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Conserved domains on  [gi|1625600651|gb|TIC51568|]
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PLP-dependent transferase [Wallemia mellicola]

Protein Classification

PLP-dependent aminotransferase family protein( domain architecture ID 139552)

PLP-dependent aminotransferase family protein may combine pyridoxal phosphate with an alpha-amino acid to form a Schiff base or aldimine intermediate, which then acts as the substrate in a reaction such as a transamination, racemization, or decarboxylation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 66-526 6.11e-139

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


The actual alignment was detected with superfamily member PLN02822:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 481  Bit Score: 410.29  E-value: 6.11e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651  66 LSSTEIDELVDDWQPEPLVPQ-AEIKQAPTIIGPPSIKPKVSQPGqpsdkaRQVTNLVSYNFLGLLGDQRIKDAATKALR 144
Cdd:PLN02822   64 LTEKEIDELCDEWTPEPLIPPiTEEMRPEPPVLESAAGPHTIING------KDVVNFASANYLGLIGNEKIKESCTSALE 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 145 VYGVGSCGPPGFYGTMDVHIDLEKSIAQTLGTESAIIYSQGFATITSVIPTFAKRGDIIVADEGCSFAIRKGLQISRSTV 224
Cdd:PLN02822  138 KYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTI 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 225 RWYKHNDMNSLETVLDSINREAKRRKAPltRKFICSEGIFQNDGSLANLKRIIELKKKYKYRLILEESYSFGVVGNTGRG 304
Cdd:PLN02822  218 VYFKHNDMESLRNTLEKLTAENKRKKKL--RRYIVVEAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRG 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 305 MTELYDIPAKEVDILVGSMANTLGSAGGFCAGESVVVEHQRINSAAFIFSASLPPMLAVSANETLSILNSSsgPNIVHSL 384
Cdd:PLN02822  296 LSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGYVFSASLPPYLASAAITAIDVLEDN--PSVLAKL 373

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 385 QTNIASFRSVLSTIDSIELASHALSPIQHVFFSQSkelqiiSTSQKEKSSeeerveaVLGDICDDALVN-GVFITVAghl 463
Cdd:PLN02822  374 KENIALLHKGLSDIPGLSIGSNTLSPIVFLHLEKS------TGSAKEDLS-------LLEHIADRMLKEdSVLVVVS--- 437

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1625600651 464 rgQES--DIGALSAGstgirvapggapppteprasIKIAISSALSKKETEKAALVVKNSINRVLK 526
Cdd:PLN02822  438 --KRStlDKCRLPVG--------------------IRLFVSAGHTESDILKASESLKRVAASVLK 480
 
Name Accession Description Interval E-value
PLN02822 PLN02822
serine palmitoyltransferase
 66-526 6.11e-139

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 410.29  E-value: 6.11e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651  66 LSSTEIDELVDDWQPEPLVPQ-AEIKQAPTIIGPPSIKPKVSQPGqpsdkaRQVTNLVSYNFLGLLGDQRIKDAATKALR 144
Cdd:PLN02822   64 LTEKEIDELCDEWTPEPLIPPiTEEMRPEPPVLESAAGPHTIING------KDVVNFASANYLGLIGNEKIKESCTSALE 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 145 VYGVGSCGPPGFYGTMDVHIDLEKSIAQTLGTESAIIYSQGFATITSVIPTFAKRGDIIVADEGCSFAIRKGLQISRSTV 224
Cdd:PLN02822  138 KYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTI 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 225 RWYKHNDMNSLETVLDSINREAKRRKAPltRKFICSEGIFQNDGSLANLKRIIELKKKYKYRLILEESYSFGVVGNTGRG 304
Cdd:PLN02822  218 VYFKHNDMESLRNTLEKLTAENKRKKKL--RRYIVVEAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRG 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 305 MTELYDIPAKEVDILVGSMANTLGSAGGFCAGESVVVEHQRINSAAFIFSASLPPMLAVSANETLSILNSSsgPNIVHSL 384
Cdd:PLN02822  296 LSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGYVFSASLPPYLASAAITAIDVLEDN--PSVLAKL 373

