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Conserved domains on  [gi|1675082402|ref|WP_138599267|]
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MULTISPECIES: 1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase [Pseudoalteromonas]

Protein Classification

1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase( domain architecture ID 10006466)

1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase is a pyridoxal-phosphate dependent enzyme family protein similar to aminocyclopropane-1-carboxylate deaminase that catalyzes a cyclopropane ring-opening reaction that leads to the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Acd COG2515
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ...
7-292 3.66e-129

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: 369.89  E-value: 3.66e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402   7 SPVQtiHHPLLAARK-VQLSIKRDDLIHPQISGNKWRKLKFNLQAMQQQKKSELLTFGGAFSNHIHATATAGKLFGFKTH 85
Cdd:COG2515    12 TPLQ--PLPRLSAALgVELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQSNHARATAAAAAKLGLKCV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402  86 GIIRGPELDEANPTLNYAKQCGMSLHPVNRITYRLRHDH--TYLAQLQAQFPNAYILPEGGTNAAALLGC----KELAQS 159
Cdd:COG2515    90 LVLRGEEPTPLNGNLLLDRLLGAELHFVSRGEYRDRDEAmeAVAAELRARGGKPYVIPEGGSNPLGALGYveaaAELAAQ 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402 160 LPSS----DVIVCPTGSGGTLAGLIEGAP---QHTKLLGVAVLKQAHYLIDEIKQLSNKANQQ------QNWQLLCDFHD 226
Cdd:COG2515   170 LAELgvdfDYIVVASGSGGTLAGLVAGLAllgSDTRVIGISVLKGADFLRERVAELARATAALlglvsrADIELDDDYHG 249
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1675082402 227 GGYGKFSDNLWQFCQTFSKQHTIPLEPIYSGKMLFAVWQLIEQGYFAKGSHIIAVHTGGLQGLNGL 292
Cdd:COG2515   250 GGYGKPTPELIEAIRLFARTEGILLDPVYTGKAMAGLIDLIRKGRFPPGSRVLFIHTGGLPGLFGY 315
 
Name Accession Description Interval E-value
Acd COG2515
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ...
7-292 3.66e-129

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: 369.89  E-value: 3.66e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402   7 SPVQtiHHPLLAARK-VQLSIKRDDLIHPQISGNKWRKLKFNLQAMQQQKKSELLTFGGAFSNHIHATATAGKLFGFKTH 85
Cdd:COG2515    12 TPLQ--PLPRLSAALgVELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQSNHARATAAAAAKLGLKCV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402  86 GIIRGPELDEANPTLNYAKQCGMSLHPVNRITYRLRHDH--TYLAQLQAQFPNAYILPEGGTNAAALLGC----KELAQS 159
Cdd:COG2515    90 LVLRGEEPTPLNGNLLLDRLLGAELHFVSRGEYRDRDEAmeAVAAELRARGGKPYVIPEGGSNPLGALGYveaaAELAAQ 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402 160 LPSS----DVIVCPTGSGGTLAGLIEGAP---QHTKLLGVAVLKQAHYLIDEIKQLSNKANQQ------QNWQLLCDFHD 226
Cdd:COG2515   170 LAELgvdfDYIVVASGSGGTLAGLVAGLAllgSDTRVIGISVLKGADFLRERVAELARATAALlglvsrADIELDDDYHG 249
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1675082402 227 GGYGKFSDNLWQFCQTFSKQHTIPLEPIYSGKMLFAVWQLIEQGYFAKGSHIIAVHTGGLQGLNGL 292
Cdd:COG2515   250 GGYGKPTPELIEAIRLFARTEGILLDPVYTGKAMAGLIDLIRKGRFPPGSRVLFIHTGGLPGLFGY 315
PRK03910 PRK03910
D-cysteine desulfhydrase; Validated
22-289 6.81e-41

