|
Name |
Accession |
Description |
Interval |
E-value |
| SpeA |
COG1166 |
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism]; |
1-630 |
0e+00 |
|
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism];
Pssm-ID: 440780 [Multi-domain] Cd Length: 633 Bit Score: 1147.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 1 MRKWRIEDSEELYNITGWGTSYFGINDKGHVVVTPRKD-GVEVDLKELVDELQLRDVAAPMLVRFPDILDNRIEKIANCF 79
Cdd:COG1166 2 MMDWTIEDARELYNIDRWGEGYFDINEKGHVTVRPDGDpGPSIDLYELVEELRERGLSLPVLLRFPDILRDRVERLNEAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 80 KQASDEYGYKAQNFIIYPIKVNQMRPVVEEIISHGKKFNLGLEAGSKPELHAVIAVNTDSDSLIICNGYKDESYIELALL 159
Cdd:COG1166 82 AKAIAEYGYQGRYRGVYPIKVNQQRHVVEEIVRAGKPYNFGLEAGSKPELMAVLALLDDPGSLIICNGYKDREYIRLALL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 160 AQKMGKRIFLVVEKMNELRLIAKMAKQLNVRPNIGIRIKLASSGSGKWEDSGGDASKFGLTSSELLEALDFLEKKDMKDC 239
Cdd:COG1166 162 GRKLGHKVIIVIEKLSELELILEEAKELGVKPLIGVRVKLASKGSGKWQNSGGERSKFGLSASEILEVVERLKEAGMLDC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 240 LKLIHFHIGSQVTKIRRIKTALREASQFYVQLHVMGFNVEFVDIGGGLGVDYDGTRSaNSESSVNYSIQEYVNDSISTLV 319
Cdd:COG1166 242 LQLLHFHLGSQIPNIRDIKRAVREAARFYAELRKLGAPIEYLDVGGGLGVDYDGSRS-NSDSSMNYSLQEYANDVVYAIK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 320 DASDKNGIPHPNIITESGRSLTAHHSVLIFEVLETATLPEMDEDFEVGENDHELVHELYEIWDNLNQSRMVEAWHDAQQI 399
Cdd:COG1166 321 EVCDEAGVPHPTIISESGRALTAHHSVLIFNVLDVERAPPEPPPPAPPEDAHELLRNLWETYESLTPRNLQECYHDALQY 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 400 REEALDLFSHGIVDLKTRAQIERLYWSVTREINQIASGLKHAPDEFRKLDKLLADKYFCNFSLFQSLPDSWAIDQIFPIM 479
Cdd:COG1166 401 KEEARSLFNLGYLSLEERALAEQLYWAICRKIRELLDPLEYHPEELDELNEKLADKYFCNFSLFQSLPDSWAIDQLFPIM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 480 PIQRLDEKPDRNATLQDITCDSDGKIANFISTRYVSHDLPVHSLKGKDAYYIGVFLVGAYQEILGDMHNLFGDTNAVHVT 559
Cdd:COG1166 481 PIHRLDEEPTRRAVLADITCDSDGKIDQFIDGQGVKSTLPLHPLKPGEPYYLGVFLVGAYQEILGDLHNLFGDTNAVHVR 560
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492422142 560 VD-DKGYSIDQVIDGETVAEVLDYVQYNPKKLVRTLETWVTKSVKEGRISVEEGKEFLSNYRSGLYGYTYLE 630
Cdd:COG1166 561 LDeDGGYEIEHVVEGDTVAEVLSYVQYDPEDLLERYRRQAEQAVRAGRLTPEERQRLLEEYEAGLRGYTYLE 632
|
|
| PRK05354 |
PRK05354 |
biosynthetic arginine decarboxylase; |
1-630 |
0e+00 |
|
biosynthetic arginine decarboxylase;
Pssm-ID: 235427 [Multi-domain] Cd Length: 634 Bit Score: 1106.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 1 MRKWRIEDSEELYNITGWGTSYFGINDKGHVVVTPRKD-GVEVDLKELVDELQLRDVAAPMLVRFPDILDNRIEKIANCF 79
Cdd:PRK05354 6 MSDWSIEDSRELYNIDHWGAGYFDINDKGHVSVRPDGDpGASIDLAELVKELRERGLRLPLLLRFPDILQDRVRSLNAAF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 80 KQASDEYGYKAQNFIIYPIKVNQMRPVVEEIISHGKKFNLGLEAGSKPELHAVIAVNTDSDSLIICNGYKDESYIELALL 159
Cdd:PRK05354 86 KKAIEEYGYQGDYRGVYPIKVNQQRRVVEEIVASGKPYNLGLEAGSKPELMAVLALAGDPGALIVCNGYKDREYIRLALI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 160 AQKMGKRIFLVVEKMNELRLIAKMAKQLNVRPNIGIRIKLASSGSGKWEDSGGDASKFGLTSSELLEALDFLEKKDMKDC 239
Cdd:PRK05354 166 GRKLGHKVFIVIEKLSELELILEEAKELGVKPRLGVRARLASQGSGKWQSSGGEKSKFGLSATEVLEAVERLREAGLLDC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 240 LKLIHFHIGSQVTKIRRIKTALREASQFYVQLHVMGFNVEFVDIGGGLGVDYDGTRSaNSESSVNYSIQEYVNDSISTLV 319
Cdd:PRK05354 246 LQLLHFHLGSQIANIRDIKTAVREAARFYVELRKLGAPIQYLDVGGGLGVDYDGTRS-QSDSSVNYSLQEYANDVVYTLK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 320 DASDKNGIPHPNIITESGRSLTAHHSVLIFEVLETATLPEMdEDFEVGENDHELVHELYEIWDNLNQSRMVEAWHDAQQI 399
Cdd:PRK05354 325 EICEEHGVPHPTIISESGRALTAHHAVLVFNVLGVESQEYE-EPPAPAEDAPPLLQNLWETYQEISERNLQEIYHDAQQD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 400 REEALDLFSHGIVDLKTRAQIERLYWSVTREINQIASGLKHAPDEFRKLDKLLADKYFCNFSLFQSLPDSWAIDQIFPIM 479
Cdd:PRK05354 404 LEEALTLFALGYLSLQERAWAEQLYWAICRKIQKLLDPKNRHPPELDELQERLADKYYVNFSLFQSLPDAWAIDQLFPIM 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 480 PIQRLDEKPDRNATLQDITCDSDGKIANFISTRYVSHDLPVHSLKGKDAYYIGVFLVGAYQEILGDMHNLFGDTNAVHVT 559
Cdd:PRK05354 484 PLHRLDEEPTRRAVLADITCDSDGKIDQFIDGQGIKTTLPLHELDPGEPYYLGFFLVGAYQEILGDMHNLFGDTNAVHVR 563
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492422142 560 VDDKG-YSIDQVIDGETVAEVLDYVQYNPKKLVRTLEtwvTKSVKEGRISVEEGKEFLSNYRSGLYGYTYLE 630
Cdd:PRK05354 564 VDEDGgYEIEHVIEGDTVADVLEYVQYDPKELLERLR---EKAVKEGKLSPEERQQLLEELEAGLRGYTYLE 632
|
|
| speA |
TIGR01273 |
arginine decarboxylase, biosynthetic; Two alternative pathways can convert arginine to ... |
4-630 |
0e+00 |
|
arginine decarboxylase, biosynthetic; Two alternative pathways can convert arginine to putrescine. One is decarboxylation by this enzyme followed by removal of the urea moeity by agmatinase. In the other, the ureohydrolase (arginase) acts first, followed by ornithine decarboxylase. This pathway leads to spermidine biosynthesis, hence the gene symbol speA. A distinct biodegradative form is also pyridoxal phosphate-dependent but is not similar in sequence. [Central intermediary metabolism, Polyamine biosynthesis]
Pssm-ID: 273532 [Multi-domain] Cd Length: 624 Bit Score: 811.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 4 WRIEDSEELYNITGWGTSYFGINDKGHVVVTPRKD--GVEVDLKELVDELQLRDVAAPMLVRFPDILDNRIEKIANCFKQ 81
