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Conserved domains on  [gi|685504957|ref|NP_001288753|]
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antizyme inhibitor 2 isoform 2 [Homo sapiens]

Protein Classification

type III PLP-dependent enzyme( domain architecture ID 10089786)

type III PLP (pyridoxal 5-phosphate)-dependent enzyme similar to Selenomonas ruminantium lysine/ornithine decarboxylase, and human ornithine decarboxylase and antizyme inhibitor 2

CATH:  3.20.20.10
EC:  4.1.1.-
Gene Ontology:  GO:0003824
PubMed:  15189147|8690703
SCOP:  4003520

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
1-313 4.06e-152

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily is composed mainly of eukaryotic ornithine decarboxylases (ODC, EC 4.1.1.17) and ODC-like enzymes from prokaryotes represented by Vibrio vulnificus LysineOrnithine decarboxylase. These are fold type III PLP-dependent enzymes that differ from most bacterial ODCs which are fold type I PLP-dependent enzymes. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. Members of this subfamily contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity. Also members of this subfamily are proteins with homology to ODC but do not possess any catalytic activity, the Antizyme inhibitor (AZI) and ODC-paralogue (ODC-p). AZI binds to the regulatory protein Antizyme with a higher affinity than ODC and prevents ODC degradation. ODC-p is a novel ODC-like protein, present only in mammals, that is specifically exressed in the brain and testes. ODC-p may function as a tissue-specific antizyme inhibitory protein.


:

Pssm-ID: 143482 [Multi-domain]  Cd Length: 362  Bit Score: 432.69  E-value: 4.06e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957   1 MELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSL 80
Cdd:cd00622   59 IELVLGLGVSPERIIFANPCKSISDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADP 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957  81 KSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTE-GAKVRFEEIAS 159
Cdd:cd00622  139 EEARELLRRAKELGLNVVGVSFHVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYdGVVPSFEEIAA 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957 160 VINSALDLYFPEGcGVDIFAELGRYYVTSAFTVAVSIIAKKEVLLDQPGREeengstsktivYHLDEGVYGIFNSVLFDN 239
Cdd:cd00622  219 VINRALDEYFPDE-GVRIIAEPGRYLVASAFTLAVNVIAKRKRGDDDRERW-----------YYLNDGVYGSFNEILFDH 286
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685504957 240 ICPTPILQKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQ-LHVGDWLVFDNMGAYTVGMGSPFWGTQACHITY 313
Cdd:cd00622  287 IRYPPRVLKDGGRDGELYPSSLWGPTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVY 361
 
Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
1-313 4.06e-152

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily is composed mainly of eukaryotic ornithine decarboxylases (ODC, EC 4.1.1.17) and ODC-like enzymes from prokaryotes represented by Vibrio vulnificus LysineOrnithine decarboxylase. These are fold type III PLP-dependent enzymes that differ from most bacterial ODCs which are fold type I PLP-dependent enzymes. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. Members of this subfamily contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity. Also members of this subfamily are proteins with homology to ODC but do not possess any catalytic activity, the Antizyme inhibitor (AZI) and ODC-paralogue (ODC-p). AZI binds to the regulatory protein Antizyme with a higher affinity than ODC and prevents ODC degradation. ODC-p is a novel ODC-like protein, present only in mammals, that is specifically exressed in the brain and testes. ODC-p may function as a tissue-specific antizyme inhibitory protein.


Pssm-ID: 143482 [Multi-domain]  Cd Length: 362  Bit Score: 432.69  E-value: 4.06e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957   1 MELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSL 80
Cdd:cd00622   59 IELVLGLGVSPERIIFANPCKSISDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADP 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957  81 KSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTE-GAKVRFEEIAS 159
Cdd:cd00622  139 EEARELLRRAKELGLNVVGVSFHVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYdGVVPSFEEIAA 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957 160 VINSALDLYFPEGcGVDIFAELGRYYVTSAFTVAVSIIAKKEVLLDQPGREeengstsktivYHLDEGVYGIFNSVLFDN 239
Cdd:cd00622  219 VINRALDEYFPDE-GVRIIAEPGRYLVASAFTLAVNVIAKRKRGDDDRERW-----------YYLNDGVYGSFNEILFDH 286
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685504957 240 ICPTPILQKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQ-LHVGDWLVFDNMGAYTVGMGSPFWGTQACHITY 313
Cdd:cd00622  287 IRYPPRVLKDGGRDGELYPSSLWGPTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVY 361
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
1-293 7.56e-91

Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent decarboxylases act on ornithine, lysine, arginine and related substrates.


