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Conserved domains on  [gi|1063688757|ref|NP_001319174|]
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D-cysteine desulfhydrase [Arabidopsis thaliana]

Protein Classification

aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase family protein( domain architecture ID 10018771)

proteins that function either as aminocyclopropane-1-carboxylate deaminase or as D-cysteine desulfhydrase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ACC_deam_rel TIGR01275
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents ...
54-375 1.73e-171

pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents a family of pyridoxal phosphate-dependent enzymes closely related to (and often designated as putative examples of) 1-aminocyclopropane-1-carboxylate deaminase. It appears that members of this family include both D-cysteine desulfhydrase (EC 4.4.1.15) and 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7).


:

Pssm-ID: 273533 [Multi-domain]  Cd Length: 318  Bit Score: 481.62  E-value: 1.73e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757  54 FSLAHLPTPIHRWNLPGLPNGTELWIKRDDFTGMELSGNKVRKLEFLMAEAVDQHADTVITIGGIQSNHCRATATASNYL 133
Cdd:TIGR01275   1 LELIGAPTPIQYLPRLSDYLGREIYIKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHARATAAVAAKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 134 NLNSHLILRTSKLLADEDPGLVGNLLVERLVGANVHLISKEEYSSIgsEALTNALKEKLEKEGKKPYVIPVGGSNSLGTW 213
Cdd:TIGR01275  81 GLHCVLLLRNPIGTTAENYLLNGNLLLDDLFGAETRIESCEEYTDI--DAQLEELAERLEKEGFKPYVIPVGGSNSLGAL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 214 GYIEAAREIEEQLNyrpDDLKFDDIVVACGSGGTIAGISLGswLGALKAK-------VHAFsVCDDPDYFYDFVQGLLDG 286
Cdd:TIGR01275 159 GYVEAALEIAQQLE---SEVKFDSIVVASGSGGTIAGLSLG--LSHLMPDvelvgvtVSRF-VADQTDKFVNLVQAIAEG 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 287 LHAGVnSRDIVNIHNAKGKGYAMNTSEELEFVKKVASSTGVILDPVYSGKAAYGLINEITKDPkcWEGRKILFIHTGGLL 366
Cdd:TIGR01275 233 LELTV-SAVIPLWDDYFGPGYGVPTSEGMEIVKKVASLEGIILDPVYTGKAFYGLIDGIRKKE--FGDKPILFIHTGGIP 309

                  ....*....
gi 1063688757 367 GLYDKVDQM 375
Cdd:TIGR01275 310 GLFAYHDHL 318
 
Name Accession Description Interval E-value
ACC_deam_rel TIGR01275
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents ...
54-375 1.73e-171

pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents a family of pyridoxal phosphate-dependent enzymes closely related to (and often designated as putative examples of) 1-aminocyclopropane-1-carboxylate deaminase. It appears that members of this family include both D-cysteine desulfhydrase (EC 4.4.1.15) and 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7).


Pssm-ID: 273533 [Multi-domain]  Cd Length: 318  Bit Score: 481.62  E-value: 1.73e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757  54 FSLAHLPTPIHRWNLPGLPNGTELWIKRDDFTGMELSGNKVRKLEFLMAEAVDQHADTVITIGGIQSNHCRATATASNYL 133
Cdd:TIGR01275   1 LELIGAPTPIQYLPRLSDYLGREIYIKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHARATAAVAAKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 134 NLNSHLILRTSKLLADEDPGLVGNLLVERLVGANVHLISKEEYSSIgsEALTNALKEKLEKEGKKPYVIPVGGSNSLGTW 213
Cdd:TIGR01275  81 GLHCVLLLRNPIGTTAENYLLNGNLLLDDLFGAETRIESCEEYTDI--DAQLEELAERLEKEGFKPYVIPVGGSNSLGAL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 214 GYIEAAREIEEQLNyrpDDLKFDDIVVACGSGGTIAGISLGswLGALKAK-------VHAFsVCDDPDYFYDFVQGLLDG 286
Cdd:TIGR01275 159 GYVEAALEIAQQLE---SEVKFDSIVVASGSGGTIAGLSLG--LSHLMPDvelvgvtVSRF-VADQTDKFVNLVQAIAEG 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 287 LHAGVnSRDIVNIHNAKGKGYAMNTSEELEFVKKVASSTGVILDPVYSGKAAYGLINEITKDPkcWEGRKILFIHTGGLL 366
Cdd:TIGR01275 233 LELTV-SAVIPLWDDYFGPGYGVPTSEGMEIVKKVASLEGIILDPVYTGKAFYGLIDGIRKKE--FGDKPILFIHTGGIP 309

