdd:TIGR00719   2 KDRSAFDIIGPIMIGPSSSHTAGAAKIANVARSIFGNEPEQIEFQFHGSFAETFKGHGTDRAIIGGILDFDPDDDRIKTA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145391   85 LEIAHQKGIKIYWDILKDSNAPHPNTVKISVKKAD-KSMSVTGVSIGGGNIQVTELNGFSVSLSMNTPTIITVHQDIPGM 163
Cdd:TIGR00719  82 FEIAEAAGIDIEFRTEDAGDNVHPNSAKITFSDEKgEEEELIGISIGGGAIEITEINGFAIEFRGEHPAILLEHNDKFGT 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 489145391  164 IAKVTDILSSSNINIATMNVTRESAGEKAIMIIEVD 199
Cdd:TIGR00719 162 IAGVANLLAGFEINIEHLETAKKDIGNIALLTIEID 197
SdaA COG1760
L-serine deaminase [Amino acid transport and metabolism];
8-200 1.02e-33

L-serine deaminase [Amino acid transport and metabolism];


Pssm-ID: 441366 [Multi-domain]  Cd Length: 275  Bit Score: 121.85  E-value: 1.02e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145391   8 SVFDIIG--------------------PVM-----IGPS-SSHTAGAVRIGKVVHSIF--------GEIPDEVTFHLYNS 53
Cdd:COG1760   14 SIFDIIGenemalrpeeeiragldriwDVMkecveIGPStSSHTAGALRIGRRARKLLrygekplpGDVLDWVNIYALAS 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145391  54 FAKTYKGHGTDKALVAGIMGMDT------------DNPDIKRSLEIAHQKGIKIYwdilkdsnaphpNTVKISVKKA--- 118
Cdd:COG1760   94 FEENAAGGGTVTAPTAGALGVIPavllyyqeflgaDDERIRDALLTAAAIGILIK------------FTASISGAEGgcq 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145391 119 ---DKSMSVTGVSI----GGGNIQV--------TELNGFSVSLSMNTPTIITVHQDIpgmIAKVTdilsssNINIATMNV 183
Cdd:COG1760  162 aevGSASAMAAASLvellGGGPIQIenaaeialEHILGLTCDPVGGLVQIPCIERNA---LAAVK------AINIARMAL 232

                        250
                 ....*....|....*..
gi 489145391 184 TRESagekaIMIIEVDS 200
Cdd:COG1760  233 ARDG-----LMVIELDE 244
ACT_LSD cd04903
C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit; ...
 152-222 4.92e-28

C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit; The C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit, found in various bacterial anaerobes such as Clostridium, Bacillis, and Treponema species. These enzymes catalyze the deamination of L-serine, producing pyruvate and ammonia. Unlike the eukaryotic L-serine dehydratase, which requires the pyridoxal-5'-phosphate (PLP) cofactor, the prokaryotic L-serine dehydratase contains an [4Fe-4S] cluster instead of a PLP active site. The LSD alpha and beta subunits of the 'clostridial' enzyme are encoded by the sdhA and sdhB genes. The single subunit bacterial homologs of L-serine dehydratase (LSD1, LSD2, TdcG) present in Escherichia coli, and other enterobacterials, lack the ACT domain described here. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153175  Cd Length: 71  Bit Score: 101.07  E-value: 4.92e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489145391 152 TIITVHQDIPGMIAKVTDILSSSNINIATMNVTRESAGEKAIMIIEVDSRECQDAVKSIAKIPNIHNVNFF 222
Cdd:cd04903    1 TLIVVHKDKPGAIAKVTSVLADHEINIAFMRVSRKEKGDQALMVIEVDQPIDEEVIEEIKKIPNIHQVILI 71
ACT_3PGDH-like cd04879
ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate ...
 152-219 8.19e-22

ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH); ACT_3PGDH-like: The ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH), with or without an extended C-terminal (xct) region found in various bacteria, archaea, fungi, and plants. 3PGDH is an enzyme that belongs to the D-isomer specific, 2-hydroxyacid dehydrogenase family and catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, which is the first step in the biosynthesis of L-serine, using NAD+ as the oxidizing agent. In bacteria, 3PGDH is feedback controlled by the end product L-serine in an allosteric manner. In the Escherichia coli homotetrameric enzyme, the interface at adjacent ACT (regulatory) domains couples to create an extended beta-sheet. Each regulatory interface forms two serine-binding sites. The mechanism by which serine transmits inhibition to the active site is postulated to involve the tethering of the regulatory domains together to create a rigid quaternary structure with a solvent-exposed active site cleft. This CD also includes the C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit, found in various bacterial anaerobes such as Clostridium, Bacillus, and Treponema species. LSD enzymes catalyze the deamination of L-serine, producing pyruvate and ammonia. Unlike the eukaryotic L-serine dehydratase, which requires the pyridoxal-5'-phosphate (PLP) cofactor, the prokaryotic L-serine dehydratase contains an [4Fe-4S] cluster instead of a PLP active site. The LSD alpha and beta subunits of the 'clostridial' enzyme are encoded by the sdhA and sdhB genes. The single subunit bacterial homologs of L-serine dehydratase (LSD1, LSD2, TdcG) present in E. coli, and other Enterobacteriales, lack the ACT domain described here. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153151  Cd Length: 71  Bit Score: 84.82  E-value: 8.19e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489145391 152 TIITVHQDIPGMIAKVTDILSSSNINIATMNVTRESAGEKAIMIIEVDSRECQDAVKSIAKIPNIHNV 219
Cdd:cd04879    1 RLLIVHKDVPGVIGKVGTILGEHGINIAAMQVGRKEKGGIAYMVLDVDSPVPEEVLEELKALPGIIRV 68
ACT_3PGDH-xct cd04902
C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH); The ...
 153-219 1.18e-17

C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH); The C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH), with an extended C-terminal (xct) region from bacteria, archaea, fungi, and plants. 3PGDH is an enzyme that belongs to the D-isomer specific, 2-hydroxyacid dehydrogenase family and catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, which is the first step in the biosynthesis of L-serine, using NAD+ as the oxidizing agent. In bacteria, 3PGDH is feedback-controlled by the end product L-serine in an allosteric manner. Some 3PGDH enzymes have an additional domain formed by an extended C-terminal region. This additional domain introduces significant asymmetry to the homotetramer. Adjacent ACT (regulatory) domains interact, creating two serine-binding sites, however, this asymmetric arrangement results in the formation of two different and distinct domain interfaces between identical domains in the asymmetric unit. How this asymmetry influences the mechanism of effector inhibition is still unknown. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153174  Cd Length: 73  Bit Score: 74.04  E-value: 1.18e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489145391 153 IITVHQDIPGMIAKVTDILSSSNINIATMNVTRESAGEKAIMIIEVDSRECQDAVKSIAKIPNIHNV 219
Cdd:cd04902    2 LVVRNTDRPGVIGKVGTILGEAGINIAGMQVGRDEPGGEALMVLSVDEPVPDEVLEELRALPGILSA 68
sda_mono TIGR00720
L-serine dehydratase, iron-sulfur-dependent, single chain form; This enzyme is also called ...
 8-138 2.77e-16