Pssm-ID: 459745 [Multi-domain]  Cd Length: 340  Bit Score: 275.90  E-value: 7.56e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957    1 MELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMELAKVVKSHPS--AKMVLCIATD---DSHSLSC--LS 73
Cdd:pfam00278  57 LERALAAGVDPERIVFAGPGKTDSEIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRINPDvdaGTHKISTggLS 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957   74 LKFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGT--EGAK 151
Cdd:pfam00278 137 SKFGIDLEDAPELLALAKELGLNVVGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPyrDEPP 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957  152 VRFEEIASVINSALDLYFPEgcGVDIFAELGRYYVTSAFTVAVSIIAKKEvlldqpgreeengSTSKTIVYhLDEGVYGI 231
Cdd:pfam00278 217 PDFEEYAAAIREALDEYFPP--DLEIIAEPGRYLVANAGVLVTRVIAVKT-------------GGGKTFVI-VDAGMNDL 280
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685504957  232 FNSVLFDNICPTPIlqKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMG 293
Cdd:pfam00278 281 FRPALYDAYHPIPV--VKEPGEGPLETYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
1-303 1.77e-37

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


Pssm-ID: 439790 [Multi-domain]  Cd Length: 417  Bit Score: 139.13  E-value: 1.77e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957   1 MELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMELAK---VVKSHPSAKMVLC-------------IATD 64
Cdd:COG0019   85 LRLALAAGFPPERIVFSGNGKSEEELEEALELGVGHINVDSLSELERlaeLAAELGKRAPVGLrvnpgvdagtheyISTG 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957  65 DSHSlsclslKFGVSLKSCRHLLENAKKH-HVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGG 143
Cdd:COG0019  165 GKDS------KFGIPLEDALEAYRRAAALpGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGG 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957 144 FPGT---EGAKVRFEEIASVINSALDLYFpeGCGVDIFAELGRYYVTSAFTVAVSIIAKKEVlldqpgreeengsTSKTI 220
Cdd:COG0019  239 LGIPyteGDEPPDLEELAAAIKEALEELC--GLGPELILEPGRALVGNAGVLLTRVLDVKEN-------------GGRRF 303
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957 221 VYhLDEGVYgifnsvlfDNICPT------PILQKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGA 294
Cdd:COG0019  304 VI-VDAGMN--------DLMRPAlygayhPIVPVGRPSGAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGA 374

                 ....*....
gi 685504957 295 YTVGMGSPF 303
Cdd:COG0019  375 YGFSMASNY 383
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
75-301 9.13e-08

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 53.93  E-value: 9.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957  75 KFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQsIAD--ARLVFEMGTelghkMHVLDLGGGFPGTEGAKV 152
Cdd:PRK08961 641 KFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHWRR-MADelASFARRFPD-----VRTIDLGGGLGIPESAGD 714
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957 153 R---FEEIASVINSALDLYfPegcGVDIFAELGRYYVtsaftvavsiiAKKEVLLDQPGREEENGStsktiVYH--LDEG 227
Cdd:PRK08961 715 EpfdLDALDAGLAEVKAQH-P---GYQLWIEPGRYLV-----------AEAGVLLARVTQVKEKDG-----VRRvgLETG 774
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685504957 228 VYGIFNSVLFD---NICPTPILqkkpsTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGS 301
Cdd:PRK08961 775 MNSLIRPALYGayhEIVNLSRL-----DEPAAGTADVVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMSS 846
 
Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
1-313 4.06e-152

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily is composed mainly of eukaryotic ornithine decarboxylases (ODC, EC 4.1.1.17) and ODC-like enzymes from prokaryotes represented by Vibrio vulnificus LysineOrnithine decarboxylase. These are fold type III PLP-dependent enzymes that differ from most bacterial ODCs which are fold type I PLP-dependent enzymes. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. Members of this subfamily contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity. Also members of this subfamily are proteins with homology to ODC but do not possess any catalytic activity, the Antizyme inhibitor (AZI) and ODC-paralogue (ODC-p). AZI binds to the regulatory protein Antizyme with a higher affinity than ODC and prevents ODC degradation. ODC-p is a novel ODC-like protein, present only in mammals, that is specifically exressed in the brain and testes. ODC-p may function as a tissue-specific antizyme inhibitory protein.


Pssm-ID: 143482 [Multi-domain]  Cd Length: 362  Bit Score: 432.69  E-value: 4.06e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957   1 MELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSL 80
Cdd:cd00622   59 IELVLGLGVSPERIIFANPCKSISDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADP 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957  81 KSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTE-GAKVRFEEIAS 159
Cdd:cd00622  139 EEARELLRRAKELGLNVVGVSFHVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYdGVVPSFEEIAA 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957 160 VINSALDLYFPEGcGVDIFAELGRYYVTSAFTVAVSIIAKKEVLLDQPGREeengstsktivYHLDEGVYGIFNSVLFDN 239
Cdd:cd00622  219 VINRALDEYFPDE-GVRIIAEPGRYLVASAFTLAVNVIAKRKRGDDDRERW-----------YYLNDGVYGSFNEILFDH 286
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685504957 240 ICPTPILQKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQ-LHVGDWLVFDNMGAYTVGMGSPFWGTQACHITY 313
Cdd:cd00622  287 IRYPPRVLKDGGRDGELYPSSLWGPTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVY 361
PLPDE_III_ODC_like_AZI cd06831
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ...
1-320 1.90e-111

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme Inhibitor; Antizyme inhibitor (AZI) is homologous to the fold type III PLP-dependent enzyme ODC but does not retain any decarboxylase activity. Like ODC, AZI is presumed to exist as a homodimer. Antizyme is a regulatory protein that binds directly to the ODC monomer to block its active site, leading to its degradation by the 26S proteasome. AZI binds to Antizyme with a higher affinity than ODC, preventing the formation of the Antizyme-ODC complex. Thus, AZI blocks the ability of Antizyme to promote ODC degradation, which leads to increased ODC enzymatic activity and polyamine levels. AZI also prevents the degradation of other proteins regulated by Antizyme, such as cyclin D1.


Pssm-ID: 143504  Cd Length: 394  Bit Score: 330.66  E-value: 1.90e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957   1 MELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSL 80
Cdd:cd06831   70 MALVQELGVSPENIIYTNPCKQASQIKYAAKVGVNIMTCDNEIELKKIARNHPNAKLLLHIATEDNIGGEEMNMKFGTTL 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957  81 KSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTEgakVRFEEIASV 160
Cdd:cd06831  150 KNCRHLLECAKELDVQIVGVKFHVSSSCKEYQTYVHALSDARCVFDMAEEFGFKMNMLDIGGGFTGSE---IQLEEVNHV 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957 161 INSALDLYFPEGCGVDIFAELGRYYVTSAFTVAVSIIAKKEVLLDQ-PGREEENGSTSKTIVYHLDEGVYGIFNSVLFDN 239
Cdd:cd06831  227 IRPLLDVYFPEGSGIQIIAEPGSYYVSSAFTLAVNVIAKKAVENDKhLSSVEKNGSDEPAFVYYMNDGVYGSFASKLSEK 306
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957 240 ICPTPILQKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGSPFWGTQACHITYAMSRVA 319
Cdd:cd06831  307 LNTTPEVHKKYKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGAGSLHEPSTFNDFQRPAIYYMMSFSD 386

                 .
gi 685504957 320 W 320
Cdd:cd06831  387 W 387
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
1-293 7.56e-91

Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent decarboxylases act on ornithine, lysine, arginine and related substrates.