D-cysteine desulfhydrase; Validated


Pssm-ID: 179673  Cd Length: 331  Bit Score: 144.59  E-value: 6.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402  22 VQLSIKRDDLIHPQISGNKWRKLKFNLQAMQQQKKSELLTFGGAFSNHIHATATAGKLFGFKTHGIIRGPELDEA-NPTL 100
Cdd:PRK03910   30 PDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQTAAAAAKLGLKCVLLLENPVPTEAeNYLA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402 101 NyakqcGmslhpvNRITYRL----------RHD-----HTYLAQLQAQFPNAYILPEGGTNAAALLG---C-KELAQSLP 161
Cdd:PRK03910  110 N-----G------NVLLDDLfgaeihvvpaGTDmdaqlEELAEELRAQGRRPYVIPVGGSNALGALGyvaCaLEIAQQLA 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402 162 SS----DVIVCPTGSGGTLAGLIEGAPQ---HTKLLGVAVLKQAHYLIDEIKQLsnkanQQQNWQLL------------- 221
Cdd:PRK03910  179 EGgvdfDAVVVASGSGGTHAGLAAGLAAlgpDIPVIGVTVSRSAAEQEPKVAKL-----AQATAELLglpteipradirl 253
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1675082402 222 -CDFHDGGYGKFSDNLWQFCQTFSKQHTIPLEPIYSGKMLFAVWQLIEQGYFAKGSHIIAVHTGGLQGL 289
Cdd:PRK03910  254 wDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFKKGGNVLFIHTGGAPAL 322
ACC_deam_rel TIGR01275
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents ...
26-289 1.72e-34

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: 127.23  E-value: 1.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402  26 IKRDDLIHPQISGNKWRKLKFNLQAMQQQKKSELLTFGGAFSNHIHATATAGKLFGFKTHGIIRGPELDEA-NPTLN--- 101
Cdd:TIGR01275  26 IKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHARATAAVAAKLGLHCVLLLRNPIGTTAeNYLLNgnl 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402 102 -YAKQCGMSLHPVNRITY-RLRHDHTYLAQ-LQAQFPNAYILPEGGTNAAALLG----CKELAQSLPSS---DVIVCPTG 171
Cdd:TIGR01275 106 lLDDLFGAETRIESCEEYtDIDAQLEELAErLEKEGFKPYVIPVGGSNSLGALGyveaALEIAQQLESEvkfDSIVVASG 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402 172 SGGTLAGL---IEGAPQHTKLLGVAV----LKQAHYLIDEIKQLSN--KANQQQNWQLLCDFHDGGYGKFSDNLWQFCQT 242
Cdd:TIGR01275 186 SGGTIAGLslgLSHLMPDVELVGVTVsrfvADQTDKFVNLVQAIAEglELTVSAVIPLWDDYFGPGYGVPTSEGMEIVKK 265
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1675082402 243 FSKQHTIPLEPIYSGKMLFAVWQLIEQGYFaKGSHIIAVHTGGLQGL 289
Cdd:TIGR01275 266 VASLEGIILDPVYTGKAFYGLIDGIRKKEF-GDKPILFIHTGGIPGL 311
ACCD cd06449
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ...
21-285 8.39e-22

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: 92.87  E-value: 8.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402  21 KVQLSIKRDDLIH-PQISGNKWRKLKFNLQAMQQQKKSELLTFGGAFSNHIHATATAGKLFGFKTHGIIRGPEldeANPT 99
Cdd:cd06449    16 KVEIYAKRDDCNSgLAFGGNKIRKLEYLLPDALAKGADTLVTVGGIQSNHTRQVAAVAAKLGLKCVLVQENWV---PYSD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402 100 LNYAKQCGMSLHPVNRITYRLrHDHTYLAQLQAQFPNA-----------YILPEGGT-NAAALLG-----------CKEL 156
Cdd:cd06449    93 AVYDRVGNILLSRIMGADVRL-VSAGFDIGIRKSFEEAaeeveakggkpYVIPAGGSeHPLGGLGyvgfvleiaqqEEEL 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402 157 AQSLpssDVIVCPTGSGGTLAGLIEGAPQ---HTKLLGVAVLKQAHylideiKQLSNKANQQQN-------------WQL 220
Cdd:cd06449   172 GFKF---DSIVVCSVTGSTHAGLSVGLAAlgrQRRVIGIDASAKPE------KTKAQVLRIAQAklaeeglevkeedVVL 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1675082402 221 LCDFHDGGYGKFSDNLWQFCQTFSKQHTIPLEPIYSGKMLFAVWQLIEQGYFAKGSHIIAVHTGG 285
Cdd:cd06449   243 DDDYAAPEYGIPNDETIEAIKLCARLEGIITDPVYEGKSMQGMIDLVRNGEFKEGSKVLFIHLGG 307
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
14-284 1.63e-11

