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Conserved domains on  [gi|303280756|ref|XP_003059670|]
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uncharacterized protein MICPUCDRAFT_65271 [Micromonas pusilla CCMP1545]

Protein Classification

D-amino-acid transaminase( domain architecture ID 10010919)

chloroplastic D-amino-acid transaminase acts as an amino acid aminotransferase using D-Asp and D-Ala as amino donors with 2-oxoglutarate as an amino acceptor; also acts as a 4-amino-4-deoxychorismate lyase catalyzing the production of 4-aminobenzoate in the folate biosynthesis pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02845 PLN02845
Branched-chain-amino-acid aminotransferase-like protein
 70-435 3.65e-153

Branched-chain-amino-acid aminotransferase-like protein


:

Pssm-ID: 215454 [Multi-domain]  Cd Length: 336  Bit Score: 437.52  E-value: 3.65e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756  70 IPVLDAAGVHARLASRTHDAAKDTFAAFYSSWTGCITTDPAAIVLPFDDHMVHRGHGVFDTAHLENGALHLLDRHLARFK 149
Cdd:PLN02845  13 PPLLSAAEMIQRLQSKWSDAKKQNFGAMYSSVVGGITTDPAAMVIPLDDHMVHRGHGVFDTATIRDGHLYELDAHLDRFL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 150 RSMAAARVPPPFGdgdgdgddcAEKMKAIILRVAAASGVRdHGQVRYYASAGPGGFALSREECVRSVFYVVVVRKKRRAG 229
Cdd:PLN02845  93 RSAAKAKIPLPFD---------RATLRRILLQTVAASGCR-NGSLRYWLSAGPGGFSLSPSGCSEPAFYAVVIEDTYAQD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 230 AgekPKRLRVVTTPIPMKPGVFATTKTTNYLPNALVVADAIDKRADVGLWVTENGFVGEGPSMNVAFLVPADdagggggg 309
Cdd:PLN02845 163 R---PEGVKVVTSSVPIKPPQFATVKSVNYLPNALSQMEAEERGAFAGIWLDEEGFVAEGPNMNVAFLTNDG-------- 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 310 deedetvcgeafktnkkwKLVSPPTSNILAGCTVARVAELVNdaKVLEHLNVAAFEFRDVGVEEGKRARETMLIGSVIHV 389
Cdd:PLN02845 232 ------------------ELVLPPFDKILSGCTARRVLELAP--RLVSPGDLRGVKQRKISVEEAKAADEMMLIGSGVPV 291

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 303280756 390 APVVEWDGEAVGDETTteTPIADALHAAVVRDIATNVPEL-TPVPYE 435
Cdd:PLN02845 292 LPIVSWDGQPIGDGKV--GPITLALHDLLLDDMRSGPPGVrTPVPYG 336
 
Name Accession Description Interval E-value
PLN02845 PLN02845
Branched-chain-amino-acid aminotransferase-like protein
 70-435 3.65e-153

Branched-chain-amino-acid aminotransferase-like protein


Pssm-ID: 215454 [Multi-domain]  Cd Length: 336  Bit Score: 437.52  E-value: 3.65e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756  70 IPVLDAAGVHARLASRTHDAAKDTFAAFYSSWTGCITTDPAAIVLPFDDHMVHRGHGVFDTAHLENGALHLLDRHLARFK 149
Cdd:PLN02845  13 PPLLSAAEMIQRLQSKWSDAKKQNFGAMYSSVVGGITTDPAAMVIPLDDHMVHRGHGVFDTATIRDGHLYELDAHLDRFL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 150 RSMAAARVPPPFGdgdgdgddcAEKMKAIILRVAAASGVRdHGQVRYYASAGPGGFALSREECVRSVFYVVVVRKKRRAG 229
Cdd:PLN02845  93 RSAAKAKIPLPFD---------RATLRRILLQTVAASGCR-NGSLRYWLSAGPGGFSLSPSGCSEPAFYAVVIEDTYAQD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 230 AgekPKRLRVVTTPIPMKPGVFATTKTTNYLPNALVVADAIDKRADVGLWVTENGFVGEGPSMNVAFLVPADdagggggg 309
Cdd:PLN02845 163 R---PEGVKVVTSSVPIKPPQFATVKSVNYLPNALSQMEAEERGAFAGIWLDEEGFVAEGPNMNVAFLTNDG-------- 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 310 deedetvcgeafktnkkwKLVSPPTSNILAGCTVARVAELVNdaKVLEHLNVAAFEFRDVGVEEGKRARETMLIGSVIHV 389
Cdd:PLN02845 232 ------------------ELVLPPFDKILSGCTARRVLELAP--RLVSPGDLRGVKQRKISVEEAKAADEMMLIGSGVPV 291