Pssm-ID: 459745 [Multi-domain]  Cd Length: 340  Bit Score: 275.90  E-value: 7.56e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957    1 MELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMELAKVVKSHPS--AKMVLCIATD---DSHSLSC--LS 73
Cdd:pfam00278  57 LERALAAGVDPERIVFAGPGKTDSEIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRINPDvdaGTHKISTggLS 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957   74 LKFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGT--EGAK 151
Cdd:pfam00278 137 SKFGIDLEDAPELLALAKELGLNVVGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPyrDEPP 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957  152 VRFEEIASVINSALDLYFPEgcGVDIFAELGRYYVTSAFTVAVSIIAKKEvlldqpgreeengSTSKTIVYhLDEGVYGI 231
Cdd:pfam00278 217 PDFEEYAAAIREALDEYFPP--DLEIIAEPGRYLVANAGVLVTRVIAVKT-------------GGGKTFVI-VDAGMNDL 280
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685504957  232 FNSVLFDNICPTPIlqKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMG 293
Cdd:pfam00278 281 FRPALYDAYHPIPV--VKEPGEGPLETYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
PLPDE_III_ODC_DapDC_like cd06810
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ...
1-307 7.91e-81

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate Decarboxylases, and Related Enzymes; This family includes eukaryotic ornithine decarboxylase (ODC, EC 4.1.1.17), diaminopimelate decarboxylase (DapDC, EC 4.1.1.20), plant and prokaryotic biosynthetic arginine decarboxylase (ADC, EC 4.1.1.19), carboxynorspermidine decarboxylase (CANSDC), and ODC-like enzymes from diverse bacterial species. These proteins are fold type III PLP-dependent enzymes that catalyze essential steps in the biosynthesis of polyamine and lysine. ODC and ADC participate in alternative pathways of the biosynthesis of putrescine, which is the precursor of aliphatic polyamines in many organisms. ODC catalyzes the direct synthesis of putrescine from L-ornithine, while ADC converts L-arginine to agmatine, which is hydrolysed to putrescine by agmatinase in a pathway that exists only in plants and bacteria. DapDC converts meso-2,6-diaminoheptanedioate to L-lysine, which is the final step of lysine biosynthesis. CANSDC catalyzes the decarboxylation of carboxynorspermidine, which is the last step in the synthesis of norspermidine. The PLP-dependent decarboxylases in this family contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Prokaryotic ornithine, lysine and biodegradative arginine decarboxylases are fold type I PLP-dependent enzymes and are not included in this family.


Pssm-ID: 143485 [Multi-domain]  Cd Length: 368  Bit Score: 251.45  E-value: 7.91e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957   1 MELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMELAKVV----KSHPSAKMVLCIATDDSH----SLSCL 72
Cdd:cd06810   59 LALALAAGVPPERIIFTGPAKSVSEIEAALASGVDHIVVDSLDELERLNelakKLGPKARILLRVNPDVSAgthkISTGG 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957  73 SL-KFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGT-EGA 150
Cdd:cd06810  139 LKsKFGLSLSEARAALERAKELDLRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPyDEQ 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957 151 KVRFEEIASVINSALDLYFPEGCGVDIFAELGRYYVTSAFTVAVSIIAKKEVLldqpgreeengstsKTIVYHLDEGVYG 230
Cdd:cd06810  219 PLDFEEYAALINPLLKKYFPNDPGVTLILEPGRYIVAQAGVLVTRVVAVKVNG--------------GRFFAVVDGGMNH 284
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685504957 231 IFNSVLFDNICPTPILQKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGSPFWGTQ 307
Cdd:cd06810  285 SFRPALAYDAYHPITPLKAPGPDEPLVPATLAGPLCDSGDVIGRDRLLPELEVGDLLVFEDMGAYGFSESSNFNSHP 361
Orn_Arg_deC_N pfam02784
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ...
1-186 5.91e-71

Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent decarboxylases acting on ornithine, lysine, arginine and related substrates This domain has a TIM barrel fold.