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 385 QTNIASFRSVLSTIDSIELASHALSPIQHVFFSQSkelqiiSTSQKEKSSeeerveaVLGDICDDALVN-GVFITVAghl 463
Cdd:PLN02822  374 KENIALLHKGLSDIPGLSIGSNTLSPIVFLHLEKS------TGSAKEDLS-------LLEHIADRMLKEdSVLVVVS--- 437

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1625600651 464 rgQES--DIGALSAGstgirvapggapppteprasIKIAISSALSKKETEKAALVVKNSINRVLK 526
Cdd:PLN02822  438 --KRStlDKCRLPVG--------------------IRLFVSAGHTESDILKASESLKRVAASVLK 480
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 116-424 1.85e-79

KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.


Pssm-ID: 99747 [Multi-domain]  Cd Length: 349  Bit Score: 252.48  E-value: 1.85e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 116 RQVTNLVSYNFLGLLGDQRIKDAATKALRVYGVGSCGPPGFYGTMDVHIDLEKSIAQTLGTESAIIYSQGFATITSVIPT 195
Cdd:cd06454     1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 196 FAKRGDIIVADEGCSFAIRKGLQISRSTVRWYKHNDMNSLETVLdsinREAKRrkaPLTRKFICSEGIFQNDGSLANLKR 275
Cdd:cd06454    81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLL----REARR---PYGKKLIVTEGVYSMDGDIAPLPE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 276 IIELKKKYKYRLILEESYSFGVVGNTGRGmTELYDIPAKEVDILVGSMANTLGSAGGFCAGESVVVEHQRINSAAFIFSA 355
Cdd:cd06454   154 LVDLAKKYGAILFVDEAHSVGVYGPHGRG-VEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFST 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 356 SLPPMLAVSANETLSILnsSSGPNIVHSLQTNIASFRSVLSTIDsIELASHALSPIQ-HVFFSQSKELQI 424
Cdd:cd06454   233 SLPPAVAAAALAALEVL--QGGPERRERLQENVRYLRRGLKELG-FPVGGSPSHIIPpLIGDDPAKAVAF 299
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 116-412 5.23e-79

7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 439926 [Multi-domain]  Cd Length: 385  Bit Score: 252.66  E-value: 5.23e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 116 RQVTNLVSYNFLGLLGDQRIKDAATKALRVYGVGSCGPPGFYGTMDVHIDLEKSIAQTLGTESAIIYSQGFATITSVIPT 195
Cdd:COG0156    37 REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISA 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 196 FAKRGDIIVADEGCSFAIRKGLQISRSTVRWYKHNDMNSLETVLdsinreAKRRKAPltRKFICSEGIFQNDGSLANLKR 275
Cdd:COG0156   117 LAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLL------KKARAAR--RKLIVTDGVFSMDGDIAPLPE 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 276 IIELKKKYKYRLILEESYSFGVVGNTGRGMTELYDIpAKEVDILVGSMANTLGSAGGFCAGESVVVEHQRINSAAFIFSA 355
Cdd:COG0156   189 IVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGL-EDRVDIIMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFST 267

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1625600651 356 SLPPMLAVSANETLSILnsSSGPNIVHSLQTNIASFRSVLSTIDSIELASHalSPIQ 412
Cdd:COG0156   268 ALPPAVAAAALAALEIL--REEPELRERLWENIAYFREGLKELGFDLGPSE--SPIV 320
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 113-395 9.85e-35