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 303280756 390 APVVEWDGEAVGDETTteTPIADALHAAVVRDIATNVPEL-TPVPYE 435
Cdd:PLN02845 292 LPIVSWDGQPIGDGKV--GPITLALHDLLLDDMRSGPPGVrTPVPYG 336
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
 107-417 1.38e-34

Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439885 [Multi-domain]  Cd Length: 285  Bit Score: 129.92  E-value: 1.38e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 107 TDPAAIVLPFDDHMVHRGHGVFDTAHLENGALHLLDRHLARFKRSMAAARVPPPFGdgdgdgddcAEKMKAIILRVAAAS 186
Cdd:COG0115   10 VPEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYT---------EEELLEAIRELVAAN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 187 GVRDhGQVRYYASAGPGGFALSREECVRSVFYVVVVRKKRRAGAGEKPKRLRVVTTPIPMkPGVFATTKTTNYLPNALVV 266
Cdd:COG0115   81 GLED-GYIRPQVTRGVGGRGVFAEEYEPTVIIIASPLPAYPAEAYEKGVRVITSPYRRAA-PGGLGGIKTGNYLNNVLAK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 267 ADAIDKRADVGLWVTENGFVGEGPSMNVaFLVpaddaggggggdeedetvcgeafktnKKWKLVSPPTSN-ILAGCTVAR 345
Cdd:COG0115  159 QEAKEAGADEALLLDTDGYVAEGSGSNV-FIV--------------------------KDGVLVTPPLSGgILPGITRDS 211

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 303280756 346 VAELvndakvLEHLNVAAFEfRDVGVEEGKRARETMLIGSVIHVAPVVEWDGEAVGDetTTETPIADALHAA 417
Cdd:COG0115  212 VIEL------ARELGIPVEE-RPISLEELYTADEVFLTGTAAEVTPVTEIDGRPIGD--GKPGPVTRRLREL 274
ADCL_like cd01559
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ...
 118-397 1.73e-34

ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent enzymes that converts 4-amino-4-deoxychorismate (ADC) to p-aminobenzoate and pyruvate. Based on the information available from the crystal structure, most members of this subgroup are likely to function as dimers. The enzyme from E.Coli, the structure of which is available, is a homodimer that is folded into a small and a larger domain. The coenzyme pyridoxal 5; -phosphate resides at the interface of the two domains that is linked by a flexible loop. Members of this subgroup are found in Eukaryotes and bacteria.


Pssm-ID: 238800 [Multi-domain]  Cd Length: 249  Bit Score: 128.97  E-value: 1.73e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 118 DHMVHRGHGVFDTAHLENGALHLLDRHLARFKRSMAAARVPPPFGdgdgdgddcaEKMKAIILRVAAASGVRDHGqVRYY 197
Cdd:cd01559    1 DRGFAYGDGVFETMRALDGRLFLLDAHLARLERSARRLGIPEPDL----------PRLRAALESLLAANDIDEGR-IRLI 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 198 ASAGPGGFALSREECVRSVFYVVVVRKKRRAGagekPKRLRVVTTPIPM-KPGVFATTKTTNYLPNALVVADAIDKRADV 276
Cdd:cd01559   70 LSRGPGGRGYAPSVCPGPALYVSVIPLPPAWR----QDGVRLITCPVRLgEQPLLAGLKHLNYLENVLAKREARDRGADE 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 277 GLWVTENGFVGEGPSMNVAFLvpaddaggggggdeedetvcgeafktnKKWKLVSPP-TSNILAGCTVARVAELVNDAKV 355
Cdd:cd01559  146 ALFLDTDGRVIEGTASNLFFV---------------------------KDGELVTPSlDRGGLAGITRQRVIELAAAKGY 198

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 303280756 356 lehlnvaAFEFRDVGVEEGKRARETMLIGSVIHVAPVVEWDG 397
Cdd:cd01559  199 -------AVDERPLRLEDLLAADEAFLTNSLLGVAPVTAIDD 233
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
 126-395 3.21e-22

Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to catalyze the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity.