Cdd:TIGR01273 1 WSASESRKTYNIAGWGAGYFAVNKLGNVSVRPGGDdtLQRIDLLELVKQVEARGLQLPLLVRFPDILQHRIRSLNAAFKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 82 ASDEYGYKAQNFIIYPIKVNQMRPVVEEIISHGKKFNLGLEAGSKPELHAVIAVNTDSDSLIICNGYKDESYIELALLAQ 161
Cdd:TIGR01273 81 AIEEYQYAGHYQGVYPIKVNQHRRVVEDIVASGKGEPYGLEAGSKPELMAAMAYATKPGAPIVCNGYKDREYIELALIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 162 KMGKRIFLVVEKMNELRLIAKMAKQLNVRPNIGIRIKLASSGSGKWEDSGGDASKFGLTSSELLEALDFLEKKDMKDCLK 241
Cdd:TIGR01273 161 KLGHNVFIVIEKLSELDLVIDEAKKLGVKPKLGLRARLASKGSGKWASSGGEKSKFGLSATQVLEVVRLLEQNGLLDSLQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 242 LIHFHIGSQVTKIRRIKTALREASQFYVQLHVMGFNVEFVDIGGGLGVDYDGTRSaNSESSVNYSIQEYVNDSISTLVDA 321
Cdd:TIGR01273 241 LLHFHIGSQISNIDDIKKGVREAARFYCELRKLGVKITYVDVGGGLGVDYDGTSS-SSDCSVNYGLEEYANDIVQALREI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 322 SDKNGIPHPNIITESGRSLTAHHSVLIFEVLETATLPEmDEDFEVGENDHELVHELYEIWDNLNQSRMVEAWHDAQQIRE 401
Cdd:TIGR01273 320 CEEKGVPHPVIITESGRAITAHHAVLITNVLGVERHEY-DPDPKIAEDAPPLVRTLRELYGPIDRRSAIEILHDAQHLKE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 402 EALDLFSHGIVDLKTRAQIERLYWSVTREINQIASGLKHAPDEFRKLDKLLADKYFCNFSLFQSLPDSWAIDQIFPIMPI 481
Cdd:TIGR01273 399 EAHEGFKLGYLDLEERAWAEQLYLSICHKVHQLSAKNKDHRPILDELQERLADKYFVNFSVFQSLPDAWGIDQLFPIMPL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 482 QRLDEKPDRNATLQDITCDSDGKIANFISTRYVSHDLPVHSLKGKDAYYIGVFLVGAYQEILGDMHNLFGDTNAVHVTVD 561
Cdd:TIGR01273 479 ERLDEKPTRRAVLLDITCDSDGKIDQFIGGQGITSTLPLHELDPDEGYFLGFFLVGAYQEILGDMHNLFGDTSAVRVVFD 558
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 562 DKG-YSIDQVIDGETVAEVLDYVQYNPKKLVRTLEtwvtKSVKEGRISVEEGKEFLSNYRSGLYGYTYLE 630
Cdd:TIGR01273 559 GDGgYEVELIREGDTTEDMLRYVQYDPKELLTLYR----DKVANNKLDAEEKKQFLEELEAGLSGYPYLS 624
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
54-558 |
0e+00 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily includes plants and biosynthetic prokaryotic arginine decarboxylases (ADC, EC 4.1.1.19). ADC is involved in the biosynthesis of putrescine, which is the precursor of aliphatic polyamines in many organisms. It catalyzes the decarboxylation of L-arginine to agmatine, which is then hydrolyzed to putrescine by agmatinase. ADC is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC), which 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. Homodimer formation and the presence of both PLP and Mg2+ cofactors may be required for catalytic activity. Prokaryotic ADCs (biodegradative), which are fold type I PLP-dependent enzymes, are not included in this family.
Pssm-ID: 143503 [Multi-domain] Cd Length: 409 Bit Score: 656.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 54 RDVAAPMLVRFPDILDNRIEKIANCFKQASDEYGYKAQNFIIYPIKVNQMRPVVEEIISHGKKFNLGLEAGSKPELHAVI 133
Cdd:cd06830 1 RGYGLPLLLRFPDILRHRIERLNAAFAKAIEEYGYKGKYQGVYPIKVNQQREVVEEIVKAGKRYNIGLEAGSKPELLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 134 AVNTDSDSLIICNGYKDESYIELALLAQKMGKRIFLVVEKMNELRLIAKMAKQLNVRPNIGIRIKLASSGSGKWEDSGGD 213
Cdd:cd06830 81 ALLKTPDALIICNGYKDDEYIELALLARKLGHNVIIVIEKLSELDLILELAKKLGVKPLLGVRIKLASKGSGKWQESGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 214 ASKFGLTSSELLEALDFLEKKDMKDCLKLIHFHIGSQVTKIRRIKTALREASQFYVQLHVMGFNVEFVDIGGGLGVDYDG 293
Cdd:cd06830 161 RSKFGLTASEILEVVEKLKEAGMLDRLKLLHFHIGSQITDIRRIKSALREAARIYAELRKLGANLRYLDIGGGLGVDYDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 294 TRSaNSESSVNYSIQEYVNDSISTLVDASDKNGIPHPNIITESGRSLTAHHSVLIFEVLETatlpemdedfevgendhel 373
Cdd:cd06830 241 SRS-SSDSSFNYSLEEYANDIVKTVKEICDEAGVPHPTIVTESGRAIVAHHSVLIFEVLGV------------------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 374 vhelyeiwdnlnqsrmveawhdaqqireealdlfshgivdlktraqierlywsvtreinqiasglkhapdefrkldKLLA 453
Cdd:cd06830 301 ----------------------------------------------------------------------------KRLA 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 454 DKYFCNFSLFQSLPDSWAIDQIFPIMPIQRLDEKPDRNATLQDITCDSDGKIANFISTRYVSHDLPVHSLKGKDAYYIGV 533
Cdd:cd06830 305 DWYFCNFSLFQSLPDSWAIDQLFPIMPLHRLNEKPTRRAVLGDITCDSDGKIDSFIDPPDILPTLPLHPLRKDEPYYLGF 384
|
490 500
....*....|....*....|....*
gi 492422142 534 FLVGAYQEILGDMHNLFGDTNAVHV 558
Cdd:cd06830 385 FLVGAYQEILGDLHNLFGDTNAVHV 409
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
79-342 |
3.02e-43 |
|
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: 155.52 E-value: 3.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 79 FKQASDEYGykaQNFIIYPIKVNQMRPVVEEIISHGkkfnLGLEAGSKPELHAVIAVNTDSDSLIICNGYKDESYIELAL 158
Cdd:pfam02784 8 HRRWKKALP---RIKPFYAVKCNSDPAVLRLLAELG----TGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 159 LAQKMgkriFLVVEKMNELRLIAKMAKqlnvRPNIGIRIKL-ASSGSGKWEdsggdaSKFGLTsseLLEALDFLEKKDMK 237
Cdd:pfam02784 81 EVGVG----CVTVDNVDELEKLARLAP----EARVLLRIKPdDSAATCPLS------SKFGAD---LDEDVEALLEAAKL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 238 DCLKLI--HFHIGSQVTKIRRIKTALREASQFYVQLHVMGFNVEFVDIGGGLGVDYDGTRSANSessvnysiqeyVNDSI 315
Cdd:pfam02784 144 LNLQVVgvSFHVGSGCTDAEAFVLALEDARGVFDQGAELGFNLKILDLGGGFGVDYTEGEEPLD-----------FEEYA 212
|
250 260
....*....|....*....|....*....