5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an enzyme for one of two routes to the heme precursor 5-aminolevulinate. The protein is a pyridoxal phosphate-dependent enzyme related to 2-amino-3-ketobutyrate CoA tranferase and 8-amino-7-oxononanoate synthase. This enzyme appears restricted to the alpha Proteobacteria and mitochondrial derivatives. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273820 [Multi-domain]  Cd Length: 402  Bit Score: 134.86  E-value: 9.85e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 113 DKARQVTNLVSYNFLGLLGDQRIKDAATKALRVYGVGSCGPPGFYGTMDVHIDLEKSIAQTLGTESAIIYSQGFATITSV 192
Cdd:TIGR01821  42 DGAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDAT 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 193 IPTFAKR--GDIIVADEGCSFAIRKGLQISRSTVRWYKHNDMNSLETVLDSINReakrrKAPltrKFICSEGIFQNDGSL 270
Cdd:TIGR01821 122 LATLAKIipGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSVDP-----NRP---KIIAFESVYSMDGDI 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 271 ANLKRIIELKKKYKYRLILEESYSFGVVGNTGRGMTELYDIpAKEVDILVGSMANTLGSAGGFCAGESVVVEHQRINSAA 350
Cdd:TIGR01821 194 APIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGL-MHRIDIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPG 272

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1625600651 351 FIFSASLPPMLAVSANETLSILNSSSGPNIVHslQTNIASFRSVL 395
Cdd:TIGR01821 273 FIFTTSLPPAIAAGATASIRHLKESQDLRRAH--QENVKRLKNLL 315
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
116-407 9.79e-26

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 108.16  E-value: 9.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 116 RQVTNLVSYNFLGLLgdqrIKDAATKALRVygvGSCGPPGFYGTMDVHIDLEKSIAQ--------TLGTESAIIYSQGFA 187
Cdd:pfam00155   1 TDKINLGSNEYLGDT----LPAVAKAEKDA---LAGGTRNLYGPTDGHPELREALAKflgrspvlKLDREAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 188 TITSVIPTFAK-RGDIIVADEGCSFAIRKGLQISRSTVRWYK-------HNDMNSLETVLDSInreakrrkapltRKFIC 259
Cdd:pfam00155  74 ANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK------------PKVVL 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 260 SEGIFQNDGSLAN---LKRIIELKKKYKYRLILEESYSFGVVGNTGRGMTELYDIPAKEVdILVGSMANTLGSAG---GF 333
Cdd:pfam00155 142 HTSPHNPTGTVATleeLEKLLDLAKEHNILLLVDEAYAGFVFGSPDAVATRALLAEGPNL-LVVGSFSKAFGLAGwrvGY 220

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1625600651 334 CAGESVVVEHQRINSAAFIFSASLPPMLAVSANETLSILnsSSGPNIVHSLQTNIASFRSVLSTIDSIELASHA 407
Cdd:pfam00155 221 ILGNAAVISQLRKLARPFYSSTHLQAAAAAALSDPLLVA--SELEEMRQRIKERRDYLRDGLQAAGLSVLPSQA 292
 
Name Accession Description Interval E-value
PLN02822 PLN02822
serine palmitoyltransferase
 66-526 6.11e-139

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 410.29  E-value: 6.11e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651  66 LSSTEIDELVDDWQPEPLVPQ-AEIKQAPTIIGPPSIKPKVSQPGqpsdkaRQVTNLVSYNFLGLLGDQRIKDAATKALR 144
Cdd:PLN02822   64 LTEKEIDELCDEWTPEPLIPPiTEEMRPEPPVLESAAGPHTIING------KDVVNFASANYLGLIGNEKIKESCTSALE 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 145 VYGVGSCGPPGFYGTMDVHIDLEKSIAQTLGTESAIIYSQGFATITSVIPTFAKRGDIIVADEGCSFAIRKGLQISRSTV 224
Cdd:PLN02822  138 KYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTI 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 225 RWYKHNDMNSLETVLDSINREAKRRKAPltRKFICSEGIFQNDGSLANLKRIIELKKKYKYRLILEESYSFGVVGNTGRG 304
Cdd:PLN02822  218 VYFKHNDMESLRNTLEKLTAENKRKKKL--RRYIVVEAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRG 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 305 MTELYDIPAKEVDILVGSMANTLGSAGGFCAGESVVVEHQRINSAAFIFSASLPPMLAVSANETLSILNSSsgPNIVHSL 384
Cdd:PLN02822  296 LSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGYVFSASLPPYLASAAITAIDVLEDN--PSVLAKL 373