Pssm-ID: 395844 [Multi-domain]  Cd Length: 221  Bit Score: 94.35  E-value: 3.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756  126 GVFDTAHLENGALHLLDRHLARFKRSMAAARVPPPFgdgdgdgddCAEKMKAIILRVAAASGVRDHGqVRYYASAGPGGF 205
Cdd:pfam01063   1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPF---------DEEDLRKIIEELLKANGLGVGR-LRLTVSRGPGGF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756  206 ALSREECVRSVFYVVVvrkkrRAGAGEKPKRLRVVTTPIPMKPgVFATTKTTNYLPNALVVADAIDKRADVGLWVTENGF 285
Cdd:pfam01063  71 GLPTSDPTLAIFVSAL-----PPPPESKKKGVISSLVRRNPPS-PLPGAKTLNYLENVLARREAKAQGADDALLLDEDGN 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756  286 VGEGPSMNVaFLVpaddaggggggdeedetvcgeafKTNkkwKLVSPP-TSNILAGCTVARVAELVNDAKVlehlnvaAF 364
Cdd:pfam01063 145 VTEGSTSNV-FLV-----------------------KGG---TLYTPPlESGILPGITRQALLDLAKALGL-------EV 190

                         250       260       270
                  ....*....|....*....|....*....|.
gi 303280756  365 EFRDVGVEEGKRARETMLIGSVIHVAPVVEW 395
Cdd:pfam01063 191 EERPITLADLQEADEAFLTNSLRGVTPVSSI 221
 
Name Accession Description Interval E-value
PLN02845 PLN02845
Branched-chain-amino-acid aminotransferase-like protein
 70-435 3.65e-153

Branched-chain-amino-acid aminotransferase-like protein


Pssm-ID: 215454 [Multi-domain]  Cd Length: 336  Bit Score: 437.52  E-value: 3.65e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756  70 IPVLDAAGVHARLASRTHDAAKDTFAAFYSSWTGCITTDPAAIVLPFDDHMVHRGHGVFDTAHLENGALHLLDRHLARFK 149
Cdd:PLN02845  13 PPLLSAAEMIQRLQSKWSDAKKQNFGAMYSSVVGGITTDPAAMVIPLDDHMVHRGHGVFDTATIRDGHLYELDAHLDRFL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 150 RSMAAARVPPPFGdgdgdgddcAEKMKAIILRVAAASGVRdHGQVRYYASAGPGGFALSREECVRSVFYVVVVRKKRRAG 229
Cdd:PLN02845  93 RSAAKAKIPLPFD---------RATLRRILLQTVAASGCR-NGSLRYWLSAGPGGFSLSPSGCSEPAFYAVVIEDTYAQD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 230 AgekPKRLRVVTTPIPMKPGVFATTKTTNYLPNALVVADAIDKRADVGLWVTENGFVGEGPSMNVAFLVPADdagggggg 309
Cdd:PLN02845 163 R---PEGVKVVTSSVPIKPPQFATVKSVNYLPNALSQMEAEERGAFAGIWLDEEGFVAEGPNMNVAFLTNDG-------- 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 310 deedetvcgeafktnkkwKLVSPPTSNILAGCTVARVAELVNdaKVLEHLNVAAFEFRDVGVEEGKRARETMLIGSVIHV 389
Cdd:PLN02845 232 ------------------ELVLPPFDKILSGCTARRVLELAP--RLVSPGDLRGVKQRKISVEEAKAADEMMLIGSGVPV 291

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 303280756 390 APVVEWDGEAVGDETTteTPIADALHAAVVRDIATNVPEL-TPVPYE 435
Cdd:PLN02845 292 LPIVSWDGQPIGDGKV--GPITLALHDLLLDDMRSGPPGVrTPVPYG 336
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
 107-417 1.38e-34

Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439885 [Multi-domain]  Cd Length: 285  Bit Score: 129.92  E-value: 1.38e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 107 TDPAAIVLPFDDHMVHRGHGVFDTAHLENGALHLLDRHLARFKRSMAAARVPPPFGdgdgdgddcAEKMKAIILRVAAAS 186
Cdd:COG0115   10 VPEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYT---------EEELLEAIRELVAAN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 187 GVRDhGQVRYYASAGPGGFALSREECVRSVFYVVVVRKKRRAGAGEKPKRLRVVTTPIPMkPGVFATTKTTNYLPNALVV 266
Cdd:COG0115   81 GLED-GYIRPQVTRGVGGRGVFAEEYEPTVIIIASPLPAYPAEAYEKGVRVITSPYRRAA-PGGLGGIKTGNYLNNVLAK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 267 ADAIDKRADVGLWVTENGFVGEGPSMNVaFLVpaddaggggggdeedetvcgeafktnKKWKLVSPPTSN-ILAGCTVAR 345
Cdd:COG0115  159 QEAKEAGADEALLLDTDGYVAEGSGSNV-FIV--------------------------KDGVLVTPPLSGgILPGITRDS 211

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 303280756 346 VAELvndakvLEHLNVAAFEfRDVGVEEGKRARETMLIGSVIHVAPVVEWDGEAVGDetTTETPIADALHAA 417
Cdd:COG0115  212 VIEL------ARELGIPVEE-RPISLEELYTADEVFLTGTAAEVTPVTEIDGRPIGD--GKPGPVTRRLREL 274
ADCL_like cd01559
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ...
 118-397 1.73e-34

ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent enzymes that converts 4-amino-4-deoxychorismate (ADC) to p-aminobenzoate and pyruvate. Based on the information available from the crystal structure, most members of this subgroup are likely to function as dimers. The enzyme from E.Coli, the structure of which is available, is a homodimer that is folded into a small and a larger domain. The coenzyme pyridoxal 5; -phosphate resides at the interface of the two domains that is linked by a flexible loop. Members of this subgroup are found in Eukaryotes and bacteria.


Pssm-ID: 238800 [Multi-domain]  Cd Length: 249  Bit Score: 128.97  E-value: 1.73e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 118 DHMVHRGHGVFDTAHLENGALHLLDRHLARFKRSMAAARVPPPFGdgdgdgddcaEKMKAIILRVAAASGVRDHGqVRYY 197
Cdd:cd01559    1 DRGFAYGDGVFETMRALDGRLFLLDAHLARLERSARRLGIPEPDL----------PRLRAALESLLAANDIDEGR-IRLI 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 198 ASAGPGGFALSREECVRSVFYVVVVRKKRRAGagekPKRLRVVTTPIPM-KPGVFATTKTTNYLPNALVVADAIDKRADV 276
Cdd:cd01559   70 LSRGPGGRGYAPSVCPGPALYVSVIPLPPAWR----QDGVRLITCPVRLgEQPLLAGLKHLNYLENVLAKREARDRGADE 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 277 GLWVTENGFVGEGPSMNVAFLvpaddaggggggdeedetvcgeafktnKKWKLVSPP-TSNILAGCTVARVAELVNDAKV 355
Cdd:cd01559  146 ALFLDTDGRVIEGTASNLFFV---------------------------KDGELVTPSlDRGGLAGITRQRVIELAAAKGY 198

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 303280756 356 lehlnvaAFEFRDVGVEEGKRARETMLIGSVIHVAPVVEWDG 397
Cdd:cd01559  199 -------AVDERPLRLEDLLAADEAFLTNSLLGVAPVTAIDD 233
PLPDE_IV cd00449
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ...
 118-414 8.55e-33

PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, one of five classes of PLPDE, consists of branched-chain amino acid aminotransferases (BCAT), D-amino acid transferases (DAAT), and 4-amino-4-deoxychorismate lyases (ADCL). BCAT catalyzes the reversible transamination reaction between the L-branched-chain amino and alpha-keto acids. DAAT catalyzes the synthesis of D-glutamic acid and D-alanine, and ADCL converts 4-amino-4-deoxychorismate to p-aminobenzoate and pyruvate. Except for a few enzymes, i. e., Escherichia coli and Salmonella BCATs, which are homohexamers arranged as a double trimer, the class IV PLPDEs are homodimers. Homodimer formation is required for catalytic activity.