                  ....*....
gi 1063688757 367 GLYDKVDQM 375
Cdd:TIGR01275 310 GLFAYHDHL 318
Acd COG2515
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ...
55-370 6.87e-113

1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family [Amino acid transport and metabolism];


Pssm-ID: 442005 [Multi-domain]  Cd Length: 317  Bit Score: 332.91  E-value: 6.87e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757  55 SLAHLPTPIHRwnLPGLP--NGTELWIKRDDFTGMELSGNKVRKLEFLMAEAVDQHADTVITIGGIQSNHCRATATASNY 132
Cdd:COG2515     6 PLAFLPTPLQP--LPRLSaaLGVELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQSNHARATAAAAAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 133 LNLNSHLILRtskllADEDPGLVGNLLVERLVGANVHLISKEEYSSIGSEAltNALKEKLEKEGKKPYVIPVGGSNSLGT 212
Cdd:COG2515    84 LGLKCVLVLR-----GEEPTPLNGNLLLDRLLGAELHFVSRGEYRDRDEAM--EAVAAELRARGGKPYVIPEGGSNPLGA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 213 WGYIEAAREIEEQLNYRpdDLKFDDIVVACGSGGTIAGISLGSWLGALKAKVHAFSVCDDPDYFYDFVQGLLDG---LHA 289
Cdd:COG2515   157 LGYVEAAAELAAQLAEL--GVDFDYIVVASGSGGTLAGLVAGLALLGSDTRVIGISVLKGADFLRERVAELARAtaaLLG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 290 GVNSRDIVNIHNAKGKGYAMNTSEELEFVKKVASSTGVILDPVYSGKAAYGLINEITKD--PKcweGRKILFIHTGGLLG 367
Cdd:COG2515   235 LVSRADIELDDDYHGGGYGKPTPELIEAIRLFARTEGILLDPVYTGKAMAGLIDLIRKGrfPP---GSRVLFIHTGGLPG 311

                  ...
gi 1063688757 368 LYD 370
Cdd:COG2515   312 LFG 314
PRK03910 PRK03910
D-cysteine desulfhydrase; Validated
55-369 2.38e-107

D-cysteine desulfhydrase; Validated


Pssm-ID: 179673  Cd Length: 331  Bit Score: 319.08  E-value: 2.38e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757  55 SLAHLPTPIHRwnlpgLPN-----GTELWIKRDDFTGMELSGNKVRKLEFLMAEAVDQHADTVITIGGIQSNHCRATATA 129
Cdd:PRK03910   10 ELAGLPTPLEP-----LPRlsaalGPDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQTAAA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 130 SNYLNLNSHLILRTSKLLADEDPGLVGNLLVERLVGANVHLISKEEyssiGSEALTNALKEKLEKEGKKPYVIPVGGSNS 209
Cdd:PRK03910   85 AAKLGLKCVLLLENPVPTEAENYLANGNVLLDDLFGAEIHVVPAGT----DMDAQLEELAEELRAQGRRPYVIPVGGSNA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 210 LGTWGYIEAAREIEEQLNYRpdDLKFDDIVVACGSGGTIAGISLGSWLGALKAKVHAFSVCDDPDYFYDFVQGLLD---- 285
Cdd:PRK03910  161 LGALGYVACALEIAQQLAEG--GVDFDAVVVASGSGGTHAGLAAGLAALGPDIPVIGVTVSRSAAEQEPKVAKLAQatae 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 286 --GLHAGVNSRDIVNIHNAKGKGYAMNTSEELEFVKKVASSTGVILDPVYSGKAAYGLINEItKDPKCWEGRKILFIHTG 363
Cdd:PRK03910  239 llGLPTEIPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLI-RQGRFKKGGNVLFIHTG 317

                  ....*.
gi 1063688757 364 GLLGLY 369
Cdd:PRK03910  318 GAPALF 323
ACCD cd06449
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ...
61-364 3.40e-72

Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.