L-serine dehydratase, iron-sulfur-dependent, single chain form; This enzyme is also called serine deaminase and L-serine dehydratase 1. L-serine ammonia-lyase converts serine into pyruvate in the gluconeogenesis pathway from serine. This enzyme is comprised of a single chain in Escherichia coli, Mycobacterium tuberculosis, and several other species, but has separate alpha and beta chains in Bacillus subtilis and related species. The beta and alpha chains are homologous to the N-terminal and C-terminal regions, respectively, but are rather deeply branched in a UPGMA tree. This enzyme requires iron and dithiothreitol for activation in vitro, and is a predicted 4Fe-4S protein. Escherichia coli Pseudomonas aeruginosa have two copies of this protein. [Energy metabolism, Amino acids and amines, Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 273233 [Multi-domain]  Cd Length: 450  Bit Score: 76.61  E-value: 2.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145391    8 SVFDI--IGpvmIGPSSSHTAGAVRIGK-----VVHSIFGEIPDEVTFHLYNSFAKTYKGHGTDKALVAGIMGMDTDNPD 80
Cdd:TIGR00720   2 SVFDLfkIG---IGPSSSHTVGPMRAAKqfaddLRDKGLLEQTTRVQVDLYGSLALTGKGHGTDKAVLLGLMGFLPETVD 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489145391   81 IKRS------------LEIAHQKGIKIYWD---ILKDSNAP-HPNTVKISV--KKADKSMSVTGVSIGGGNIqVTE 138
Cdd:TIGR00720  79 IDSIearieevlenkrLLLGGQHEIPFDYEkdlIFHNEFLPlHPNGMRFTAynGDGEVLYEKTYYSVGGGFI-VDE 153
SDH_beta pfam03315
Serine dehydratase beta chain; L-serine dehydratase (EC:4.2.1.13) is a found as a heterodimer ...
 18-138 1.05e-15

Serine dehydratase beta chain; L-serine dehydratase (EC:4.2.1.13) is a found as a heterodimer of alpha and beta chain or as a fusion of the two chains in a single protein. This enzyme catalyzes the deamination of serine to form pyruvate. This enzyme is part of the gluconeogenesis pathway.


Pssm-ID: 427239 [Multi-domain]  Cd Length: 146  Bit Score: 71.28  E-value: 1.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145391   18 IGPSSSHTAGAVRIGKvvhsIF-------GEIPD--EVTFHLYNSFAKTYKGHGTDKALVAGIMGMDTDN--PDIKRSL- 85
Cdd:pfam03315   1 IGPSSSHTVGPMRAAA----RFldelrekGLLDRvaRVRVELYGSLAATGKGHGTDRAVLLGLEGEDPETvdPDAIDARl 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489145391   86 -EIAHQKGIKIY----------WDIL--KDSNAP-HPNTVKISVKKADKSMSVTGV--SIGGGNIqVTE 138
Cdd:pfam03315  77 aAIRATGRLPLGgeheipfdpdRDIVfhRRESLPfHPNGMRFTAFDADGELLLERTyySIGGGFV-VDE 144
PRK15040 PRK15040
L-serine ammonia-lyase;
8-157 1.41e-09

L-serine ammonia-lyase;


Pssm-ID: 185000 [Multi-domain]  Cd Length: 454  Bit Score: 56.98  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145391   8 SVFDIIgPVMIGPSSSHTAGAVRIGK-----VVHSifGEIP--DEVTFHLYNSFAKTYKGHGTDKALVAGIMGMDTDN-- 78
Cdd:PRK15040   3 SAFDIF-KIGIGPSSSHTVGPMNAGKsfidrLESS--GLLTatSHIVVDLYGSLSLTGKGHATDVAIIMGLAGNSPQDvv 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145391  79 --------PDIKRSLEIAHQKGIKIYWDILKDSNAPHP-------NTVKISVKKADKS-MSVTGVSIGGGNIqvTELNGF 142
Cdd:PRK15040  80 ideipafiELVTRSGRLPVASGAHIVDFPVAKNIIFHPemlprheNGMRITAWKGQEElLSKTYYSVGGGFI--VEEEHF 157

                        170
                 ....*....|....*
gi 489145391 143 SVSLSMNTPTIITVH 157
Cdd:PRK15040 158 GLSHDVETSVPYDFH 172
ACT_3PGDH cd04901
C-terminal ACT (regulatory) domain of D-3-Phosphoglycerate Dehydrogenase (3PGDH) found in ...
 153-219 8.21e-09