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: 63.48  E-value: 1.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402  14 HPLLAARKVQLSIKRDDLiHPqISGNKWRKLkFNLQAMQQQKKSELLTFGGAFSNHIHATATAGKLFGFKTHGIIrgPEl 93
Cdd:pfam00291  14 PRLSKELGVDVYLKLESL-NP-TGSFKDRGA-LNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIVV--PE- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402  94 DEANPTLNYAKQCGMSLHPVNRITYRLRHdhtYLAQLQAQFPNAYILPEGGtNAAALLGCK----ELAQSL-PSSDVIVC 168
Cdd:pfam00291  88 DAPPGKLLLMRALGAEVVLVGGDYDEAVA---AARELAAEGPGAYYINQYD-NPLNIEGYGtiglEILEQLgGDPDAVVV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402 169 PTGSGGTLAG----LIEGAPqHTKLLGV-----------------AVLKQAHYLIDEIKQLSNKANqqQNWQLLCDFHDG 227
Cdd:pfam00291 164 PVGGGGLIAGiargLKELGP-DVRVIGVepegapalarslaagrpVPVPVADTIADGLGVGDEPGA--LALDLLDEYVGE 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1675082402 228 GYGKFSDNLWQFCQTFSKQHTIPLEPiYSGKMLFAVwQLIEQGYFAKGSHIIAVHTG 284
Cdd:pfam00291 241 VVTVSDEEALEAMRLLARREGIVVEP-SSAAALAAL-KLALAGELKGGDRVVVVLTG 295
 
Name Accession Description Interval E-value
Acd COG2515
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ...
7-292 3.66e-129

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: 369.89  E-value: 3.66e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402   7 SPVQtiHHPLLAARK-VQLSIKRDDLIHPQISGNKWRKLKFNLQAMQQQKKSELLTFGGAFSNHIHATATAGKLFGFKTH 85
Cdd:COG2515    12 TPLQ--PLPRLSAALgVELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQSNHARATAAAAAKLGLKCV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402  86 GIIRGPELDEANPTLNYAKQCGMSLHPVNRITYRLRHDH--TYLAQLQAQFPNAYILPEGGTNAAALLGC----KELAQS 159
Cdd:COG2515    90 LVLRGEEPTPLNGNLLLDRLLGAELHFVSRGEYRDRDEAmeAVAAELRARGGKPYVIPEGGSNPLGALGYveaaAELAAQ 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402 160 LPSS----DVIVCPTGSGGTLAGLIEGAP---QHTKLLGVAVLKQAHYLIDEIKQLSNKANQQ------QNWQLLCDFHD 226
Cdd:COG2515   170 LAELgvdfDYIVVASGSGGTLAGLVAGLAllgSDTRVIGISVLKGADFLRERVAELARATAALlglvsrADIELDDDYHG 249
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1675082402 227 GGYGKFSDNLWQFCQTFSKQHTIPLEPIYSGKMLFAVWQLIEQGYFAKGSHIIAVHTGGLQGLNGL 292
Cdd:COG2515   250 GGYGKPTPELIEAIRLFARTEGILLDPVYTGKAMAGLIDLIRKGRFPPGSRVLFIHTGGLPGLFGY 315
PRK03910 PRK03910
D-cysteine desulfhydrase; Validated
22-289 6.81e-41

D-cysteine desulfhydrase; Validated


Pssm-ID: 179673  Cd Length: 331  Bit Score: 144.59  E-value: 6.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402  22 VQLSIKRDDLIHPQISGNKWRKLKFNLQAMQQQKKSELLTFGGAFSNHIHATATAGKLFGFKTHGIIRGPELDEA-NPTL 100
Cdd:PRK03910   30 PDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQTAAAAAKLGLKCVLLLENPVPTEAeNYLA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402 101 NyakqcGmslhpvNRITYRL----------RHD-----HTYLAQLQAQFPNAYILPEGGTNAAALLG---C-KELAQSLP 161
Cdd:PRK03910  110 N-----G------NVLLDDLfgaeihvvpaGTDmdaqlEELAEELRAQGRRPYVIPVGGSNALGALGyvaCaLEIAQQLA 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402 162 SS----DVIVCPTGSGGTLAGLIEGAPQ---HTKLLGVAVLKQAHYLIDEIKQLsnkanQQQNWQLL------------- 221
Cdd:PRK03910  179 EGgvdfDAVVVASGSGGTHAGLAAGLAAlgpDIPVIGVTVSRSAAEQEPKVAKL-----AQATAELLglpteipradirl 253
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1675082402 222 -CDFHDGGYGKFSDNLWQFCQTFSKQHTIPLEPIYSGKMLFAVWQLIEQGYFAKGSHIIAVHTGGLQGL 289
Cdd:PRK03910  254 wDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFKKGGNVLFIHTGGAPAL 322
ACC_deam_rel TIGR01275
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents ...
26-289 1.72e-34