Pssm-ID: 397077 [Multi-domain]  Cd Length: 241  Bit Score: 221.77  E-value: 5.91e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957    1 MELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSL 80
Cdd:pfam02784  51 LERVLAAGVPPERIIFANPCKQRSFLRYALEVGVGCVTVDNVDELEKLARLAPEARVLLRIKPDDSAATCPLSSKFGADL 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957   81 -KSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFpGTE----GAKVRFE 155
Cdd:pfam02784 131 dEDVEALLEAAKLLNLQVVGVSFHVGSGCTDAEAFVLALEDARGVFDQGAELGFNLKILDLGGGF-GVDytegEEPLDFE 209
                         170       180       190
                  ....*....|....*....|....*....|.
gi 685504957  156 EIASVINSALDLYFPEGCGVDIFAELGRYYV 186
Cdd:pfam02784 210 EYANVINEALEEYFPGDPGVTIIAEPGRYFV 240
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
1-303 1.77e-37

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


Pssm-ID: 439790 [Multi-domain]  Cd Length: 417  Bit Score: 139.13  E-value: 1.77e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957   1 MELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMELAK---VVKSHPSAKMVLC-------------IATD 64
Cdd:COG0019   85 LRLALAAGFPPERIVFSGNGKSEEELEEALELGVGHINVDSLSELERlaeLAAELGKRAPVGLrvnpgvdagtheyISTG 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957  65 DSHSlsclslKFGVSLKSCRHLLENAKKH-HVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGG 143
Cdd:COG0019  165 GKDS------KFGIPLEDALEAYRRAAALpGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGG 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957 144 FPGT---EGAKVRFEEIASVINSALDLYFpeGCGVDIFAELGRYYVTSAFTVAVSIIAKKEVlldqpgreeengsTSKTI 220
Cdd:COG0019  239 LGIPyteGDEPPDLEELAAAIKEALEELC--GLGPELILEPGRALVGNAGVLLTRVLDVKEN-------------GGRRF 303
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957 221 VYhLDEGVYgifnsvlfDNICPT------PILQKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGA 294
Cdd:COG0019  304 VI-VDAGMN--------DLMRPAlygayhPIVPVGRPSGAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGA 374

                 ....*....
gi 685504957 295 YTVGMGSPF 303
Cdd:COG0019  375 YGFSMASNY 383
PLPDE_III cd06808
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
1-148 3.83e-33

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme family is predominantly composed of two-domain proteins with similarity to bacterial alanine racemases (AR) including eukaryotic ornithine decarboxylases (ODC), prokaryotic diaminopimelate decarboxylases (DapDC), biosynthetic arginine decarboxylases (ADC), carboxynorspermidine decarboxylases (CANSDC), and similar proteins. AR-like proteins contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. These proteins play important roles in the biosynthesis of amino acids and polyamine. The family also includes the single-domain YBL036c-like proteins, which contain a single PLP-binding TIM-barrel domain without any N- or C-terminal extensions. Due to the lack of a second domain, these proteins may possess only limited D- to L-alanine racemase activity or non-specific racemase activity.


Pssm-ID: 143484 [Multi-domain]  Cd Length: 211  Bit Score: 122.43  E-value: 3.83e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957   1 MELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMELAKV----VKSHPSAKMVLCIATDDshslscLSLKF 76
Cdd:cd06808   49 ALLLRAAGIPPEPILFLGPCKQVSELEDAAEQGVIVVTVDSLEELEKLeeaaLKAGPPARVLLRIDTGD------ENGKF 122
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 685504957  77 GVSLKSCRHLLENAKKH-HVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTE 148
Cdd:cd06808  123 GVRPEELKALLERAKELpHLRLVGLHTHFGSADEDYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILY 195
PLPDE_III_DapDC cd06828
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ...
1-301 2.19e-24

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; Diaminopimelate decarboxylase (DapDC, EC 4.1.1.20) participates in the last step of lysine biosynthesis. It converts meso-2,6-diaminoheptanedioate to L-lysine. It is a fold type III PLP-dependent enzyme that contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. DapDC exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity.