Pssm-ID: 238254 [Multi-domain]  Cd Length: 256  Bit Score: 124.25  E-value: 8.55e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 118 DHMVHRGHGVFDTAHLENGALHLLDRHLARFKRSMAAARVPPPFGDgdgdgddcaEKMKAIILRVAAASGVRDhGQVRYY 197
Cdd:cd00449    1 DRGLHYGDGVFEGLRAGKGRLFRLDEHLDRLNRSAKRLGLPIPYDR---------EELREALKELVAANNGAS-LYIRPL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 198 ASAGPGGFALSREECVRSVFYVVVVRKKRRAGAGEKPKRLRVVTTPIPMKPGVFATTKTTNYLPNALVVADAIDKRADVG 277
Cdd:cd00449   71 LTRGVGGLGVAPPPSPEPTFVVFASPVGAYAKGGEKGVRLITSPDRRRAAPGGTGDAKTGGNLNSVLAKQEAAEAGADEA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 278 LWVTENGFVGEGPSMNVaFLVpaddaggggggdeedetvcgeafktnKKWKLVSPPTSN-ILAGCTVARVAELVNDakvl 356
Cdd:cd00449  151 LLLDDNGYVTEGSASNV-FIV--------------------------KDGELVTPPLDGgILPGITRDSVIELAKE---- 199

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 303280756 357 ehLNVAAFEfRDVGVEEGKRARETMLIGSVIHVAPVVEWDGEAVGDETTteTPIADAL 414
Cdd:cd00449  200 --LGIKVEE-RPISLDELYAADEVFLTGTAAEVTPVTEIDGRGIGDGKP--GPVTRKL 252
D-AAT_like cd01558
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ...
 115-402 5.23e-24

D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes transamination between D-amino acids and their respective alpha-keto acids. It plays a major role in the synthesis of bacterial cell wall components like D-alanine and D-glutamate in addition to other D-amino acids. The enzyme like other members of this superfamily requires PLP as a cofactor. Members of this subgroup are found in all three forms of life.


Pssm-ID: 238799 [Multi-domain]  Cd Length: 270  Bit Score: 100.75  E-value: 5.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 115 PFDDHMVHRGHGVFDTAHLENGALHLLDRHLARFKRSMAAARVPPPFGDgdgdgddcaEKMKAIILRVAAASGVRdHGQV 194
Cdd:cd01558   15 SVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTR---------EELKELIRELVAKNEGG-EGDV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 195 RYYAS--AGPGGFALSREECvrsVFYVVVVRKKRRAGAGEKPKRLRVVTTPIP--MKPGVfattKTTNYLPNALVVADAI 270
Cdd:cd01558   85 YIQVTrgVGPRGHDFPKCVK---PTVVIITQPLPLPPAELLEKGVRVITVPDIrwLRCDI----KSLNLLNNVLAKQEAK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 271 DKRADVGLWVTENGFVGEGPSMNVaFLVpaddaggggggdeedetvcgeafktnKKWKLVSPPTSN-ILAGCTVARVAEL 349
Cdd:cd01558  158 EAGADEAILLDADGLVTEGSSSNV-FIV--------------------------KNGVLVTPPLDNgILPGITRATVIEL 210

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 303280756 350 VNDakvlehLNVAAFEfRDVGVEEGKRARETMLIGSVIHVAPVVEWDGEAVGD 402
Cdd:cd01558  211 AKE------LGIPVEE-RPFSLEELYTADEVFLTSTTAEVMPVVEIDGRPIGD 256
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
 126-395 3.21e-22

Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to catalyze the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity.