Pssm-ID: 107210  Cd Length: 307  Bit Score: 228.46  E-value: 3.40e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757  61 TPIHrwNLPGL----PNGTELWIKRDDFTGM-ELSGNKVRKLEFLMAEAVDQHADTVITIGGIQSNHCRATATASNYLNL 135
Cdd:cd06449     1 TPIQ--YLPRLsehlGGKVEIYAKRDDCNSGlAFGGNKIRKLEYLLPDALAKGADTLVTVGGIQSNHTRQVAAVAAKLGL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 136 NSHLILRTSKLLADEDPGLVGNLLVERLVGANVHLISKEEYssIGSEALTNALKEKLEKEGKKPYVIPVGGS-NSLGTWG 214
Cdd:cd06449    79 KCVLVQENWVPYSDAVYDRVGNILLSRIMGADVRLVSAGFD--IGIRKSFEEAAEEVEAKGGKPYVIPAGGSeHPLGGLG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 215 YIEAAREIEEQLNyrPDDLKFDDIVVACGSGGTIAGISLGSWLGALKAKVHAFSVCDDP-DYFYDFV---QGLLDGLHAG 290
Cdd:cd06449   157 YVGFVLEIAQQEE--ELGFKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPeKTKAQVLriaQAKLAEEGLE 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063688757 291 VNSRDIVNIHNAKGKGYAMNTSEELEFVKKVASSTGVILDPVYSGKAAYGLINEITKDpKCWEGRKILFIHTGG 364
Cdd:cd06449   235 VKEEDVVLDDDYAAPEYGIPNDETIEAIKLCARLEGIITDPVYEGKSMQGMIDLVRNG-EFKEGSKVLFIHLGG 307
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
55-363 1.45e-30

Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.


Pssm-ID: 459749 [Multi-domain]  Cd Length: 295  Bit Score: 118.57  E-value: 1.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757  55 SLAHLPTPIHRWNLPGLPNGTELWIKRDDF--TGmelsGNKVRKLEFLMAEAVdQHADTVITIGGIQSNHCRATATASNY 132
Cdd:pfam00291   2 SLGIGPTPLVRLPRLSKELGVDVYLKLESLnpTG----SFKDRGALNLLLRLK-EGEGGKTVVEASSGNHGRALAAAAAR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 133 LNLNSHLILRtskllADEDPGlvgNLLVERLVGANVHLISK--EEYSSIGSEALTNalkeklekeGKKPYVIPVGGsNSL 210
Cdd:pfam00291  77 LGLKVTIVVP-----EDAPPG---KLLLMRALGAEVVLVGGdyDEAVAAARELAAE---------GPGAYYINQYD-NPL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 211 GTWGYIEAAREIEEQLNyrpddLKFDDIVVACGSGGTIAGISLGSWLGALKAKVHAFSVcDDPDYFYDFVQG-------- 282
Cdd:pfam00291 139 NIEGYGTIGLEILEQLG-----GDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEP-EGAPALARSLAAgrpvpvpv 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 283 ---LLDGLHAGVN--SRDIVNIHNAKGKGYAMNTSEELEFVKKVASSTGVILDPvYSGKAAYGLinEITKDPKCWEGRKI 357
Cdd:pfam00291 213 adtIADGLGVGDEpgALALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEP-SSAAALAAL--KLALAGELKGGDRV 289

                  ....*.
gi 1063688757 358 LFIHTG 363
Cdd:pfam00291 290 VVVLTG 295
 
Name Accession Description Interval E-value
ACC_deam_rel TIGR01275
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents ...
54-375 1.73e-171

pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents a family of pyridoxal phosphate-dependent enzymes closely related to (and often designated as putative examples of) 1-aminocyclopropane-1-carboxylate deaminase. It appears that members of this family include both D-cysteine desulfhydrase (EC 4.4.1.15) and 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7).