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 385 QTNIASFRSVLSTIDSIELASHALSPIQHVFFSQSkelqiiSTSQKEKSSeeerveaVLGDICDDALVN-GVFITVAghl 463
Cdd:PLN02822  374 KENIALLHKGLSDIPGLSIGSNTLSPIVFLHLEKS------TGSAKEDLS-------LLEHIADRMLKEdSVLVVVS--- 437

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1625600651 464 rgQES--DIGALSAGstgirvapggapppteprasIKIAISSALSKKETEKAALVVKNSINRVLK 526
Cdd:PLN02822  438 --KRStlDKCRLPVG--------------------IRLFVSAGHTESDILKASESLKRVAASVLK 480
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 120-527 3.02e-84

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 266.39  E-value: 3.02e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 120 NLVSYNFLGLLGDQRIKDAATKALRVYGVGSCGPPGFYGTMDVHIDLEKSIAQTLGTESAIIYSQGFATITSVIPTFAKR 199
Cdd:PLN03227    2 NFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAKR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 200 GDIIVADEGCSFAIRKGLQISRSTVRWYKHNDMNSLETVLDSINRE--AKRRKAPLTRKFICSEGIFQNDGSLANLKRII 277
Cdd:PLN03227   82 GDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQVRAQdvALKRKPTDQRRFLVVEGLYKNTGTLAPLKELV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 278 ELKKKYKYRLILEESYSFGVVGNTGRGMTELYDI-PAKEVDILVGSMANTLGSAGGFCAGESVVVEHQRINSAAFIFSAS 356
Cdd:PLN03227  162 ALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLkPMVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFSAS 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 357 LPPMLAVSANETLSilNSSSGPNIVHSLQTNIASFRSVLSTidsielASHALS-PIQHVFFSQSKELQIISTSQKEKSSE 435
Cdd:PLN03227  242 APPFLAKADATATA--GELAGPQLLNRLHDSIANLYSTLTN------SSHPYAlKLRNRLVITSDPISPIIYLRLSDQEA 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 436 EERVEAV--LGDICDDALVNGVFITVAGhlrgqesdigalsagsTGIRVAPGGAPPPtepraSIKIAISSALSKKETEKA 513
Cdd:PLN03227  314 TRRTDETliLDQIAHHSLSEGVAVVSTG----------------GHVKKFLQLVPPP-----CLRVVANASHTREDIDKL 372

                         410
                  ....*....|....
gi 1625600651 514 ALVVKNSINRVLKR 527
Cdd:PLN03227  373 LTVLGEAVEAILCK 386
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 116-424 1.85e-79

KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.


Pssm-ID: 99747 [Multi-domain]  Cd Length: 349  Bit Score: 252.48  E-value: 1.85e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 116 RQVTNLVSYNFLGLLGDQRIKDAATKALRVYGVGSCGPPGFYGTMDVHIDLEKSIAQTLGTESAIIYSQGFATITSVIPT 195
Cdd:cd06454     1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 196 FAKRGDIIVADEGCSFAIRKGLQISRSTVRWYKHNDMNSLETVLdsinREAKRrkaPLTRKFICSEGIFQNDGSLANLKR 275
Cdd:cd06454    81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLL----REARR---PYGKKLIVTEGVYSMDGDIAPLPE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 276 IIELKKKYKYRLILEESYSFGVVGNTGRGmTELYDIPAKEVDILVGSMANTLGSAGGFCAGESVVVEHQRINSAAFIFSA 355
Cdd:cd06454   154 LVDLAKKYGAILFVDEAHSVGVYGPHGRG-VEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFST 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 356 SLPPMLAVSANETLSILnsSSGPNIVHSLQTNIASFRSVLSTIDsIELASHALSPIQ-HVFFSQSKELQI 424
Cdd:cd06454   233 SLPPAVAAAALAALEVL--QGGPERRERLQENVRYLRRGLKELG-FPVGGSPSHIIPpLIGDDPAKAVAF 299
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 116-412 5.23e-79