Pssm-ID: 395844 [Multi-domain]  Cd Length: 221  Bit Score: 94.35  E-value: 3.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756  126 GVFDTAHLENGALHLLDRHLARFKRSMAAARVPPPFgdgdgdgddCAEKMKAIILRVAAASGVRDHGqVRYYASAGPGGF 205
Cdd:pfam01063   1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPF---------DEEDLRKIIEELLKANGLGVGR-LRLTVSRGPGGF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756  206 ALSREECVRSVFYVVVvrkkrRAGAGEKPKRLRVVTTPIPMKPgVFATTKTTNYLPNALVVADAIDKRADVGLWVTENGF 285
Cdd:pfam01063  71 GLPTSDPTLAIFVSAL-----PPPPESKKKGVISSLVRRNPPS-PLPGAKTLNYLENVLARREAKAQGADDALLLDEDGN 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756  286 VGEGPSMNVaFLVpaddaggggggdeedetvcgeafKTNkkwKLVSPP-TSNILAGCTVARVAELVNDAKVlehlnvaAF 364
Cdd:pfam01063 145 VTEGSTSNV-FLV-----------------------KGG---TLYTPPlESGILPGITRQALLDLAKALGL-------EV 190

                         250       260       270
                  ....*....|....*....|....*....|.
gi 303280756  365 EFRDVGVEEGKRARETMLIGSVIHVAPVVEW 395
Cdd:pfam01063 191 EERPITLADLQEADEAFLTNSLRGVTPVSSI 221
PRK06680 PRK06680
D-amino acid aminotransferase; Reviewed
 124-402 6.63e-12

D-amino acid aminotransferase; Reviewed


Pssm-ID: 180656 [Multi-domain]  Cd Length: 286  Bit Score: 65.72  E-value: 6.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 124 GHGVFDTAHLENGALHLLDRHLARFKRSMAAARVPPPFGDGDGdgddcAEKMKAII-----------LRVAAASGVRDHG 192
Cdd:PRK06680  29 ADGIYEVCAVRDGKLVDLDRHLARLFRSLGEIRIAPPMTRAEL-----VEVLRELIrrnrvreglvyLQVTRGVARRDHV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 193 qvryYASAG--PGGFALSREecvrsvfyVVVVRKKRRAGAGekpkrLRVVTTPIPMKPgvFATTKTTNYLPNALVVADAI 270
Cdd:PRK06680 104 ----FPAADvkPSVVVFAKS--------VDFARPAAAAETG-----IKVITVPDNRWK--RCDIKSVGLLPNVLAKQAAK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 271 DKRADVGlWVTENGFVGEGPSMNvAFLVpaddaggggggdeedetvcgeafktNKKWKLVSPPTSN-ILAGCTVARVAEL 349
Cdd:PRK06680 165 EAGAQEA-WMVDDGFVTEGASSN-AWIV-------------------------TKDGKLVTRPADNfILPGITRHTLIDL 217

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 303280756 350 vndAKVLeHLNVaafEFRDVGVEEGKRARETMLIGSVIHVAPVVEWDGEAVGD 402
Cdd:PRK06680 218 ---AKEL-GLEV---EERPFTLQEAYAAREAFITAASSFVFPVVQIDGKQIGN 263
PRK12479 PRK12479
branched-chain-amino-acid transaminase;
108-430 6.38e-09

branched-chain-amino-acid transaminase;


Pssm-ID: 183549 [Multi-domain]  Cd Length: 299  Bit Score: 56.89  E-value: 6.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 108 DPAAIVLPFDDHMVHRGHGVFDTAHLENGALHLLDRHLARFKRSMAAARVPPPFGdgdgdgddcAEKMKAIILRVAAASG 187
Cdd:PRK12479  14 EKEKAVVSVYDHGFLYGDGVFEGIRSYGGNVFCLKEHVKRLYESAKSILLTIPLT---------VDEMEEAVLQTLQKNE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 188 VRDhGQVRYYASAGPGGFALSREECVRSVFYVVVVRKKRRagagekPKR-----LRVVT------TPIPMKPGVfattKT 256
Cdd:PRK12479  85 YAD-AYIRLIVSRGKGDLGLDPRSCVKPSVIIIAEQLKLF------PQEfydngLSVVSvasrrnTPDALDPRI----KS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 257 TNYLPNALVVADAIDKRADVGLWVTENGFVGEGPSMNVaFLVpaddaggggggdeedetvcgeafktnKKWKLVSPPTS- 335
Cdd:PRK12479 154 MNYLNNVLVKIEAAQAGVLEALMLNQQGYVCEGSGDNV-FVV--------------------------KDGKVLTPPSYl 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 336 NILAGCTVARVAELVNDAKVleHLNVAAFEFRDVGVeegkrARETMLIGSVIHVAPVVEWDGEAVGDETTTE-TPIADAL 414
Cdd:PRK12479 207 GALEGITRNSVIELCERLSI--PCEERPFTRHDVYV-----ADEVFLTGTAAELIPVVKVDSREIGDGKPGSvTKQLTEE 279