Pssm-ID: 273533 [Multi-domain]  Cd Length: 318  Bit Score: 481.62  E-value: 1.73e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757  54 FSLAHLPTPIHRWNLPGLPNGTELWIKRDDFTGMELSGNKVRKLEFLMAEAVDQHADTVITIGGIQSNHCRATATASNYL 133
Cdd:TIGR01275   1 LELIGAPTPIQYLPRLSDYLGREIYIKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHARATAAVAAKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 134 NLNSHLILRTSKLLADEDPGLVGNLLVERLVGANVHLISKEEYSSIgsEALTNALKEKLEKEGKKPYVIPVGGSNSLGTW 213
Cdd:TIGR01275  81 GLHCVLLLRNPIGTTAENYLLNGNLLLDDLFGAETRIESCEEYTDI--DAQLEELAERLEKEGFKPYVIPVGGSNSLGAL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 214 GYIEAAREIEEQLNyrpDDLKFDDIVVACGSGGTIAGISLGswLGALKAK-------VHAFsVCDDPDYFYDFVQGLLDG 286
Cdd:TIGR01275 159 GYVEAALEIAQQLE---SEVKFDSIVVASGSGGTIAGLSLG--LSHLMPDvelvgvtVSRF-VADQTDKFVNLVQAIAEG 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 287 LHAGVnSRDIVNIHNAKGKGYAMNTSEELEFVKKVASSTGVILDPVYSGKAAYGLINEITKDPkcWEGRKILFIHTGGLL 366
Cdd:TIGR01275 233 LELTV-SAVIPLWDDYFGPGYGVPTSEGMEIVKKVASLEGIILDPVYTGKAFYGLIDGIRKKE--FGDKPILFIHTGGIP 309

                  ....*....
gi 1063688757 367 GLYDKVDQM 375
Cdd:TIGR01275 310 GLFAYHDHL 318
Acd COG2515
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ...
55-370 6.87e-113

1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family [Amino acid transport and metabolism];


Pssm-ID: 442005 [Multi-domain]  Cd Length: 317  Bit Score: 332.91  E-value: 6.87e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757  55 SLAHLPTPIHRwnLPGLP--NGTELWIKRDDFTGMELSGNKVRKLEFLMAEAVDQHADTVITIGGIQSNHCRATATASNY 132
Cdd:COG2515     6 PLAFLPTPLQP--LPRLSaaLGVELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQSNHARATAAAAAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 133 LNLNSHLILRtskllADEDPGLVGNLLVERLVGANVHLISKEEYSSIGSEAltNALKEKLEKEGKKPYVIPVGGSNSLGT 212
Cdd:COG2515    84 LGLKCVLVLR-----GEEPTPLNGNLLLDRLLGAELHFVSRGEYRDRDEAM--EAVAAELRARGGKPYVIPEGGSNPLGA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 213 WGYIEAAREIEEQLNYRpdDLKFDDIVVACGSGGTIAGISLGSWLGALKAKVHAFSVCDDPDYFYDFVQGLLDG---LHA 289
Cdd:COG2515   157 LGYVEAAAELAAQLAEL--GVDFDYIVVASGSGGTLAGLVAGLALLGSDTRVIGISVLKGADFLRERVAELARAtaaLLG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 290 GVNSRDIVNIHNAKGKGYAMNTSEELEFVKKVASSTGVILDPVYSGKAAYGLINEITKD--PKcweGRKILFIHTGGLLG 367
Cdd:COG2515   235 LVSRADIELDDDYHGGGYGKPTPELIEAIRLFARTEGILLDPVYTGKAMAGLIDLIRKGrfPP---GSRVLFIHTGGLPG 311