Pssm-ID: 143501 [Multi-domain]  Cd Length: 373  Bit Score: 102.56  E-value: 2.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957   1 MELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIA--------------TDDS 66
Cdd:cd06828   62 LYRALKAGFPPERIVFTGNGKSDEELELALELGILRINVDSLSELERLGEIAPELGKGAPVAlrvnpgvdagthpyISTG 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957  67 HSLSclslKFGVSLKSCRHLLENAKK-HHVEVVGVSFHIGSGCPDPQAYAQSiadARLVFEMGTEL---GHKMHVLDLGG 142
Cdd:cd06828  142 GKDS----KFGIPLEQALEAYRRAKElPGLKLVGLHCHIGSQILDLEPFVEA---AEKLLDLAAELrelGIDLEFLDLGG 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957 143 GF--PGTEGAK-VRFEEIASVINSALDLYFPEGCGVDIFAELGRYYVTSAFTVAVSIIAKKEvlldqpgreeengSTSKT 219
Cdd:cd06828  215 GLgiPYRDEDEpLDIEEYAEAIAEALKELCEGGPDLKLIIEPGRYIVANAGVLLTRVGYVKE-------------TGGKT 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957 220 IVyHLDEGvygiFNsvlfDNICPT------PILQKKPSTEQPLYSSSLWGPAvdgC---DCVAEGLWLPQLHVGDWLVFD 290
Cdd:cd06828  282 FV-GVDAG----MN----DLIRPAlygayhEIVPVNKPGEGETEKVDVVGPI---CesgDVFAKDRELPEVEEGDLLAIH 349
                        330
                 ....*....|.
gi 685504957 291 NMGAYTVGMGS 301
Cdd:cd06828  350 DAGAYGYSMSS 360
PLPDE_III_MccE_like cd06841
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ...
1-303 2.01e-23

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of uncharacterized proteins with similarity to Escherichia coli MccE, a hypothetical protein that is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine. Most members of this subfamily share the same domain architecture as ODC and DapDC. A few members, including Escherichia coli MccE, contain an additional acetyltransferase domain at the C-terminus.


Pssm-ID: 143508 [Multi-domain]  Cd Length: 379  Bit Score: 100.03  E-value: 2.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957   1 MELVQHIGIPASKIICANPCKQIAQIKYAAKHG--IQLLSFDNEMELAKVVKSHP-SAKMVLCIATD-DSHSLSclslKF 76
Cdd:cd06841   68 YELALKLGVPGKRIIFNGPYKSKEELEKALEEGalINIDSFDELERILEIAKELGrVAKVGIRLNMNyGNNVWS----RF 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957  77 GVSLKSCRHLLENAKKH----HVEVVGVSFHIGSGCPDPQAYAQSIADarLVFEMGTELGHKMHVLDLGGGFPG------ 146
Cdd:cd06841  144 GFDIEENGEALAALKKIqeskNLSLVGLHCHVGSNILNPEAYSAAAKK--LIELLDRLFGLELEYLDLGGGFPAktplsl 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957 147 ---TEGAKVRFEEIASVINSALDLYFPEGCG-VDIFAELGRYYVTSAFTVAVSIIAKKEVlldqPGREeengstsktiVY 222
Cdd:cd06841  222 aypQEDTVPDPEDYAEAIASTLKEYYANKENkPKLILEPGRALVDDAGYLLGRVVAVKNR----YGRN----------IA 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957 223 HLDEGvygIFNSVLFDNICPtPILQKKPSTEQPLYSSS-LWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGS 301
Cdd:cd06841  288 VTDAG---INNIPTIFWYHH-PILVLRPGKEDPTSKNYdVYGFNCMESDVLFPNVPLPPLNVGDILAIRNVGAYNMTQSN 363

                 ..
gi 685504957 302 PF 303
Cdd:cd06841  364 QF 365
PLPDE_III_ODC_DapDC_like_1 cd06836
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ...
1-299 2.85e-12

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with similarity to Ornithine and Diaminopimelate Decarboxylases; This subfamily contains uncharacterized proteins with similarity to ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine. Proteins in this subfamily may function as PLP-dependent decarboxylases. Homodimer formation and the presence of the PLP cofactor may be required for catalytic activity.