7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 439926 [Multi-domain]  Cd Length: 385  Bit Score: 252.66  E-value: 5.23e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 116 RQVTNLVSYNFLGLLGDQRIKDAATKALRVYGVGSCGPPGFYGTMDVHIDLEKSIAQTLGTESAIIYSQGFATITSVIPT 195
Cdd:COG0156    37 REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISA 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 196 FAKRGDIIVADEGCSFAIRKGLQISRSTVRWYKHNDMNSLETVLdsinreAKRRKAPltRKFICSEGIFQNDGSLANLKR 275
Cdd:COG0156   117 LAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLL------KKARAAR--RKLIVTDGVFSMDGDIAPLPE 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 276 IIELKKKYKYRLILEESYSFGVVGNTGRGMTELYDIpAKEVDILVGSMANTLGSAGGFCAGESVVVEHQRINSAAFIFSA 355
Cdd:COG0156   189 IVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGL-EDRVDIIMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFST 267

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1625600651 356 SLPPMLAVSANETLSILnsSSGPNIVHSLQTNIASFRSVLSTIDSIELASHalSPIQ 412
Cdd:COG0156   268 ALPPAVAAAALAALEIL--REEPELRERLWENIAYFREGLKELGFDLGPSE--SPIV 320
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 116-513 2.60e-55

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 190.37  E-value: 2.60e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 116 RQVTNLVSYNFLGLLGDQRIKDAATKALRVYGVGSCGPPGFYGTMDVHIDLEKSIAQTLGTESAIIYSQGFATITSVIPT 195
Cdd:PRK05958   39 RRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTA 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 196 FAKRGDIIVADEGCSFAIRKGLQISRSTVRWYKHNDMNSLETVLdsinreAKRRKApltRKFICSEGIFQNDGSLANLKR 275
Cdd:PRK05958  119 LAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALL------AKWRAG---RALIVTESVFSMDGDLAPLAE 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 276 IIELKKKYKYRLILEESYSFGVVGNTGRGMTELYDIPAKEVDILVGSMANTLGSAGGFCAGESVVVEHQrINSAA-FIFS 354
Cdd:PRK05958  190 LVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVILVGTLGKALGSSGAAVLGSETLIDYL-INRARpFIFT 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 355 ASLPPMLAVSANETLSILnsSSGPNIVHSLQTNIASFRSVLSTIDSIELASHalSPIQHVffsqskelqiistsqkekss 434
Cdd:PRK05958  269 TALPPAQAAAARAALRIL--RREPERRERLAALIARLRAGLRALGFQLMDSQ--SAIQPL-------------------- 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 435 eeerveaVLGDicddalvNGVFITVAGHLRGQESDIGAlsagstgIRvapggapPPTEPR--ASIKIAISSALSKKETEK 512
Cdd:PRK05958  325 -------IVGD-------NERALALAAALQEQGFWVGA-------IR-------PPTVPAgtSRLRITLTAAHTEADIDR 376


                  .
gi 1625600651 513 A 513
Cdd:PRK05958  377 L 377
PLN02483 PLN02483
serine palmitoyltransferase
 112-395 2.81e-50

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 179.57  E-value: 2.81e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 112 SDKARQVTNLVSYNFLGLLG-DQRIKDAATKALRVYGVGSCGPPGFYGTMDVHIDLEKSIAQTLGTESAIIYSQGFATIT 190
Cdd:PLN02483   96 TTKTRRCLNLGSYNYLGFAAaDEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNS 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 191 SVIPTFAKRGDIIVADEGCSFAIRKGLQISRSTVRWYKHNDMNSLETVL-DSINREAKRRKAPLTRKFICSEGIFQNDGS 269
Cdd:PLN02483  176 TIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLrEQIAEGQPRTHRPWKKIIVIVEGIYSMEGE 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 270 LANLKRIIELKKKYKYRLILEESYSFGVVGNTGRGMTELYDIPAKEVDILVGSMANTLGSAGGFCAGESVVVEHQRINSA 349
Cdd:PLN02483  256 LCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCP 335