gi 492422142 316 STLVDASDKN--GIPHPNIITESGRSLTA 342
Cdd:pfam02784 213 NVINEALEEYfpGDPGVTIIAEPGRYFVA 241
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SpeA |
COG1166 |
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism]; |
1-630 |
0e+00 |
|
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism];
Pssm-ID: 440780 [Multi-domain] Cd Length: 633 Bit Score: 1147.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 1 MRKWRIEDSEELYNITGWGTSYFGINDKGHVVVTPRKD-GVEVDLKELVDELQLRDVAAPMLVRFPDILDNRIEKIANCF 79
Cdd:COG1166 2 MMDWTIEDARELYNIDRWGEGYFDINEKGHVTVRPDGDpGPSIDLYELVEELRERGLSLPVLLRFPDILRDRVERLNEAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 80 KQASDEYGYKAQNFIIYPIKVNQMRPVVEEIISHGKKFNLGLEAGSKPELHAVIAVNTDSDSLIICNGYKDESYIELALL 159
Cdd:COG1166 82 AKAIAEYGYQGRYRGVYPIKVNQQRHVVEEIVRAGKPYNFGLEAGSKPELMAVLALLDDPGSLIICNGYKDREYIRLALL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 160 AQKMGKRIFLVVEKMNELRLIAKMAKQLNVRPNIGIRIKLASSGSGKWEDSGGDASKFGLTSSELLEALDFLEKKDMKDC 239
Cdd:COG1166 162 GRKLGHKVIIVIEKLSELELILEEAKELGVKPLIGVRVKLASKGSGKWQNSGGERSKFGLSASEILEVVERLKEAGMLDC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 240 LKLIHFHIGSQVTKIRRIKTALREASQFYVQLHVMGFNVEFVDIGGGLGVDYDGTRSaNSESSVNYSIQEYVNDSISTLV 319
Cdd:COG1166 242 LQLLHFHLGSQIPNIRDIKRAVREAARFYAELRKLGAPIEYLDVGGGLGVDYDGSRS-NSDSSMNYSLQEYANDVVYAIK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 320 DASDKNGIPHPNIITESGRSLTAHHSVLIFEVLETATLPEMDEDFEVGENDHELVHELYEIWDNLNQSRMVEAWHDAQQI 399
Cdd:COG1166 321 EVCDEAGVPHPTIISESGRALTAHHSVLIFNVLDVERAPPEPPPPAPPEDAHELLRNLWETYESLTPRNLQECYHDALQY 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 400 REEALDLFSHGIVDLKTRAQIERLYWSVTREINQIASGLKHAPDEFRKLDKLLADKYFCNFSLFQSLPDSWAIDQIFPIM 479
Cdd:COG1166 401 KEEARSLFNLGYLSLEERALAEQLYWAICRKIRELLDPLEYHPEELDELNEKLADKYFCNFSLFQSLPDSWAIDQLFPIM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 480 PIQRLDEKPDRNATLQDITCDSDGKIANFISTRYVSHDLPVHSLKGKDAYYIGVFLVGAYQEILGDMHNLFGDTNAVHVT 559
Cdd:COG1166 481 PIHRLDEEPTRRAVLADITCDSDGKIDQFIDGQGVKSTLPLHPLKPGEPYYLGVFLVGAYQEILGDLHNLFGDTNAVHVR 560
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492422142 560 VD-DKGYSIDQVIDGETVAEVLDYVQYNPKKLVRTLETWVTKSVKEGRISVEEGKEFLSNYRSGLYGYTYLE 630
Cdd:COG1166 561 LDeDGGYEIEHVVEGDTVAEVLSYVQYDPEDLLERYRRQAEQAVRAGRLTPEERQRLLEEYEAGLRGYTYLE 632
|
|
| PRK05354 |
PRK05354 |
biosynthetic arginine decarboxylase; |
1-630 |
0e+00 |
|
biosynthetic arginine decarboxylase;
Pssm-ID: 235427 [Multi-domain] Cd Length: 634 Bit Score: 1106.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 1 MRKWRIEDSEELYNITGWGTSYFGINDKGHVVVTPRKD-GVEVDLKELVDELQLRDVAAPMLVRFPDILDNRIEKIANCF 79
Cdd:PRK05354 6 MSDWSIEDSRELYNIDHWGAGYFDINDKGHVSVRPDGDpGASIDLAELVKELRERGLRLPLLLRFPDILQDRVRSLNAAF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 80 KQASDEYGYKAQNFIIYPIKVNQMRPVVEEIISHGKKFNLGLEAGSKPELHAVIAVNTDSDSLIICNGYKDESYIELALL 159
Cdd:PRK05354 86 KKAIEEYGYQGDYRGVYPIKVNQQRRVVEEIVASGKPYNLGLEAGSKPELMAVLALAGDPGALIVCNGYKDREYIRLALI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 160 AQKMGKRIFLVVEKMNELRLIAKMAKQLNVRPNIGIRIKLASSGSGKWEDSGGDASKFGLTSSELLEALDFLEKKDMKDC 239
Cdd:PRK05354 166 GRKLGHKVFIVIEKLSELELILEEAKELGVKPRLGVRARLASQGSGKWQSSGGEKSKFGLSATEVLEAVERLREAGLLDC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 240 LKLIHFHIGSQVTKIRRIKTALREASQFYVQLHVMGFNVEFVDIGGGLGVDYDGTRSaNSESSVNYSIQEYVNDSISTLV 319
Cdd:PRK05354 246 LQLLHFHLGSQIANIRDIKTAVREAARFYVELRKLGAPIQYLDVGGGLGVDYDGTRS-QSDSSVNYSLQEYANDVVYTLK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 320 DASDKNGIPHPNIITESGRSLTAHHSVLIFEVLETATLPEMdEDFEVGENDHELVHELYEIWDNLNQSRMVEAWHDAQQI 399
Cdd:PRK05354 325 EICEEHGVPHPTIISESGRALTAHHAVLVFNVLGVESQEYE-EPPAPAEDAPPLLQNLWETYQEISERNLQEIYHDAQQD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 400 REEALDLFSHGIVDLKTRAQIERLYWSVTREINQIASGLKHAPDEFRKLDKLLADKYFCNFSLFQSLPDSWAIDQIFPIM 479