                  ...
gi 1063688757 368 LYD 370
Cdd:COG2515   312 LFG 314
PRK03910 PRK03910
D-cysteine desulfhydrase; Validated
55-369 2.38e-107

D-cysteine desulfhydrase; Validated


Pssm-ID: 179673  Cd Length: 331  Bit Score: 319.08  E-value: 2.38e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757  55 SLAHLPTPIHRwnlpgLPN-----GTELWIKRDDFTGMELSGNKVRKLEFLMAEAVDQHADTVITIGGIQSNHCRATATA 129
Cdd:PRK03910   10 ELAGLPTPLEP-----LPRlsaalGPDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQTAAA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 130 SNYLNLNSHLILRTSKLLADEDPGLVGNLLVERLVGANVHLISKEEyssiGSEALTNALKEKLEKEGKKPYVIPVGGSNS 209
Cdd:PRK03910   85 AAKLGLKCVLLLENPVPTEAENYLANGNVLLDDLFGAEIHVVPAGT----DMDAQLEELAEELRAQGRRPYVIPVGGSNA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 210 LGTWGYIEAAREIEEQLNYRpdDLKFDDIVVACGSGGTIAGISLGSWLGALKAKVHAFSVCDDPDYFYDFVQGLLD---- 285
Cdd:PRK03910  161 LGALGYVACALEIAQQLAEG--GVDFDAVVVASGSGGTHAGLAAGLAALGPDIPVIGVTVSRSAAEQEPKVAKLAQatae 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 286 --GLHAGVNSRDIVNIHNAKGKGYAMNTSEELEFVKKVASSTGVILDPVYSGKAAYGLINEItKDPKCWEGRKILFIHTG 363
Cdd:PRK03910  239 llGLPTEIPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLI-RQGRFKKGGNVLFIHTG 317

                  ....*.
gi 1063688757 364 GLLGLY 369
Cdd:PRK03910  318 GAPALF 323
ACCD cd06449
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ...
61-364 3.40e-72

Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.


Pssm-ID: 107210  Cd Length: 307  Bit Score: 228.46  E-value: 3.40e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757  61 TPIHrwNLPGL----PNGTELWIKRDDFTGM-ELSGNKVRKLEFLMAEAVDQHADTVITIGGIQSNHCRATATASNYLNL 135
Cdd:cd06449     1 TPIQ--YLPRLsehlGGKVEIYAKRDDCNSGlAFGGNKIRKLEYLLPDALAKGADTLVTVGGIQSNHTRQVAAVAAKLGL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 136 NSHLILRTSKLLADEDPGLVGNLLVERLVGANVHLISKEEYssIGSEALTNALKEKLEKEGKKPYVIPVGGS-NSLGTWG 214
Cdd:cd06449    79 KCVLVQENWVPYSDAVYDRVGNILLSRIMGADVRLVSAGFD--IGIRKSFEEAAEEVEAKGGKPYVIPAGGSeHPLGGLG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 215 YIEAAREIEEQLNyrPDDLKFDDIVVACGSGGTIAGISLGSWLGALKAKVHAFSVCDDP-DYFYDFV---QGLLDGLHAG 290
Cdd:cd06449   157 YVGFVLEIAQQEE--ELGFKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPeKTKAQVLriaQAKLAEEGLE 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063688757 291 VNSRDIVNIHNAKGKGYAMNTSEELEFVKKVASSTGVILDPVYSGKAAYGLINEITKDpKCWEGRKILFIHTGG 364
Cdd:cd06449   235 VKEEDVVLDDDYAAPEYGIPNDETIEAIKLCARLEGIITDPVYEGKSMQGMIDLVRNG-EFKEGSKVLFIHLGG 307
PRK14045 PRK14045
1-aminocyclopropane-1-carboxylate deaminase; Provisional
61-379 7.86e-56