Pssm-ID: 143505 [Multi-domain]  Cd Length: 379  Bit Score: 67.03  E-value: 2.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957   1 MELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQlLSFDNEMELAKV---VKSHPSAKMVLCI--------ATDDSHSL 69
Cdd:cd06836   61 LELALAAGFPPERIVFDSPAKTRAELREALELGVA-INIDNFQELERIdalVAEFKEASSRIGLrvnpqvgaGKIGALST 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957  70 SCLSLKFGVSLK-SCRHLLENAKKHHVEVVGVSFHIGS-GCPDPQAyaqsIADARLVFEMGTELGHKM-----HVLDLGG 142
Cdd:cd06836  140 ATATSKFGVALEdGARDEIIDAFARRPWLNGLHVHVGSqGCELSLL----AEGIRRVVDLAEEINRRVgrrqiTRIDIGG 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957 143 GFP---GTEGAKVRFEEIASVINSALDLYFPEGCGVdiFAELGRYYVTSA-FTVAVSIIAKK----EVLLDQPGREEENG 214
Cdd:cd06836  216 GLPvnfESEDITPTFADYAAALKAAVPELFDGRYQL--VTEFGRSLLAKCgTIVSRVEYTKSsggrRIAITHAGAQVATR 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957 215 STSKTIVYHLDEGVYgifnsvlfdnicpTPilQKKPSTEqPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGA 294
Cdd:cd06836  294 TAYAPDDWPLRVTVF-------------DA--NGEPKTG-PEVVTDVAGPCCFAGDVLAKERALPPLEPGDYVAVHDTGA 357

                 ....*
gi 685504957 295 YTVGM 299
Cdd:cd06836  358 YYFSS 362
PLPDE_III_Y4yA_like cd06842
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ...
2-145 4.24e-12

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the hypothetical Rhizobium sp. protein Y4yA and similar uncharacterized bacterial proteins. These proteins are homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine. Proteins in this subfamily may function as PLP-dependent decarboxylases.


Pssm-ID: 143509 [Multi-domain]  Cd Length: 423  Bit Score: 66.90  E-value: 4.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957   2 ELVQHI--GIPASKIICANPCKQIAQIKYAAKHGIqLLSFDNEMELAKVVK-----SHPSAKMVLCIATDDSHSLSclsl 74
Cdd:cd06842   70 ELRQALaaGVRGDRIVATGPAKTDEFLWLAVRHGA-TIAVDSLDELDRLLAlargyTTGPARVLLRLSPFPASLPS---- 144
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 685504957  75 KFGVSLKSCRHLLENAKKH--HVEVVGVSFHIGSGCPDPQAYAqsIADARLVFEMGTELGHKMHVLDLGGGFP 145
Cdd:cd06842  145 RFGMPAAEVRTALERLAQLreRVRLVGFHFHLDGYSAAQRVAA--LQECLPLIDRARALGLAPRFIDIGGGFP 215
PLPDE_III_Btrk_like cd06839
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ...
1-295 5.22e-12

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is composed of Bacillus circulans BtrK decarboxylase and similar proteins. These proteins are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases, eukaryotic ornithine decarboxylases and diaminopimelate decarboxylases. BtrK is presumed to function as a PLP-dependent decarboxylase involved in the biosynthesis of the aminoglycoside antibiotic butirosin. Homodimer formation and the presence of the PLP cofactor may be required for catalytic activity.


Pssm-ID: 143506 [Multi-domain]  Cd Length: 382  Bit Score: 66.46  E-value: 5.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957   1 MELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMELAKV----VKSHPSAKMVLCIATDDSHSLSCLSL-- 74
Cdd:cd06839   65 LALALEAGVPPEKILFAGPGKSDAELRRAIEAGIGTINVESLEELERIdalaEEHGVVARVALRINPDFELKGSGMKMgg 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957  75 ---KFGVS---LKSCRHLLENAkkHHVEVVGvsFHI--GSGCPDPQAYAQSIADA-RLVFEMGTELGHKMHVLDLGGGF- 144
Cdd:cd06839  145 gpsQFGIDveeLPAVLARIAAL--PNLRFVG--LHIypGTQILDADALIEAFRQTlALALRLAEELGLPLEFLDLGGGFg 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957 145 -P-GTEGAKVRFEEIASVINSALDLYFPEGCGVDIFAELGRYYVTSAFTVAVSIIAKKEvlldqpgreeengSTSKTIVY 222
Cdd:cd06839  221 iPyFPGETPLDLEALGAALAALLAELGDRLPGTRVVLELGRYLVGEAGVYVTRVLDRKV-------------SRGETFLV 287
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685504957 223 hLDEGVY------GIFNSVLFDNIcPTPILQKkpSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAY 295
Cdd:cd06839  288 -TDGGMHhhlaasGNFGQVLRRNY-PLAILNR--MGGEERETVTVVGPLCTPLDLLGRNVELPPLEPGDLVAVLQSGAY 362
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
75-301 9.13e-08