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1625600651 350 AFIFSASLPPmlaVSANETLSILN-------SSSGPNIVHSLQTNIASFRSVL 395
Cdd:PLN02483  336 AHLYATSMSP---PAVQQVISAIKvilgedgTNRGAQKLAQIRENSNFFRSEL 385
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 116-396 2.67e-45

2-amino-3-ketobutyrate coenzyme A ligase; Provisional


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 163.83  E-value: 2.67e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 116 RQVTNLVSYNFLGLLGDQRIKDAATKALRVYGVGS------CGppgfygTMDVHIDLEKSIAQTLGTESAIIYSQGFATI 189
Cdd:PRK06939   42 KEVINFCANNYLGLANHPELIAAAKAALDSHGFGMasvrfiCG------TQDLHKELEEKLAKFLGTEDAILYSSCFDAN 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 190 TSVIPTFAKRGDIIVADEGCSFAIRKGLQISRSTVRWYKHNDMNSLETVLdsinREAkrRKAPLTRKFICSEGIFQNDGS 269
Cdd:PRK06939  116 GGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQL----KEA--KEAGARHKLIATDGVFSMDGD 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 270 LANLKRIIELKKKYKYRLILEESYSFGVVGNTGRGMTELYDIPAKeVDILVGSMANTLGSA-GGFCAGESVVVEHQRINS 348
Cdd:PRK06939  190 IAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDR-VDIITGTLGKALGGAsGGYTAGRKEVIDWLRQRS 268

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1625600651 349 AAFIFSASLPPMLAVSANETLSILnsSSGPNIVHSLQTNIASFRSVLS 396
Cdd:PRK06939  269 RPYLFSNSLAPAIVAASIKVLELL--EESDELRDRLWENARYFREGMT 314
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 113-395 9.85e-35

5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an enzyme for one of two routes to the heme precursor 5-aminolevulinate. The protein is a pyridoxal phosphate-dependent enzyme related to 2-amino-3-ketobutyrate CoA tranferase and 8-amino-7-oxononanoate synthase. This enzyme appears restricted to the alpha Proteobacteria and mitochondrial derivatives. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273820 [Multi-domain]  Cd Length: 402  Bit Score: 134.86  E-value: 9.85e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 113 DKARQVTNLVSYNFLGLLGDQRIKDAATKALRVYGVGSCGPPGFYGTMDVHIDLEKSIAQTLGTESAIIYSQGFATITSV 192
Cdd:TIGR01821  42 DGAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDAT 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 193 IPTFAKR--GDIIVADEGCSFAIRKGLQISRSTVRWYKHNDMNSLETVLDSINReakrrKAPltrKFICSEGIFQNDGSL 270
Cdd:TIGR01821 122 LATLAKIipGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSVDP-----NRP---KIIAFESVYSMDGDI 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 271 ANLKRIIELKKKYKYRLILEESYSFGVVGNTGRGMTELYDIpAKEVDILVGSMANTLGSAGGFCAGESVVVEHQRINSAA 350
Cdd:TIGR01821 194 APIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGL-MHRIDIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPG 272

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1625600651 351 FIFSASLPPMLAVSANETLSILNSSSGPNIVHslQTNIASFRSVL 395
Cdd:TIGR01821 273 FIFTTSLPPAIAAGATASIRHLKESQDLRRAH--QENVKRLKNLL 315
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 113-399 7.54e-32