1-aminocyclopropane-1-carboxylate deaminase; Provisional


Pssm-ID: 172537 [Multi-domain]  Cd Length: 329  Bit Score: 186.63  E-value: 7.86e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757  61 TPIHRwnlpgLPN-----GTELWIKRDDFTGMELSGNKVRKLEFLMAEAVDQHADTVITIGGIQSNHCRATATASNYLNL 135
Cdd:PRK14045   22 TPIQY-----LPNisrelGADVYVKRDDLTGLGIGGNKIRKLEYLLGDALSRGADVVITVGAVHSNHAFVTGLAAKKLGL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 136 NSHLILRTSKLLAdedpglvGNLLVERLVGanvhlISKEEYSSIGSEAL---TNALKEKLEKEGKKPYVIPVGGSNSLGT 212
Cdd:PRK14045   97 DAVLVLRGKEELK-------GNYLLDKIMG-----IETRVYEAKDSFELmkyAEEVAEELKGEGRKPYIIPPGGASPVGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 213 WGYIEAAREIEEQLNyrPDDLKFDDIVVACGSGGTIAGISLGSWLGALKAKVHAFSVCDDPDYFYDFVQGLLD--GLHAG 290
Cdd:PRK14045  165 LGYVRAVGEIATQVK--KLGVRFDSIVVAVGSGGTLAGLSLGLAILNAEWRVVGIAVGSFGEKMKEKVKNLVKktKELLG 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 291 VNSRDI-VNIHNAKGKGYAMNTSEELEFVKKVASSTGVILDPVYSGKAAYGLINEITKDPKcweGRKILFIHTGGLLGLY 369
Cdd:PRK14045  243 VKVKVQePELYDYSFGEYGKITKEVAKLIRSVGTMEGLILDPVYTGKAFYGLMDLAKKGEL---GEKILFIHTGGISGTF 319
                         330
                  ....*....|
gi 1063688757 370 DKVDQMASLM 379
Cdd:PRK14045  320 HYGDKMLSLL 329
PRK12390 PRK12390
1-aminocyclopropane-1-carboxylate deaminase; Provisional
60-364 3.31e-41

1-aminocyclopropane-1-carboxylate deaminase; Provisional


Pssm-ID: 183494  Cd Length: 337  Bit Score: 148.26  E-value: 3.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757  60 PTPIHRwnLPGLP----NGTELWIKRDDF-TGMELSGNKVRKLEFLMAEAVDQHADTVITIGGIQSNHCRATATASNYLN 134
Cdd:PRK12390   15 PTPIHP--LKRLSahlgGKVELYAKREDCnSGLAFGGNKTRKLEYLVPDALAQGADTLVSIGGVQSNHTRQVAAVAAHLG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 135 LNSHLIlrTSKLLADEDPGL--VGNLLVERLVGANVHLISkeEYSSIG-----SEALTNAlkeklEKEGKKPYVIPVGGS 207
Cdd:PRK12390   93 MKCVLV--QENWVNYEDAVYdrVGNILLSRIMGADVRLVP--DGFDIGirkswEDALEDV-----RAAGGKPYAIPAGAS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 208 -NSLGTWGYIEAAREI---EEQLNYRpddlkFDDIVVACGSGGTIAGISLGSWLGALKAKVHAFSVCDDPDYFYDFVQGL 283
Cdd:PRK12390  164 dHPLGGLGFVGFAEEVraqEAELGFK-----FDYIVVCSVTGSTQAGMVVGFAADGRARRVIGIDASAKPEQTRAQVLRI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 284 ------LDGLHAGVNSRDIVNIHNAKGKGYAMNTSEELEFVKKVASSTGVILDPVYSGKAAYGLINEITKD--PkcwEGR 355
Cdd:PRK12390  239 arntaeLVELGRDITEDDVVLDERYAGPEYGLPNEGTLEAIRLCARLEGMLTDPVYEGKSMHGMIDLVRKGefP---EGS 315

                  ....*....
gi 1063688757 356 KILFIHTGG 364
Cdd:PRK12390  316 KVLYAHLGG 324
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
55-363 1.45e-30

Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.