Cdd:PRK05354 404 LEEALTLFALGYLSLQERAWAEQLYWAICRKIQKLLDPKNRHPPELDELQERLADKYYVNFSLFQSLPDAWAIDQLFPIM 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 480 PIQRLDEKPDRNATLQDITCDSDGKIANFISTRYVSHDLPVHSLKGKDAYYIGVFLVGAYQEILGDMHNLFGDTNAVHVT 559
Cdd:PRK05354 484 PLHRLDEEPTRRAVLADITCDSDGKIDQFIDGQGIKTTLPLHELDPGEPYYLGFFLVGAYQEILGDMHNLFGDTNAVHVR 563
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492422142 560 VDDKG-YSIDQVIDGETVAEVLDYVQYNPKKLVRTLEtwvTKSVKEGRISVEEGKEFLSNYRSGLYGYTYLE 630
Cdd:PRK05354 564 VDEDGgYEIEHVIEGDTVADVLEYVQYDPKELLERLR---EKAVKEGKLSPEERQQLLEELEAGLRGYTYLE 632
|
|
| speA |
TIGR01273 |
arginine decarboxylase, biosynthetic; Two alternative pathways can convert arginine to ... |
4-630 |
0e+00 |
|
arginine decarboxylase, biosynthetic; Two alternative pathways can convert arginine to putrescine. One is decarboxylation by this enzyme followed by removal of the urea moeity by agmatinase. In the other, the ureohydrolase (arginase) acts first, followed by ornithine decarboxylase. This pathway leads to spermidine biosynthesis, hence the gene symbol speA. A distinct biodegradative form is also pyridoxal phosphate-dependent but is not similar in sequence. [Central intermediary metabolism, Polyamine biosynthesis]
Pssm-ID: 273532 [Multi-domain] Cd Length: 624 Bit Score: 811.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 4 WRIEDSEELYNITGWGTSYFGINDKGHVVVTPRKD--GVEVDLKELVDELQLRDVAAPMLVRFPDILDNRIEKIANCFKQ 81
Cdd:TIGR01273 1 WSASESRKTYNIAGWGAGYFAVNKLGNVSVRPGGDdtLQRIDLLELVKQVEARGLQLPLLVRFPDILQHRIRSLNAAFKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 82 ASDEYGYKAQNFIIYPIKVNQMRPVVEEIISHGKKFNLGLEAGSKPELHAVIAVNTDSDSLIICNGYKDESYIELALLAQ 161
Cdd:TIGR01273 81 AIEEYQYAGHYQGVYPIKVNQHRRVVEDIVASGKGEPYGLEAGSKPELMAAMAYATKPGAPIVCNGYKDREYIELALIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 162 KMGKRIFLVVEKMNELRLIAKMAKQLNVRPNIGIRIKLASSGSGKWEDSGGDASKFGLTSSELLEALDFLEKKDMKDCLK 241
Cdd:TIGR01273 161 KLGHNVFIVIEKLSELDLVIDEAKKLGVKPKLGLRARLASKGSGKWASSGGEKSKFGLSATQVLEVVRLLEQNGLLDSLQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 242 LIHFHIGSQVTKIRRIKTALREASQFYVQLHVMGFNVEFVDIGGGLGVDYDGTRSaNSESSVNYSIQEYVNDSISTLVDA 321
Cdd:TIGR01273 241 LLHFHIGSQISNIDDIKKGVREAARFYCELRKLGVKITYVDVGGGLGVDYDGTSS-SSDCSVNYGLEEYANDIVQALREI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 322 SDKNGIPHPNIITESGRSLTAHHSVLIFEVLETATLPEmDEDFEVGENDHELVHELYEIWDNLNQSRMVEAWHDAQQIRE 401
Cdd:TIGR01273 320 CEEKGVPHPVIITESGRAITAHHAVLITNVLGVERHEY-DPDPKIAEDAPPLVRTLRELYGPIDRRSAIEILHDAQHLKE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 402 EALDLFSHGIVDLKTRAQIERLYWSVTREINQIASGLKHAPDEFRKLDKLLADKYFCNFSLFQSLPDSWAIDQIFPIMPI 481
Cdd:TIGR01273 399 EAHEGFKLGYLDLEERAWAEQLYLSICHKVHQLSAKNKDHRPILDELQERLADKYFVNFSVFQSLPDAWGIDQLFPIMPL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 482 QRLDEKPDRNATLQDITCDSDGKIANFISTRYVSHDLPVHSLKGKDAYYIGVFLVGAYQEILGDMHNLFGDTNAVHVTVD 561
Cdd:TIGR01273 479 ERLDEKPTRRAVLLDITCDSDGKIDQFIGGQGITSTLPLHELDPDEGYFLGFFLVGAYQEILGDMHNLFGDTSAVRVVFD 558
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 562 DKG-YSIDQVIDGETVAEVLDYVQYNPKKLVRTLEtwvtKSVKEGRISVEEGKEFLSNYRSGLYGYTYLE 630
Cdd:TIGR01273 559 GDGgYEVELIREGDTTEDMLRYVQYDPKELLTLYR----DKVANNKLDAEEKKQFLEELEAGLSGYPYLS 624
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
54-558 |
0e+00 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily includes plants and biosynthetic prokaryotic arginine decarboxylases (ADC, EC 4.1.1.19). ADC is involved in the biosynthesis of putrescine, which is the precursor of aliphatic polyamines in many organisms. It catalyzes the decarboxylation of L-arginine to agmatine, which is then hydrolyzed to putrescine by agmatinase. ADC is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC), which 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. Homodimer formation and the presence of both PLP and Mg2+ cofactors may be required for catalytic activity. Prokaryotic ADCs (biodegradative), which are fold type I PLP-dependent enzymes, are not included in this family.