                        330
                 ....*....|....*.
gi 303280756 415 HAAVVRDIATNVPELT 430
Cdd:PRK12479 280 FKKLTRERGVRVPGLA 295
PRK08320 PRK08320
branched-chain amino acid aminotransferase; Reviewed
 118-402 5.48e-08

branched-chain amino acid aminotransferase; Reviewed


Pssm-ID: 236238 [Multi-domain]  Cd Length: 288  Bit Score: 54.11  E-value: 5.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 118 DHMVHRGHGVFDTAHLENGALHLLDRHLARFKRSMAAARVPPPFGdgdgdgddcAEKMKAIILRVAAASGVRDhGQVRYY 197
Cdd:PRK08320  23 DHGFLYGDGVFEGIRAYNGRVFRLKEHIDRLYDSAKAIMLEIPLS---------KEEMTEIVLETLRKNNLRD-AYIRLV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 198 ASAGPGGFALSREECvrsvfyvvvvrkkrragagEKP------------------KRLRVVTTPI------PMKPGVfat 253
Cdd:PRK08320  93 VSRGVGDLGLDPRKC-------------------PKPtvvciaepiglypgelyeKGLKVITVSTrrnrpdALSPQV--- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 254 tKTTNYLPNALVVADAIDKRADVGLWVTENGFVGEGPSMNVaFLVpaddaggggggdeedetvcgeafktnKKWKLVSPP 333
Cdd:PRK08320 151 -KSLNYLNNILAKIEANLAGVDEAIMLNDEGYVAEGTGDNI-FIV--------------------------KNGKLITPP 202

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 303280756 334 TS-NILAGCTVARVAELVNDA--KVLEhlnvAAFEFRDVGVeegkrARETMLIGSVIHVAPVVEWDGEAVGD 402
Cdd:PRK08320 203 TYaGALEGITRNAVIEIAKELgiPVRE----ELFTLHDLYT-----ADEVFLTGTAAEVIPVVKVDGRVIGD 265
PRK07849 PRK07849
aminodeoxychorismate lyase;
108-421 8.44e-07

aminodeoxychorismate lyase;


Pssm-ID: 236114 [Multi-domain]  Cd Length: 292  Bit Score: 50.34  E-value: 8.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 108 DPAAIVLPFDDHMVHRGHGVFDTAHLENGALHLLDRHLARFKRSMAAARVP-PPFGDGDGDGDDCAEKMKAI----ILRV 182
Cdd:PRK07849  22 DPSAPLLHADDLAAVRGDGVFETLLVRDGRPCNLEAHLERLARSAALLDLPePDLDRWRRAVELAIEEWRAPedeaALRL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 183 AAASGVRDHGQVRYYASAGPGGFALSREecvrsvfyvvvvrkkRRAGagekpkrLRVVTTPIPMKPGVFATT-------K 255
Cdd:PRK07849 102 VYSRGRESGGAPTAWVTVSPVPERVARA---------------RREG-------VSVITLDRGYPSDAAERApwllagaK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 256 TTNYLPNALVVADAIDKRADVGLWVTENGFVGEGPSMNVaflvpaddaggggggdeedETVCGEAFKTnkkwklvSPPTS 335
Cdd:PRK07849 160 TLSYAVNMAALRYAARRGADDVIFTSTDGYVLEGPTSTV-------------------VIATDDRLLT-------PPPWY 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 336 NILAGCTVARvaelvndakVLEHLNVAAFE--FRDVGVEEGKRARETMLIGSVIHVAPVVEWDGEAVG-DETTTEtpIAD 412
Cdd:PRK07849 214 GILPGTTQAA---------LFEVAREKGWDceYRALRPADLFAADGVWLVSSVRLAARVHTLDGRPLPrDPLADE--LTE 282