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 126.89  E-value: 7.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 113 DKARQVTNLVSYNFLGLLGDQRIKDAATKALRVYGVGSCGPPGFYGTMDVHIDLEKSIAQTLGTESAIIYSQGFATITSV 192
Cdd:PRK13392   43 DGPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAA 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 193 IPTFAKR--GDIIVADEGCSFAIRKGLQISRSTVRWYKHNDMNSLETVLDSinreakrrkAPLTR-KFICSEGIFQNDGS 269
Cdd:PRK13392  123 LSTLGKLlpGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLAS---------VDPDRpKLIAFESVYSMDGD 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 270 LANLKRIIELKKKYKYRLILEESYSFGVVGNTGRGMTElYDIPAKEVDILVGSMANTLGSAGGFCAGESVVVEHQRINSA 349
Cdd:PRK13392  194 IAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAE-RDGLMDRIDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAP 272

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1625600651 350 AFIFSASLPPMLAVSANETLSILNSSSGPNivHSLQTNIASFRSVLSTID 399
Cdd:PRK13392  273 GFIFTTALPPAVAAGATAAIRHLKTSQTER--DAHQDRVAALKAKLNANG 320
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
116-407 9.79e-26

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 108.16  E-value: 9.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 116 RQVTNLVSYNFLGLLgdqrIKDAATKALRVygvGSCGPPGFYGTMDVHIDLEKSIAQ--------TLGTESAIIYSQGFA 187
Cdd:pfam00155   1 TDKINLGSNEYLGDT----LPAVAKAEKDA---LAGGTRNLYGPTDGHPELREALAKflgrspvlKLDREAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 188 TITSVIPTFAK-RGDIIVADEGCSFAIRKGLQISRSTVRWYK-------HNDMNSLETVLDSInreakrrkapltRKFIC 259
Cdd:pfam00155  74 ANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK------------PKVVL 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 260 SEGIFQNDGSLAN---LKRIIELKKKYKYRLILEESYSFGVVGNTGRGMTELYDIPAKEVdILVGSMANTLGSAG---GF 333
Cdd:pfam00155 142 HTSPHNPTGTVATleeLEKLLDLAKEHNILLLVDEAYAGFVFGSPDAVATRALLAEGPNL-LVVGSFSKAFGLAGwrvGY 220

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1625600651 334 CAGESVVVEHQRINSAAFIFSASLPPMLAVSANETLSILnsSSGPNIVHSLQTNIASFRSVLSTIDSIELASHA 407
Cdd:pfam00155 221 ILGNAAVISQLRKLARPFYSSTHLQAAAAAALSDPLLVA--SELEEMRQRIKERRDYLRDGLQAAGLSVLPSQA 292
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 125-364 3.88e-20

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 93.20  E-value: 3.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 125 NFLGLLGDQRIKDAATKALRVYGVGSCGPPGFYGTMDVHIDLEKSIAQTLGTESAIIYSQGFATITSVIPTFAKRGDIIV 204
Cdd:PLN02955  111 DYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVAIGSVASLLA 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 205 AD----------------------EGCSFAIRKGlqisRSTVRWYKHNDMNSLETVLDSINreakrrkapLTRKFICSEG 262
Cdd:PLN02955  191 ASgkplknekvaifsdalnhasiiDGVRLAERQG----NVEVFVYRHCDMYHLNSLLSSCK---------MKRKVVVTDS 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 263 IFQNDGSLANLKRIIELKKKYKYRLILEESYSFGVVGNTGRGMTELYDIPAkEVDILVGSMANTLGSAGGFCAGESVVVE 342
Cdd:PLN02955  258 LFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEA-DVDLCVGTLSKAAGCHGGFIACSKKWKQ 336

                         250       260
                  ....*....|....*....|...
gi 1625600651 343 HQRINSAAFIFSASLP-PMLAVS 364
Cdd:PLN02955  337 LIQSRGRSFIFSTAIPvPMAAAA 359
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 118-364 4.52e-17