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 53.93  E-value: 9.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957  75 KFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQsIAD--ARLVFEMGTelghkMHVLDLGGGFPGTEGAKV 152
Cdd:PRK08961 641 KFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHWRR-MADelASFARRFPD-----VRTIDLGGGLGIPESAGD 714
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957 153 R---FEEIASVINSALDLYfPegcGVDIFAELGRYYVtsaftvavsiiAKKEVLLDQPGREEENGStsktiVYH--LDEG 227
Cdd:PRK08961 715 EpfdLDALDAGLAEVKAQH-P---GYQLWIEPGRYLV-----------AEAGVLLARVTQVKEKDG-----VRRvgLETG 774
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685504957 228 VYGIFNSVLFD---NICPTPILqkkpsTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGS 301
Cdd:PRK08961 775 MNSLIRPALYGayhEIVNLSRL-----DEPAAGTADVVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMSS 846
PLPDE_III_Bif_AspK_DapDC cd06840
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ...
75-301 1.55e-07

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase/Diaminopimelate Decarboxylase; Bifunctional aspartate kinase/diaminopimelate decarboxylase (AspK/DapDC, EC 4.1.1.20/EC 2.7.2.4) typically exists in bacteria. These proteins contain an N-terminal AspK region and a C-terminal DapDC region, which contains a PLP-binding TIM-barrel domain followed by beta-sandwich domain, characteristic of fold type III PLP-dependent enzymes. Members of this subfamily have not been fully characterized. Based on their sequence, these proteins may catalyze both reactions catalyzed by AspK and DapDC. AspK catalyzes the phosphorylation of L-aspartate to produce 4-phospho-L-aspartate while DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine.


Pssm-ID: 143507 [Multi-domain]  Cd Length: 368  Bit Score: 52.44  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957  75 KFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIAD-ARLVFEMGTelghkMHVLDLGGGFPGTEGAKVR 153
Cdd:cd06840  150 KFGLDVDELDEARDLAKKAGIIVIGLHAHSGSGVEDTDHWARHGDYlASLARHFPA-----VRILNVGGGLGIPEAPGGR 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957 154 FEEIASVINS--ALDLYFPegcGVDIFAELGRYyvtsaftvavsIIAKKEVLLdqpGREEENGSTSKTIVYHLDEGVYGI 231
Cdd:cd06840  225 PIDLDALDAAlaAAKAAHP---QYQLWMEPGRF-----------IVAESGVLL---ARVTQIKHKDGVRFVGLETGMNSL 287
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957 232 FNSVLFDniCPTPILQKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGS 301
Cdd:cd06840  288 IRPALYG--AYHEIVNLSRLDEPPAGNADVVGPICESGDVLGRDRLLPETEEGDVILIANAGAYGFCMAS 355
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
76-177 3.24e-05

Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 45.00  E-value: 3.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504957  76 FGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTEGAKVRFE 155
Cdd:COG1082   35 GDLDEADLAELRAALADHGLEISSLHAPGLNLAPDPEVREAALERLKRAIDLAAELGAKVVVVHPGSPPPPDLPPEEAWD 114
                         90       100
                 ....*....|....*....|..
gi 685504957 156 EIASVINSALDLYfpEGCGVDI 177
Cdd:COG1082  115 RLAERLRELAELA--EEAGVTL 134
 
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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