Pssm-ID: 143503 [Multi-domain] Cd Length: 409 Bit Score: 656.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 54 RDVAAPMLVRFPDILDNRIEKIANCFKQASDEYGYKAQNFIIYPIKVNQMRPVVEEIISHGKKFNLGLEAGSKPELHAVI 133
Cdd:cd06830 1 RGYGLPLLLRFPDILRHRIERLNAAFAKAIEEYGYKGKYQGVYPIKVNQQREVVEEIVKAGKRYNIGLEAGSKPELLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 134 AVNTDSDSLIICNGYKDESYIELALLAQKMGKRIFLVVEKMNELRLIAKMAKQLNVRPNIGIRIKLASSGSGKWEDSGGD 213
Cdd:cd06830 81 ALLKTPDALIICNGYKDDEYIELALLARKLGHNVIIVIEKLSELDLILELAKKLGVKPLLGVRIKLASKGSGKWQESGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 214 ASKFGLTSSELLEALDFLEKKDMKDCLKLIHFHIGSQVTKIRRIKTALREASQFYVQLHVMGFNVEFVDIGGGLGVDYDG 293
Cdd:cd06830 161 RSKFGLTASEILEVVEKLKEAGMLDRLKLLHFHIGSQITDIRRIKSALREAARIYAELRKLGANLRYLDIGGGLGVDYDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 294 TRSaNSESSVNYSIQEYVNDSISTLVDASDKNGIPHPNIITESGRSLTAHHSVLIFEVLETatlpemdedfevgendhel 373
Cdd:cd06830 241 SRS-SSDSSFNYSLEEYANDIVKTVKEICDEAGVPHPTIVTESGRAIVAHHSVLIFEVLGV------------------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 374 vhelyeiwdnlnqsrmveawhdaqqireealdlfshgivdlktraqierlywsvtreinqiasglkhapdefrkldKLLA 453
Cdd:cd06830 301 ----------------------------------------------------------------------------KRLA 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 454 DKYFCNFSLFQSLPDSWAIDQIFPIMPIQRLDEKPDRNATLQDITCDSDGKIANFISTRYVSHDLPVHSLKGKDAYYIGV 533
Cdd:cd06830 305 DWYFCNFSLFQSLPDSWAIDQLFPIMPLHRLNEKPTRRAVLGDITCDSDGKIDSFIDPPDILPTLPLHPLRKDEPYYLGF 384
|
490 500
....*....|....*....|....*
gi 492422142 534 FLVGAYQEILGDMHNLFGDTNAVHV 558
Cdd:cd06830 385 FLVGAYQEILGDLHNLFGDTNAVHV 409
|
|
| PLN02439 |
PLN02439 |
arginine decarboxylase |
60-629 |
0e+00 |
|
arginine decarboxylase
Pssm-ID: 215240 [Multi-domain] Cd Length: 559 Bit Score: 556.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 60 MLVRFPDILDNRIEKIANCFKQASDEYGYKAQNFIIYPIKVNQMRPVVEEIISHGKKFNLGLEAGSKPELHAVIA--VNT 137
Cdd:PLN02439 1 LIVRFPDVLKNRLESLQSAFDYAIQSQGYNSHYQGVFPVKCNQDRFLVEDIVKFGSPFRFGLEAGSKPELLLAMSclCKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 138 DSDSLIICNGYKDESYIELALLAQKMGKRIFLVVEKMNELRLIAKMAKQLNVRPNIGIRIKLASSGSGKWEDSGGDASKF 217
Cdd:PLN02439 81 SPDAFLICNGYKDAEYVSLALLARKLGLNTVIVLEQEEELDLVIEASQRLGVRPVIGVRAKLRTKHSGHFGSTSGEKGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 218 GLTSSELLEALDFLEKKDMKDCLKLIHFHIGSQVTKIRRIKTALREASQFYVQLHVMGFNVEFVDIGGGLGVDYDGTRSA 297
Cdd:PLN02439 161 GLTATEIVRVVRKLRKEGMLDCLQLLHFHIGSQIPSTSLLKDGVSEAAQIYCELVRLGAPMRVIDIGGGLGIDYDGSKSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 298 NSESSVNYSIQEYVNDSISTLVDASDKNGIPHPNIITESGRSLTAHHSVLIFEVLETATLPEMDEDFEVGENDHELVHEL 377
Cdd:PLN02439 241 SSDMSVAYSLEEYANAVVAAVRDVCDRKGVKHPVICSESGRALVSHHSVLIFEAVSASKRGVPAADDDDQYLLLGLTEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 378 YEIWDNLNQSRMV----EAWHDAQQIREEALDLFSHGIVDLKTRAQIERLYWSVTREINqiasglkhAPDEFRkldklla 453
Cdd:PLN02439 321 RADYENLYAAADRgdyeECLLYADQLKQECVRLFKEGLLSLEQRAAVDGLCELVSKRVG--------ASDPVA------- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 454 dKYFCNFSLFQSLPDSWAIDQIFPIMPIQRLDEKPDRNATLQDITCDSDGKIANFISTRyvsHDLPVHSLKGKDA--YYI 531
Cdd:PLN02439 386 -TYHINLSVFTSIPDFWAIGQLFPIVPLHRLDERPTVRGILSDLTCDSDGKIDKFIGGE---GSLPLHELEKNGGgpYYL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 532 GVFLVGAYQEILGDMHNLFGDTNAVHVTVDDK--GYSIDQVIDGETVAEVLDYVQYNPKKLVRTLETWVTKSVKEGRISv 609
Cdd:PLN02439 462 GMFLGGAYQEALGSLHNLFGGPSVVRVSQSDGpgGFAVTRAVPGQSCADVLRAMQHEPELMFETLKHRAEEYVHKGGLS- 540
|
570 580
....*....|....*....|
gi 492422142 610 eegKEFLSNYRSGLYGYTYL 629
Cdd:PLN02439 541 ---GAVAANLARSFHNMPYL 557
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
58-558 |
1.66e-55 |
|
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: 192.52 E-value: 1.66e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 58 APMLVRFPDILDNRIEKIANCFKQasdeyGYKaqnfIIYPIKVNQMRPVVEEIISHGkkfnLGLEAGSKPELHAVIAVNT 137
Cdd:cd06810 1 TPFYVYDLDIIRAHYAALKEALPS-----GVK----LFYAVKANPNPHVLRTLAEAG----TGFDVASKGELALALAAGV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 138 DSDsLIICNGY-KDESYIELALlaqKMGKRIFlVVEKMNELRLIAKMAKQLNVRPNIGIRIKLASSGSGKWEDSGGDASK 216
Cdd:cd06810 68 PPE-RIIFTGPaKSVSEIEAAL---ASGVDHI-VVDSLDELERLNELAKKLGPKARILLRVNPDVSAGTHKISTGGLKSK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 217 FGLTSSELLEALDFLEKKDMKdcLKLIHFHIGSQVTKIRRIKTALREASQFYVQLHVMGFNVEFVDIGGGLGVDYDGtrs 296
Cdd:cd06810 143 FGLSLSEARAALERAKELDLR--LVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPYDE--- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 297 ansessVNYSIQEYvNDSISTLVDASDKNGiPHPNIITESGRSLTAHHSVLIFEVLETatlpemdedfevgendhelvhe 376
Cdd:cd06810 218 ------QPLDFEEY-AALINPLLKKYFPND-PGVTLILEPGRYIVAQAGVLVTRVVAV---------------------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 377 lyeiwdnlnqsrmveawhdaqqireealdlfshgivdlktraqierlywsvtreinqiasglKHAPDEFrkldklladKY 456
Cdd:cd06810 268 --------------------------------------------------------------KVNGGRF---------FA 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 457 FCNFSLFQSLPDSWAIDQIFPIMPIQRL--DEKPDRnATLQDITCDSDGKIANFistryvSHDLPVHSlkgkdAYYIGVF 534
Cdd:cd06810 277 VVDGGMNHSFRPALAYDAYHPITPLKAPgpDEPLVP-ATLAGPLCDSGDVIGRD------RLLPELEV-----GDLLVFE 344
|
490 500
....*....|....*....|....
gi 492422142 535 LVGAYQEILGDMHNLFGDTNAVHV 558
Cdd:cd06810 345 DMGAYGFSESSNFNSHPRPAEYLV 368
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
79-342 |
3.02e-43 |
|
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: 155.52 E-value: 3.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 79 FKQASDEYGykaQNFIIYPIKVNQMRPVVEEIISHGkkfnLGLEAGSKPELHAVIAVNTDSDSLIICNGYKDESYIELAL 158
Cdd:pfam02784 8 HRRWKKALP---RIKPFYAVKCNSDPAVLRLLAELG----TGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 159 LAQKMgkriFLVVEKMNELRLIAKMAKqlnvRPNIGIRIKL-ASSGSGKWEdsggdaSKFGLTsseLLEALDFLEKKDMK 237
Cdd:pfam02784 81 EVGVG----CVTVDNVDELEKLARLAP----EARVLLRIKPdDSAATCPLS------SKFGAD---LDEDVEALLEAAKL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 238 DCLKLI--HFHIGSQVTKIRRIKTALREASQFYVQLHVMGFNVEFVDIGGGLGVDYDGTRSANSessvnysiqeyVNDSI 315
Cdd:pfam02784 144 LNLQVVgvSFHVGSGCTDAEAFVLALEDARGVFDQGAELGFNLKILDLGGGFGVDYTEGEEPLD-----------FEEYA 212
|
250 260
....*....|....*....|....*....