C-terminal ACT (regulatory) domain of D-3-Phosphoglycerate Dehydrogenase (3PGDH) found in fungi and bacteria; The C-terminal ACT (regulatory) domain of D-3-Phosphoglycerate Dehydrogenase (3PGDH) found in fungi and bacteria. 3PGDH is an enzyme that belongs to the D-isomer specific, 2-hydroxyacid dehydrogenase family and catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, which is the first step in the biosynthesis of L-serine, using NAD+ as the oxidizing agent. In Escherichia coli, the SerA 3PGDH is feedback-controlled by the end product L-serine in an allosteric manner. In the homotetrameric enzyme, the interface at adjacent ACT (regulatory) domains couples to create an extended beta-sheet. Each regulatory interface forms two serine-binding sites. The mechanism by which serine transmits inhibition to the active site is postulated to involve the tethering of the regulatory domains together to create a rigid quaternary structure with a solvent-exposed active site cleft. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153173  Cd Length: 69  Bit Score: 50.58  E-value: 8.21e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489145391 153 IITVHQDIPGMIAKVTDILSSSNINIATMnvTRESAGEKAIMIIEVDSRECQDAVKSIAKIPNIHNV 219
Cdd:cd04901    2 ILHIHKNVPGVLGQINTILAEHNINIAAQ--YLQTRGEIGYVVIDIDSEVSEELLEALRAIPGTIRV 66
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 153-212 1.50e-07

ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times.


Pssm-ID: 153139 [Multi-domain]  Cd Length: 60  Bit Score: 46.90  E-value: 1.50e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145391 153 IITVHQDIPGMIAKVTDILSSSNINIATMNVTRESAGEKAIMIIEVDSRECQDAVKSIAK 212
Cdd:cd02116    1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFIVVDGDGDLEKLLEALE 60
ACTx2 COG4747
ACT domain-containing protein [General function prediction only];
135-199 3.00e-06

ACT domain-containing protein [General function prediction only];


Pssm-ID: 443781 [Multi-domain]  Cd Length: 129  Bit Score: 45.13  E-value: 3.00e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489145391 135 QVTELNGFSVSLsmnTPTIITVHQDIPGMIAKVTDILSSSNINIATMNVTRESAGEKAIMIIEVD 199
Cdd:COG4747   54 EVLKEAGFTVSE---TDVLAVELPDRPGGLAEILKALAEAGINIEYMYAFVGRPGGKAVLILRVD 115
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 152-215 1.48e-05

ACT domain; This family of domains generally have a regulatory role. ACT domains are 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 ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 41.52  E-value: 1.48e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489145391  152 TIITVHQDIPGMIAKVTDILSSSNINIATMNVTR-ESAGEKAIMIIEVDSRECQDAVKSIAKIPN 215
Cdd:pfam01842   2 VLEVLVPDRPGLLARVLGALADRGINITSIEQGTsEDKGGIVFVVIVVDEEDLEEVLEALKKLEG 66
PRK15023 PRK15023
L-serine deaminase; Provisional
 8-134 2.38e-05

L-serine deaminase; Provisional


Pssm-ID: 184984 [Multi-domain]  Cd Length: 454  Bit Score: 44.67  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145391   8 SVFDIIgPVMIGPSSSHTAGAVRIGK-----VVHSIFGEIPDEVTFHLYNSFAKTYKGHGTDKALVAGIMGMDTDNPDI- 81
Cdd:PRK15023   3 SLFDMF-KVGIGPSSSHTVGPMKAGKqfvddLVEKGLLDSVTRVAVDVYGSLSLTGKGHHTDIAIIMGLAGNEPATVDId 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489145391  82 --------------------KRSLEIAHQKGIKIYwdilkDSNAP-HPNTVKISVKKADKSM-SVTGVSIGGGNI 134
Cdd:PRK15023  82 sipgfirdveererlllaqgRHEVDFPRDNGMRFH-----NGNLPlHENGMQIHAYNGDEVVySKTYYSIGGGFI 151
PRK11790 PRK11790
phosphoglycerate dehydrogenase;
144-214 8.25e-05

phosphoglycerate dehydrogenase;


Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 42.86  E-value: 8.25e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489145391 144 VSLSMNTPT--IITVHQDIPGMIAKVTDILSSSNINIATMNV-TRESAGekaIMIIEVDSRECQDAVKSIAKIP 214
Cdd:PRK11790 330 VSLPEHPGGhrLLHIHENRPGVLAAINQIFAEQGINIAAQYLqTDGEIG---YVVIDVDADYAEEALDALKAIP 400
MetL1 COG0527
Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the ...
 83-178 1.10e-04

Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440293 [Multi-domain]  Cd Length: 407  Bit Score: 42.38  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145391  83 RSLEIAHQKGIKIYwdiLKDSNAP-HPNTVkISVKKADKSMSVTGVSIgggniqvteLNGFsvslsmntpTIITVH---- 157
Cdd:COG0527  215 RAVEPAMKYNIPLR---VRSTFNPdAPGTL-ITAEDEMEGPVVKGIAS---------DKDI---------ALITVSgvpm 272

                         90       100
                 ....*....|....*....|.
gi 489145391 158 QDIPGMIAKVTDILSSSNINI 178
Cdd:COG0527  273 VDEPGFAARIFSALAEAGINV 293
ACT_HSDH-Hom cd04881
ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine ...
 158-216 1.24e-04

ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine dehydrogenase (HSDH) and related domains; The ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine dehydrogenase (HSDH) encoded by the hom gene of Bacillus subtilis and other related sequences. HSDH reduces aspartate semi-aldehyde to the amino acid homoserine, one that is required for the biosynthesis of Met, Thr, and Ile from Asp. Neither the enzyme nor the aspartate pathway is found in the animal kingdom. This mostly bacterial HSDH group has a C-terminal ACT domain and is believed to be involved in enzyme regulation. A C-terminal deletion in the Corynebacterium glutamicum HSDH abolished allosteric inhibition by L-threonine. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153153 [Multi-domain]  Cd Length: 79  Bit Score: 39.42  E-value: 1.24e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489145391 158 QDIPGMIAKVTDILSSSNINIATMNVTRESAGEKAIMII---EVDSRECQDAVKSIAKIPNI 216
Cdd:cd04881    8 KDKPGVLAKITGILAEHGISIESVIQKEADGGETAPVVIvthETSEAALNAALAEIEALDAV 69
ACT_PDH-BS-like cd04889
C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH) ...
 159-202 6.72e-03

C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH) enzyme that catalyzes the formation of 4-hydroxyphenylpyruvate from prephenate; Included in this CD is the C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH) enzyme that catalyzes the formation of 4-hydroxyphenylpyruvate from prephenate, found in Bacillus subtilis (BS) and other Firmicutes, Deinococci, and Bacteroidetes. PDH is the first enzyme in the aromatic amino acid pathway specific for the biosynthesis of tyrosine. This enzyme is feedback inhibited by tyrosine in B. subtilis and other microorganisms. Both phenylalanine and tryptophan have been shown to be inhibitors of this activity in B. subtilis. Bifunctional chorismate mutase-PDH (TyrA) enzymes such as those seen in Escherichia coli do not contain an ACT domain. Also included in this CD is the N-terminal ACT domain of a novel protein composed almost entirely of two tandem ACT domains as seen in the uncharacterized structure (pdb 2F06) of the Bt0572 protein from Bacteroides thetaiotaomicron and related ACT domains. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153161  Cd Length: 56  Bit Score: 34.02  E-value: 6.72e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 489145391 159 DIPGMIAKVTDILSSSNINIATMNVTrESAGEKAIMIIEVDSRE 202
Cdd:cd04889    7 NKPGRLAEVTEILAEAGINIKAISIA-ETRGEFGILRLIFSDPE 49
ACT_Bt0572_2 cd04882
C-terminal ACT domain of a novel protein composed of just two ACT domains; Included in this CD ...
 158-202 6.88e-03

C-terminal ACT domain of a novel protein composed of just two ACT domains; Included in this CD is the C-terminal ACT domain of a novel protein composed of just two ACT domains, as seen in the yet uncharacterized structure (pdb 2F06) of the Bt0572 protein from Bacteroides thetaiotaomicron and related proteins. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153154  Cd Length: 65  Bit Score: 34.12  E-value: 6.88e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 489145391 158 QDIPGMIAKVTDILSSSNINIATMNVTRESAGEKAIMIIEVDSRE 202
Cdd:cd04882    7 PDKPGGLHEILQILSEEGINIEYMYAFVEKKGGKALLIFRTEDIE 51
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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