                 ....*....
gi 303280756 413 ALHAAVVRD 421
Cdd:PRK07849 283 LVDAAIVSD 291
PRK12400 PRK12400
D-amino acid aminotransferase; Reviewed
 124-402 4.97e-06

D-amino acid aminotransferase; Reviewed


Pssm-ID: 171470  Cd Length: 290  Bit Score: 48.09  E-value: 4.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 124 GHGVFDTAHLENGALHLLDRHLARFKRSMAAARVPPPFgdgdgdgddcaEKMKAIIL--RVAAASGVRDHGQVRYYASAG 201
Cdd:PRK12400  33 GDGVYEVIRLYKGNFHLLDPHITRLYRSMEEIELTLPF-----------SKAELITLlyKLIENNNFHEDGTIYLQVSRG 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 202 PGGFALSREECVRSVFYVVVVRKKRRAGAGEKPkrLRVVTTPIPMkpGVFATTKTTNYLPNALVVADAIDKRADVGLWVt 281
Cdd:PRK12400 102 VQARTHTFSYDVPPTIYAYITKKERPALWIEYG--VRAISEPDTR--WLRCDIKSLNLLPNILAATKAERKGCKEALFV- 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 282 ENGFVGEGPSMNVaFLVpaddaggggggdeedetvcgeafktnKKWKLVSPPTSN-ILAGCTVARVAELVNDAK--VLEH 358
Cdd:PRK12400 177 RNGTVTEGSHSNF-FLI--------------------------KNGTLYTHPANHlILNGIIRQYVLSLAKTLRipVQEE 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 303280756 359 LnvaaFEFRDVgveegKRARETMLIGSVIHVAPVVEWDGEAVGD 402
Cdd:PRK12400 230 L----FSVRDV-----YQADECFFTGTTIEILPMTHLDGTAIQD 264
PRK07650 PRK07650
4-amino-4-deoxychorismate lyase; Provisional
 111-296 3.62e-04

4-amino-4-deoxychorismate lyase; Provisional


Pssm-ID: 181067  Cd Length: 283  Bit Score: 42.26  E-value: 3.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 111 AIVLPFDdHMVHRGHGVFDTAHLENGALHLLDRHLARFKRSMAAARVPPPFGDgdgdgddcaEKMKAIILRVAAASGVRd 190
Cdd:PRK07650  14 ARISPFD-HGYLYGLGVFETFRIYNGHPFLLDDHYDRLNDALDTLQIEWTMTK---------DEVLLILKNLLEKNGLE- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 191 HGQVRYYASAGPGGFALSREECvrsvfyvvvvrkkrragagEKPKRLrVVTTPIPM------KPGVFATT---------- 254
Cdd:PRK07650  83 NAYVRFNVSAGIGEIGLQTEMY-------------------EEPTVI-VYMKPLAPpglpaeKEGVVLKQrrntpegafr 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 303280756 255 -KTTNYLPNALVVADaIDKRADV-GLWVTENGFVGEGPSMNVAF 296
Cdd:PRK07650 143 lKSHHYLNNILGKRE-IGNDPNKeGIFLTEEGYVAEGIVSNLFW 185
PRK06606 PRK06606
branched-chain amino acid transaminase;
256-420 2.09e-03

branched-chain amino acid transaminase;


Pssm-ID: 235841  Cd Length: 306  Bit Score: 39.74  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 256 TTNYLPNALVVADAIDKRADVGLWVTENGFVGEGPSMNVaFLVpaddaggggggdeedetvcgeafktnKKWKLVSPP-T 334
Cdd:PRK06606 161 SGNYLNSILAKTEARRNGYDEALLLDVEGYVSEGSGENI-FIV--------------------------RDGVLYTPPlT 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303280756 335 SNILAGCTVARVAELVNDA--KVLEhlnvaafefRDVGVEEGKRARETMLIGSVIHVAPVVEWDGEAVGDEttTETPIAD 412
Cdd:PRK06606 214 SSILEGITRDTVITLAKDLgiEVIE---------RRITRDELYIADEVFFTGTAAEVTPIREVDGRQIGNG--KRGPITE 282

                        170
                 ....*....|.
gi 303280756 413 ALHAA---VVR 420
Cdd:PRK06606 283 KLQSAyfdIVR 293
 
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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