gi 492422142 316 STLVDASDKN--GIPHPNIITESGRSLTA 342
Cdd:pfam02784 213 NVINEALEEYfpGDPGVTIIAEPGRYFVA 241
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
94-352 |
2.29e-34 |
|
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: 133.38 E-value: 2.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 94 IIYPIKVNQMRPVVEEIISHGkkfnLGLEAGSKPELHAVIAVNTDSDSLIICNGYKDESYIELALlaqKMGKRIFlVVEK 173
Cdd:pfam00278 26 IFYAVKANPNPAVLRLLAELG----AGFDVASGGELERALAAGVDPERIVFAGPGKTDSEIRYAL---EAGVLCF-NVDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 174 MNELRLIAKMAKQLNVRpnIGIRIKLASSGSGKWEDSGGDASKFGLTSSELLEALDFLEKKDMKdcLKLIHFHIGSQVTK 253
Cdd:pfam00278 98 EDELEKIAKLAPELVAR--VALRINPDVDAGTHKISTGGLSSKFGIDLEDAPELLALAKELGLN--VVGVHFHIGSQITD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 254 IRRIKTALREASQFYVQLHVMGFNVEFVDIGGGLGVDYDGTRSansessvnYSIQEYVndsiSTLVDASDKNGIPHPNII 333
Cdd:pfam00278 174 LEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPYRDEPP--------PDFEEYA----AAIREALDEYFPPDLEII 241
|
250
....*....|....*....
gi 492422142 334 TESGRSLTAHHSVLIFEVL 352
Cdd:pfam00278 242 AEPGRYLVANAGVLVTRVI 260
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
42-352 |
1.70e-32 |
|
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: 129.88 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 42 VDLKELVDElqlrdVAAPMLVRFPDILDNRIEKIANCFKQASDEygykaqnfIIYPIKVNQMRPVVEEIISHGkkfnLGL 121
Cdd:COG0019 15 VDLAELAEE-----YGTPLYVYDEAALRRNLRALREAFPGSGAK--------VLYAVKANSNLAVLRLLAEEG----LGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 122 EAGSKPELHAVIAVNTDSDSLII-CNGYKDESyIELALlaqKMGKRIFlVVEKMNELRLIAKMAKQLNVRPNIGIRIK-L 199
Cdd:COG0019 78 DVVSGGELRLALAAGFPPERIVFsGNGKSEEE-LEEAL---ELGVGHI-NVDSLSELERLAELAAELGKRAPVGLRVNpG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 200 ASSGSGKWEDSGGDASKFGLTSSELLEALDFLeKKDMKDCLKLIHFHIGSQVTKIRRIKTALREASQFYVQLHVMGFNVE 279
Cdd:COG0019 153 VDAGTHEYISTGGKDSKFGIPLEDALEAYRRA-AALPGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLE 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492422142 280 FVDIGGGLGVDYDgtrsansESSVNYSIQEYvndsISTLVDASDKNGIPHPNIITESGRSLTAHHSVLIFEVL 352
Cdd:COG0019 232 WLDLGGGLGIPYT-------EGDEPPDLEEL----AAAIKEALEELCGLGPELILEPGRALVGNAGVLLTRVL 293
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
70-352 |
2.65e-27 |
|
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: 113.73 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 70 NRIEKIANCFKQASDEYGYKaqnfIIYPIKVNQMRPVVEEIISHGkkfnLGLEAGSKPELHAVIAVNTDSDSLII-CNGy 148
Cdd:cd06828 11 ATIRENYRRLKEAFSGPGFK----ICYAVKANSNLAILKLLAEEG----LGADVVSGGELYRALKAGFPPERIVFtGNG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 149 KDESYIELALlaqKMGKRIFlVVEKMNELRLIAKMAKQLNVRPNIGIRIKLA-SSGSGKWEDSGGDASKFGLTSSELLEA 227
Cdd:cd06828 82 KSDEELELAL---ELGILRI-NVDSLSELERLGEIAPELGKGAPVALRVNPGvDAGTHPYISTGGKDSKFGIPLEQALEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 228 LDFLEKKDmkdCLKL--IHFHIGSQVTKIRRIKTALREASQFYVQLHVMGFNVEFVDIGGGLGVDYDgtrsansESSVNY 305
Cdd:cd06828 158 YRRAKELP---GLKLvgLHCHIGSQILDLEPFVEAAEKLLDLAAELRELGIDLEFLDLGGGLGIPYR-------DEDEPL 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 492422142 306 SIQEYVnDSISTLVDASdKNGIPHPNIITESGRSLTAHHSVLIFEVL 352
Cdd:cd06828 228 DIEEYA-EAIAEALKEL-CEGGPDLKLIIEPGRYIVANAGVLLTRVG 272
|
|
| Arg_decarb_HB |
pfam17810 |
Arginine decarboxylase helical bundle domain; This entry represents a helical bundle domain ... |
368-451 |
1.20e-26 |
|
Arginine decarboxylase helical bundle domain; This entry represents a helical bundle domain that is found between the two enzymatic domains of the arginine decarboxylases.
Pssm-ID: 436060 [Multi-domain] Cd Length: 84 Bit Score: 103.42 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 368 ENDHELVHELYEIWDNLNQSRMVEAWHDAQQIREEALDLFSHGIVDLKTRAQIERLYWSVTREINQIASGLKHAPDEFrk 447
Cdd:pfam17810 2 EDAPLLLQNLWELLENLSQRNLLESYHDALHYLDEAHTLFNHGYLSLEQRALAEQLYWAICRRIRALLDPLKRVHREI-- 79
|
....
gi 492422142 448 LDKL 451
Cdd:pfam17810 80 LDEL 83
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
23-352 |
7.39e-26 |
|
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an enzyme which catalyzes the conversion of diaminopimelic acid into lysine during the last step of lysine biosynthesis. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273415 [Multi-domain] Cd Length: 414 Bit Score: 110.46 E-value: 7.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 23 FGINDKGHVVVTprkdgvEVDLKELVDELqlrdvAAPMLVRFPDILDNRIEKiancFKQAsdeygYKAQNFIIYPIKVNQ 102
Cdd:TIGR01048 1 TVENEDGELFIE------GVPLLELAQEF-----GTPLYVYDEDTIRRRFRA----YKEA-----FGGRSLVCYAVKANS 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 103 MRPVVEEIISHGkkfnLGLEAGSKPELHAVIAVNTDSDSlIICNGY-KDESYIELALLAqkmgkRIFLVVEKMNELRLIA 181
Cdd:TIGR01048 61 NLAVLRLLAELG----SGFDVVSGGELYRALAAGFPPEK-IVFSGNgKSRAELERALEL-----GICINVDSFSELERLN 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 182 KMAKQLNVRPNIGIRIK-LASSGSGKWEDSGGDASKFGLTSSELLEALDFLEKKDMKDCLKlIHFHIGSQVTKIRRIKTA 260
Cdd:TIGR01048 131 EIAPELGKKARISLRVNpGVDAKTHPYISTGLKDSKFGIDVEEALEAYLYALQLPHLELVG-IHCHIGSQITDLSPFVEA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 261 LREASQFYVQLHvMGFNVEFVDIGGGLGVDYDGTRSAnsessvnYSIQEYVNDSISTLVDASDKNgiPHPNIITESGRSL 340
Cdd:TIGR01048 210 AEKVVKLAESLA-EGIDLEFLDLGGGLGIPYTPEEEP-------PDLSEYAQAILNALEGYADLG--LDPKLILEPGRSI 279
|
330
....*....|..