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: 127.23  E-value: 1.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402  26 IKRDDLIHPQISGNKWRKLKFNLQAMQQQKKSELLTFGGAFSNHIHATATAGKLFGFKTHGIIRGPELDEA-NPTLN--- 101
Cdd:TIGR01275  26 IKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHARATAAVAAKLGLHCVLLLRNPIGTTAeNYLLNgnl 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402 102 -YAKQCGMSLHPVNRITY-RLRHDHTYLAQ-LQAQFPNAYILPEGGTNAAALLG----CKELAQSLPSS---DVIVCPTG 171
Cdd:TIGR01275 106 lLDDLFGAETRIESCEEYtDIDAQLEELAErLEKEGFKPYVIPVGGSNSLGALGyveaALEIAQQLESEvkfDSIVVASG 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402 172 SGGTLAGL---IEGAPQHTKLLGVAV----LKQAHYLIDEIKQLSN--KANQQQNWQLLCDFHDGGYGKFSDNLWQFCQT 242
Cdd:TIGR01275 186 SGGTIAGLslgLSHLMPDVELVGVTVsrfvADQTDKFVNLVQAIAEglELTVSAVIPLWDDYFGPGYGVPTSEGMEIVKK 265
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1675082402 243 FSKQHTIPLEPIYSGKMLFAVWQLIEQGYFaKGSHIIAVHTGGLQGL 289
Cdd:TIGR01275 266 VASLEGIILDPVYTGKAFYGLIDGIRKKEF-GDKPILFIHTGGIPGL 311
PRK14045 PRK14045
1-aminocyclopropane-1-carboxylate deaminase; Provisional
5-288 4.81e-27

1-aminocyclopropane-1-carboxylate deaminase; Provisional


Pssm-ID: 172537 [Multi-domain]  Cd Length: 329  Bit Score: 107.67  E-value: 4.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402   5 FESPVQTIhhPLLAAR-KVQLSIKRDDLIHPQISGNKWRKLKFNLQAMQQQKKSELLTFGGAFSNHIHATATAGKLFGFK 83
Cdd:PRK14045   20 WETPIQYL--PNISRElGADVYVKRDDLTGLGIGGNKIRKLEYLLGDALSRGADVVITVGAVHSNHAFVTGLAAKKLGLD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402  84 THGIIRGPELDEANPTLNYAKQCGMSLHPVNRITYRLRHDHTYLAQLQAQFPNAYILPEGGTNAAALLG----CKELAQS 159
Cdd:PRK14045   98 AVLVLRGKEELKGNYLLDKIMGIETRVYEAKDSFELMKYAEEVAEELKGEGRKPYIIPPGGASPVGTLGyvraVGEIATQ 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402 160 LPSS----DVIVCPTGSGGTLAGLIEGAP---QHTKLLGVAVLKQAHYLIDEIKQLSNKA-------NQQQNWQLLcDFH 225
Cdd:PRK14045  178 VKKLgvrfDSIVVAVGSGGTLAGLSLGLAilnAEWRVVGIAVGSFGEKMKEKVKNLVKKTkellgvkVKVQEPELY-DYS 256
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1675082402 226 DGGYGKFSDNLWQFCQTFSKQHTIPLEPIYSGKMLFAVWQLIEQGYFakGSHIIAVHTGGLQG 288
Cdd:PRK14045  257 FGEYGKITKEVAKLIRSVGTMEGLILDPVYTGKAFYGLMDLAKKGEL--GEKILFIHTGGISG 317
ACCD cd06449
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ...
21-285 8.39e-22

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: 92.87  E-value: 8.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402  21 KVQLSIKRDDLIH-PQISGNKWRKLKFNLQAMQQQKKSELLTFGGAFSNHIHATATAGKLFGFKTHGIIRGPEldeANPT 99
Cdd:cd06449    16 KVEIYAKRDDCNSgLAFGGNKIRKLEYLLPDALAKGADTLVTVGGIQSNHTRQVAAVAAKLGLKCVLVQENWV---PYSD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402 100 LNYAKQCGMSLHPVNRITYRLrHDHTYLAQLQAQFPNA-----------YILPEGGT-NAAALLG-----------CKEL 156
Cdd:cd06449    93 AVYDRVGNILLSRIMGADVRL-VSAGFDIGIRKSFEEAaeeveakggkpYVIPAGGSeHPLGGLGyvgfvleiaqqEEEL 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402 157 AQSLpssDVIVCPTGSGGTLAGLIEGAPQ---HTKLLGVAVLKQAHylideiKQLSNKANQQQN-------------WQL 220
Cdd:cd06449   172 GFKF---DSIVVCSVTGSTHAGLSVGLAAlgrQRRVIGIDASAKPE------KTKAQVLRIAQAklaeeglevkeedVVL 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1675082402 221 LCDFHDGGYGKFSDNLWQFCQTFSKQHTIPLEPIYSGKMLFAVWQLIEQGYFAKGSHIIAVHTGG 285
Cdd:cd06449   243 DDDYAAPEYGIPNDETIEAIKLCARLEGIITDPVYEGKSMQGMIDLVRNGEFKEGSKVLFIHLGG 307
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
14-284 1.63e-11