Pssm-ID: 459749 [Multi-domain]  Cd Length: 295  Bit Score: 118.57  E-value: 1.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757  55 SLAHLPTPIHRWNLPGLPNGTELWIKRDDF--TGmelsGNKVRKLEFLMAEAVdQHADTVITIGGIQSNHCRATATASNY 132
Cdd:pfam00291   2 SLGIGPTPLVRLPRLSKELGVDVYLKLESLnpTG----SFKDRGALNLLLRLK-EGEGGKTVVEASSGNHGRALAAAAAR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 133 LNLNSHLILRtskllADEDPGlvgNLLVERLVGANVHLISK--EEYSSIGSEALTNalkeklekeGKKPYVIPVGGsNSL 210
Cdd:pfam00291  77 LGLKVTIVVP-----EDAPPG---KLLLMRALGAEVVLVGGdyDEAVAAARELAAE---------GPGAYYINQYD-NPL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 211 GTWGYIEAAREIEEQLNyrpddLKFDDIVVACGSGGTIAGISLGSWLGALKAKVHAFSVcDDPDYFYDFVQG-------- 282
Cdd:pfam00291 139 NIEGYGTIGLEILEQLG-----GDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEP-EGAPALARSLAAgrpvpvpv 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 283 ---LLDGLHAGVN--SRDIVNIHNAKGKGYAMNTSEELEFVKKVASSTGVILDPvYSGKAAYGLinEITKDPKCWEGRKI 357
Cdd:pfam00291 213 adtIADGLGVGDEpgALALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEP-SSAAALAAL--KLALAGELKGGDRV 289

                  ....*.
gi 1063688757 358 LFIHTG 363
Cdd:pfam00291 290 VVVLTG 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
61-364 1.59e-17

Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.


Pssm-ID: 107202 [Multi-domain]  Cd Length: 244  Bit Score: 81.41  E-value: 1.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757  61 TPIHRWNLPGLPNGTELWIKRDDF--TGmelsGNKVRKLEFLMAEAVDQ---HADTVITIGGiqSNHCRATATASNYLNL 135
Cdd:cd00640     1 TPLVRLKRLSKLGGANIYLKLEFLnpTG----SFKDRGALNLILLAEEEgklPKGVIIESTG--GNTGIALAAAAARLGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 136 NSHLIL-RTSKLladedpglvGNLLVERLVGANVHLISkEEYSSIGSEALTNALKEKLekegkkpYVIPVGGSNSLGTWG 214
Cdd:cd00640    75 KCTIVMpEGASP---------EKVAQMRALGAEVVLVP-GDFDDAIALAKELAEEDPG-------AYYVNQFDNPANIAG 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 215 YIEAAREIEEQLnyrpDDLKFDDIVVACGSGGTIAGISLGswLGALKAKVHAFSVcdDPDYFYdfvqglldglhagVNSR 294
Cdd:cd00640   138 QGTIGLEILEQL----GGQKPDAVVVPVGGGGNIAGIARA--LKELLPNVKVIGV--EPEVVT-------------VSDE 196
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063688757 295 DIvnihnakgkgyamntseeLEFVKKVASSTGVILDPVySGKAAYGLINEITKDPKcweGRKILFIHTGG 364
Cdd:cd00640   197 EA------------------LEAIRLLAREEGILVEPS-SAAALAAALKLAKKLGK---GKTVVVILTGG 244
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
219-252 5.51e-03

CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.


Pssm-ID: 107204 [Multi-domain]  Cd Length: 291  Bit Score: 38.26  E-value: 5.51e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1063688757 219 AREIEEQLNYRPDDLkfddiVVACGSGGTIAGIS 252
Cdd:cd01561   150 APEIWEQLDGKVDAF-----VAGVGTGGTITGVA 178
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
219-252 5.63e-03

Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439802 [Multi-domain]  Cd Length: 301  Bit Score: 38.49  E-value: 5.63e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1063688757 219 AREIEEQLnyrpdDLKFDDIVVACGSGGTIAGIS 252
Cdd:COG0031   159 GPEIWEQT-----DGKVDAFVAGVGTGGTITGVG 187
 
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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