gi 492422142 341 TAHHSVLIFEVL 352
Cdd:TIGR01048 280 VANAGVLLTRVG 291
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
94-371 |
6.30e-25 |
|
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: 106.91 E-value: 6.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 94 IIYPIKVNQMRPVVEEIISHGkkfnLGLEAGSKPELHAVIAVNTDSDSLIICNGYKDESYIELALLAQKmgkrIFLVVEK 173
Cdd:cd06839 34 IYYSLKANPNPALVAHLRQLG----DGAEVASAGELALALEAGVPPEKILFAGPGKSDAELRRAIEAGI----GTINVES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 174 MNELRLIAKMAKQLNVRPNIGIRIK--LASSGSGKweDSGGDASKFGLTSSELLEALDFLEKKDMkdcLKLIHFHI--GS 249
Cdd:cd06839 106 LEELERIDALAEEHGVVARVALRINpdFELKGSGM--KMGGGPSQFGIDVEELPAVLARIAALPN---LRFVGLHIypGT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 250 QVTKIRRIKTALREASQFYVQL-HVMGFNVEFVDIGGGLGVDYDGTrsansESSVNYsiqEYVNDSISTLVDASDKNgIP 328
Cdd:cd06839 181 QILDADALIEAFRQTLALALRLaEELGLPLEFLDLGGGFGIPYFPG-----ETPLDL---EALGAALAALLAELGDR-LP 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 492422142 329 HPNIITESGRSLTAHHSVLIFEVLETATLpeMDEDFEV---GENDH 371
Cdd:cd06839 252 GTRVVLELGRYLVGEAGVYVTRVLDRKVS--RGETFLVtdgGMHHH 295
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
67-354 |
4.13e-24 |
|
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: 104.65 E-value: 4.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 67 ILD-NRIEKIANCFKQASDEYGYKAQnfIIYPIKVNQMrPVVEEIIsHGKkfNLGLEAGSKPELHAVIAVNTDSDSlIIC 145
Cdd:cd06841 11 VFDeDALRENYRELLGAFKKRYPNVV--IAYSYKTNYL-PAICKIL-HEE--GGYAEVVSAMEYELALKLGVPGKR-IIF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 146 NG-YKDESYIELALLAQKMgkrifLVVEKMNELRLIAKMAKQLNVRPNIGIRIKLaSSGSGKWedsggdaSKFGLTSSEL 224
Cdd:cd06841 84 NGpYKSKEELEKALEEGAL-----INIDSFDELERILEIAKELGRVAKVGIRLNM-NYGNNVW-------SRFGFDIEEN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 225 LEALDFLEKKDMKDCLKL--IHFHIGSQVTKIRRIKTALREASQFYVQLHvmGFNVEFVDIGGGLGVDYDgTRSANSESS 302
Cdd:cd06841 151 GEALAALKKIQESKNLSLvgLHCHVGSNILNPEAYSAAAKKLIELLDRLF--GLELEYLDLGGGFPAKTP-LSLAYPQED 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 492422142 303 VNYSIQEYVNDSISTLVDaSDKNGIPHPNIITESGRSLTAHHSVLIFEVLET 354
Cdd:cd06841 228 TVPDPEDYAEAIASTLKE-YYANKENKPKLILEPGRALVDDAGYLLGRVVAV 278
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
96-352 |
9.99e-18 |
|
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: 85.24 E-value: 9.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 96 YPIKVNQMRPVVEEIISHGkkfnLGLEAGSKPELHAVIAVNTDSDSLIICNGYKDESYIELAllaQKMGKRIFlVVEKMN 175
Cdd:cd00622 30 YAVKCNPDPAVLRTLAALG----AGFDCASKGEIELVLGLGVSPERIIFANPCKSISDIRYA---AELGVRLF-TFDSED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 176 ELRLIAKMAkqlnvrPNIGIRIKLASSGSGKWEDSGGdasKFGltsSELLEALDFLEK-KDMKDCLKLIHFHIGSQVTKI 254
Cdd:cd00622 102 ELEKIAKHA------PGAKLLLRIATDDSGALCPLSR---KFG---ADPEEARELLRRaKELGLNVVGVSFHVGSQCTDP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 255 RRIKTALREASQFYVQLHVMGFNVEFVDIGGGLGVDYDGtrsansessVNYSIQEY---VNDSISTLVdasdknGIPHPN 331
Cdd:cd00622 170 SAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDG---------VVPSFEEIaavINRALDEYF------PDEGVR 234
|
250 260
....*....|....*....|.
gi 492422142 332 IITESGRSLTAHHSVLIFEVL 352
Cdd:cd00622 235 IIAEPGRYLVASAFTLAVNVI 255
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
44-291 |
3.54e-17 |
|
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: 84.23 E-value: 3.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 44 LKELVDELqlrdvAAPMLVRFPDILDNRIEKIANCFkqasDEYGYKAQnfIIYPIKVNQMRPVVEEIISHGkkfnLGLEA 123
Cdd:cd06842 1 LVALVEAY-----GSPLNVLFPQTFRENIAALRAVL----DRHGVDGR--VYFARKANKSLALVRAAAAAG----IGVDV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 124 GSKPELHAVIAVNTDSDSLIICNGYKDESYIELALLaqkmgKRIFLVVEKMNELRLIAKMAKQLNVRPnigIRIKLASSG 203
Cdd:cd06842 66 ASLAELRQALAAGVRGDRIVATGPAKTDEFLWLAVR-----HGATIAVDSLDELDRLLALARGYTTGP---ARVLLRLSP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 204 sgkweDSGGDASKFGLTSSELLEALDFLEKKDMKDCLKLIHFHIG--SQVTKIRriktALREASQFYVQLHVMGFNVEFV 281
Cdd:cd06842 138 -----FPASLPSRFGMPAAEVRTALERLAQLRERVRLVGFHFHLDgySAAQRVA----ALQECLPLIDRARALGLAPRFI 208
|
250
....*....|
gi 492422142 282 DIGGGLGVDY 291
Cdd:cd06842 209 DIGGGFPVSY 218
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
94-295 |
2.37e-14 |
|
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: 72.35 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 94 IIYPIKVNQMRPVVEEIISHGkkfnLGLEAGSKPELHAVIAVNTDSDSLIICNGYKDESYIELALLAQkmgkRIFLVVEK 173
Cdd:cd06808 18 LFAVVKANANPEVARTLAALG----TGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAAEQG----VIVVTVDS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 174 MNELRLIAKMAKQLNVRPNIGIRIklassgsgkweDSGGDASKFGLTSSELLEALDFLEKKDMkdcLKL--IHFHIGSQV 251
Cdd:cd06808 90 LEELEKLEEAALKAGPPARVLLRI-----------DTGDENGKFGVRPEELKALLERAKELPH---LRLvgLHTHFGSAD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492422142 252 TKIRRIKTALREASQFYVQLHVMGFNVEFVDIGGGLGVDYDGTR 295
Cdd:cd06808 156 EDYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILYLQEL 199
|
|
| Arg_decarbox_C |
pfam17944 |
Arginine decarboxylase C-terminal helical extension; This small three helical domain is found ... |
576-629 |
5.11e-13 |
|
Arginine decarboxylase C-terminal helical extension; This small three helical domain is found at the C-terminus of the arginine decarboxylase enzyme.