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: 63.48  E-value: 1.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402  14 HPLLAARKVQLSIKRDDLiHPqISGNKWRKLkFNLQAMQQQKKSELLTFGGAFSNHIHATATAGKLFGFKTHGIIrgPEl 93
Cdd:pfam00291  14 PRLSKELGVDVYLKLESL-NP-TGSFKDRGA-LNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIVV--PE- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402  94 DEANPTLNYAKQCGMSLHPVNRITYRLRHdhtYLAQLQAQFPNAYILPEGGtNAAALLGCK----ELAQSL-PSSDVIVC 168
Cdd:pfam00291  88 DAPPGKLLLMRALGAEVVLVGGDYDEAVA---AARELAAEGPGAYYINQYD-NPLNIEGYGtiglEILEQLgGDPDAVVV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402 169 PTGSGGTLAG----LIEGAPqHTKLLGV-----------------AVLKQAHYLIDEIKQLSNKANqqQNWQLLCDFHDG 227
Cdd:pfam00291 164 PVGGGGLIAGiargLKELGP-DVRVIGVepegapalarslaagrpVPVPVADTIADGLGVGDEPGA--LALDLLDEYVGE 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1675082402 228 GYGKFSDNLWQFCQTFSKQHTIPLEPiYSGKMLFAVwQLIEQGYFAKGSHIIAVHTG 284
Cdd:pfam00291 241 VVTVSDEEALEAMRLLARREGIVVEP-SSAAALAAL-KLALAGELKGGDRVVVVLTG 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
7-285 1.32e-04

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: 42.50  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402   7 SPVQTIHHpLLAARKVQLSIKRDDLihpQISG-NKWRKLKFN-LQAMQQQKKSELLTFGGAFSNHIHATATAGKLFGFKT 84
Cdd:cd00640     1 TPLVRLKR-LSKLGGANIYLKLEFL---NPTGsFKDRGALNLiLLAEEEGKLPKGVIIESTGGNTGIALAAAAARLGLKC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402  85 HgIIrgpeLDEANPTLNYAKqcgMSLHPVNRITYRLRHDH--TYLAQLQAQFPNAYILPeGGTNAAALLG----CKELAQ 158
Cdd:cd00640    77 T-IV----MPEGASPEKVAQ---MRALGAEVVLVPGDFDDaiALAKELAEEDPGAYYVN-QFDNPANIAGqgtiGLEILE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402 159 SLPSS--DVIVCPTGSGGTLAG----LIEGAPqHTKLLGVavlkQAH-YLIDEikqlsnkanqqqnwqllcdfhdggygk 231
Cdd:cd00640   148 QLGGQkpDAVVVPVGGGGNIAGiaraLKELLP-NVKVIGV----EPEvVTVSD--------------------------- 195
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1675082402 232 fsDNLWQFCQTFSKQHTIPLEPiYSGKMLFAVWQLIEQGyfAKGSHIIAVHTGG 285
Cdd:cd00640   196 --EEALEAIRLLAREEGILVEP-SSAAALAAALKLAKKL--GKGKTVVVILTGG 244
PRK12390 PRK12390
1-aminocyclopropane-1-carboxylate deaminase; Provisional
165-294 4.43e-04

1-aminocyclopropane-1-carboxylate deaminase; Provisional


Pssm-ID: 183494  Cd Length: 337  Bit Score: 41.17  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675082402 165 VIVCpTGSGGTLAGLIEG-APQ--HTKLLGV---AVLKQAHYLIDEIKQlsNKANQ--------QQNWQLLCDFHDGGYG 230
Cdd:PRK12390  193 IVVC-SVTGSTQAGMVVGfAADgrARRVIGIdasAKPEQTRAQVLRIAR--NTAELvelgrditEDDVVLDERYAGPEYG 269
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1675082402 231 KFSDNLWQFCQTFSKQHTIPLEPIYSGKMLFAVWQLIEQGYFAKGSHIIAVHTGGLQGLNGLKY 294
Cdd:PRK12390  270 LPNEGTLEAIRLCARLEGMLTDPVYEGKSMHGMIDLVRKGEFPEGSKVLYAHLGGVPALNAYSF 333
 
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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