Pssm-ID: 436163 [Multi-domain] Cd Length: 50 Bit Score: 63.71 E-value: 5.11e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 492422142 576 VAEVLDYVQYNPKKLVRTLEtwvtKSVKEGRISVEEGKEFLSNYRSGLYGYTYL 629
Cdd:pfam17944 1 VADVLRYVQYDPEELLERYR----RQVEAARLSAEERRALLEELEAGLKGYTYL 50
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
98-351 |
1.04e-11 |
|
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: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 98 IKVNQMRPVVEEIISHGkkfnLGLEAGSKPELHAVIAVNTDSDSLIICNGYKDESYIELALlaqKMGkrIFLVVEKMNEL 177
Cdd:cd06836 34 VKANPLVPVLRLLAEAG----AGAEVASPGELELALAAGFPPERIVFDSPAKTRAELREAL---ELG--VAINIDNFQEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 178 -RLIAKMAKQLNVRPNIGIRIKlASSGSGKWED-SGGDA-SKFGL-----TSSELLEAldFLEKKdmkdCLKLIHFHIGS 249
Cdd:cd06836 105 eRIDALVAEFKEASSRIGLRVN-PQVGAGKIGAlSTATAtSKFGValedgARDEIIDA--FARRP----WLNGLHVHVGS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 250 Q-------VTKIRRIkTALREAsqfyVQLHVMGFNVEFVDIGGGLGVDYDGTrsansesSVNYSIQEYVN---DSISTLV 319
Cdd:cd06836 178 QgcelsllAEGIRRV-VDLAEE----INRRVGRRQITRIDIGGGLPVNFESE-------DITPTFADYAAalkAAVPELF 245
|
250 260 270
....*....|....*....|....*....|..
gi 492422142 320 DasDKNGiphpnIITESGRSLTAHHSVLIFEV 351
Cdd:cd06836 246 D--GRYQ-----LVTEFGRSLLAKCGTIVSRV 270
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
96-353 |
1.26e-11 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE from Vibrio parahaemolyticus and similar proteins. PvsE is a vibrioferrin biosynthesis protein which 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. It has been suggested that PvsE may be involved in the biosynthesis of the polycarboxylate siderophore vibrioferrin. It may catalyze the decarboxylation of serine to yield ethanolamine. PvsE may require homodimer formation and the presence of the PLP cofactor for activity.
Pssm-ID: 143510 [Multi-domain] Cd Length: 377 Bit Score: 66.54 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 96 YPIKVNQMRPVVEEIISHGKkfnlGLEAGSKPELHAVIAVNTDSdSLIICNGYKDESYIELALLaqkmGKRIFLVVEKMN 175
Cdd:cd06843 31 YAIKANSDPPILRALAPHVD----GFEVASGGEIAHVRAAVPDA-PLIFGGPGKTDSELAQALA----QGVERIHVESEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 176 ELRLIAKMAKQLNVRPNIGIRIKLAS-SGSGKWEDSGGDASKFGLTSSELLEALDFLekKDMkDCLKL--IHFHIGS--- 249
Cdd:cd06843 102 ELRRLNAVARRAGRTAPVLLRVNLALpDLPSSTLTMGGQPTPFGIDEADLPDALELL--RDL-PNIRLrgFHFHLMShnl 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 250 ----QVTKIRR-IKTALREASQFYVQLHVmgfnvefVDIGGGLGVDYdgtrsANSESSVNYSiqEYVnDSISTLVDASDk 324
Cdd:cd06843 179 daaaHLALVKAyLETARQWAAEHGLDLDV-------VNVGGGIGVNY-----ADPEEQFDWA--GFC-EGLDQLLAEYE- 242
|
250 260
....*....|....*....|....*....
gi 492422142 325 ngiPHPNIITESGRSLTAHHSVLIFEVLE 353
Cdd:cd06843 243 ---PGLTLRFECGRYISAYCGYYVTEVLD 268
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
92-351 |
1.29e-10 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 63.66 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 92 NFIIYPIKVNQMRPVVEE--------IISHGKKFNLGLEAGSKPelhaviavntdsdSLIICNGyKDESYIELALLAQKm 163
Cdd:PLN02537 44 SIIGYAIKANNNLKILEHlrelgcgaVLVSGNELRLALRAGFDP-------------TRCIFNG-NGKLLEDLVLAAQE- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 164 gkRIFLVVEKMNELRLIAKMAKQLNVRPNIGIRIKL-ASSGSGKWEDSGGDASKFGLTSSELLEALDflEKKDMKDCLKL 242
Cdd:PLN02537 109 --GVFVNVDSEFDLENIVEAARIAGKKVNVLLRINPdVDPQVHPYVATGNKNSKFGIRNEKLQWFLD--AVKAHPNELKL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 243 I--HFHIGSQVTKIRRIKTALREASQFYVQLHVMGFNVEFVDIGGGLGVDYDGTRsansessvnySIQEYVNDSISTLVD 320
Cdd:PLN02537 185 VgaHCHLGSTITKVDIFRDAAVLMVNYVDEIRAQGFELSYLNIGGGLGIDYYHAG----------AVLPTPRDLIDTVRE 254
|
250 260 270
....*....|....*....|....*....|.
gi 492422142 321 ASDKNGIphpNIITESGRSLTAHHSVLIFEV 351
Cdd:PLN02537 255 LVLSRDL---TLIIEPGRSLIANTCCFVNRV 282
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
79-354 |
8.39e-05 |
|
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: 45.12 E-value: 8.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 79 FKQASDEY-GYKAQNFIIYPIKVNQMRPVVEEIISHGkkfnLGLEAGSKPELHAVIAV--NTDSDSLIICNGYKDESYIE 155
Cdd:cd06840 22 VRARARQVsALKAVDSLFYAIKANPHPDVLRTLEEAG----LGFECVSIGELDLVLKLfpDLDPRRVLFTPNFAARSEYE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 156 LALlaqKMGkrIFLVVEKMNELRLIAKMAK--QLNVRPNIGiriklASSGSGKWEDSGGDASKFGLTSSELLEALDFLEK 233
Cdd:cd06840 98 QAL---ELG--VNVTVDNLHPLREWPELFRgrEVILRIDPG-----QGEGHHKHVRTGGPESKFGLDVDELDEARDLAKK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 234 KDMKdcLKLIHFHIGSQVTKirriKTALREASQFYVQLHVMGFNVEFVDIGGGLGVDYD-GTRSANSESsvnysiqeyVN 312
Cdd:cd06840 168 AGII--VIGLHAHSGSGVED----TDHWARHGDYLASLARHFPAVRILNVGGGLGIPEApGGRPIDLDA---------LD 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 492422142 313 DSISTLvdasdKNGIPHPNIITESGRSLTAHHSVLIFEVLET 354
Cdd:cd06840 233 AALAAA-----KAAHPQYQLWMEPGRFIVAESGVLLARVTQI 269
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
192-291 |
1.66e-04 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 44.69 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492422142 192 NIGIRIKLASsGSGKWE--DSGGDASKFGLTSSELLEALDFLEKKDMKdcLKLIHFHIGSQVTKI---RRIKTALRE-AS 265
Cdd:PRK08961 616 EVWLRIDPGH-GDGHHEkvRTGGKESKFGLSQTRIDEFVDLAKTLGIT--VVGLHAHLGSGIETGehwRRMADELASfAR 692
|
90 100
....*....|....*....|....*.
gi 492422142 266 QFYvqlhvmgfNVEFVDIGGGLGVDY 291
Cdd:PRK08961 693 RFP--------DVRTIDLGGGLGIPE 710
|
|
| |