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 82.91  E-value: 4.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 118 VTNlvsyNFLGLLGDQRIKDAATKALRVY-------GVGSCGPPGFYGTMDVHIDLEKSIAQTLGTESAIIYSQGFATIT 190
Cdd:PRK05937   10 VTN----DFLGFSRSDTLVHEVEKRYRLYcrqfphaQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 191 SVIPTFAKRGDIIVADEGCSFAIRKGLQISRSTVRWYKHNDMNSLETVLDSINREAKRRkaplTRKFICSegIFQNDGSL 270
Cdd:PRK05937   86 GLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQRSFGR----IFIFVCS--VYSFKGTL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 271 ANLKRIIELKKKYKYRLILEESYSFGVVGNTGRGMTelYDIPAKEVDILVGSMANTLGSAGGFCAGESVVVEHQRINSAA 350
Cdd:PRK05937  160 APLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFC--HSLGYENFYAVLVTYSKALGSMGAALLSSSEVKQDLMLNSPP 237

                         250
                  ....*....|....
gi 1625600651 351 FIFSASLPPMLAVS 364
Cdd:PRK05937  238 LRYSTGLPPHLLIS 251
PRK07505 PRK07505
hypothetical protein; Provisional
 113-430 4.17e-12

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 68.08  E-value: 4.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 113 DKARQVTNLVSYNFLGLLGDQRIKDAATKALRVYGV-------GSCGPPgfygtmdVHIDLEKSIAQTLGTEsAIIYSQG 185
Cdd:PRK07505   43 ADGHTFVNFVSCSYLGLDTHPAIIEGAVDALKRTGSlhlsssrTRVRSQ-------ILKDLEEALSELFGAS-VLTFTSC 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 186 FATITSVIP-----TFAKRGDII-VADEGC--SFAIRKGLQISRSTVRWYKHNDMNSLETVldsinreAKRRKAPltrkF 257
Cdd:PRK07505  115 SAAHLGILPllasgHLTGGVPPHmVFDKNAhaSLNILKGICADETEVETIDHNDLDALEDI-------CKTNKTV----A 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 258 ICSEGIFQNdGSLANLKRIIELKKKYKYRLILEESYSFGVVGNTGRG--MTELyDIPAKEVDILVGSMANTLGSAGGFCa 335
Cdd:PRK07505  184 YVADGVYSM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyvRSEL-DYRLNERTIIAASLGKAFGASGGVI- 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 336 gesVVVEHQRINSA-----AFIFSASLP-PMLAVSAnETLSILNSSSGPNIVHSLQTNIASFRSVLSTIDsielaSHALS 409
Cdd:PRK07505  261 ---MLGDAEQIELIlryagPLAFSQSLNvAALGAIL-ASAEIHLSEELDQLQQKLQNNIALFDSLIPTEQ-----SGSFL 331

                         330       340
                  ....*....|....*....|.
gi 1625600651 410 PIQHVFFsqSKELQIISTSQK 430
Cdd:PRK07505  332 PIRLIYI--GDEDTAIKAAKQ 350
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 165-332 7.15e-06

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


Pssm-ID: 99742 [Multi-domain]  Cd Length: 170  Bit Score: 46.22  E-value: 7.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 165 DLEKSIAQTLGT--ESAIIYSQGFATITSVIPTFAKRGDIIVADEGCSF------AIRKGLQIsrstvrwykhNDMNSLE 236
Cdd:cd01494     4 ELEEKLARLLQPgnDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGsrywvaAELAGAKP----------VPVPVDD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 237 TVLDSIN-REAKRRKAPLTRKFICSEGIFQNDGSLANLKRIIELKKKYKYRLILEESYsfgVVGNTGRGMTELYDIPAke 315
Cdd:cd01494    74 AGYGGLDvAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAAS---AGGASPAPGVLIPEGGA-- 148

                         170
                  ....*....|....*..
gi 1625600651 316 vDILVGSMANTLGSAGG 332
Cdd:cd01494   149 -DVVTFSLHKNLGGEGG 164
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 166-247 5.39e-04

CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.


Pssm-ID: 99738 [Multi-domain]  Cd Length: 369  Bit Score: 42.19  E-value: 5.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600651 166 LEKSIAQTLGTESAIIYSQGFATITSVIPTFAKRGDIIVADE---GCSFA-IRKGLQISRSTVRWYkhnDMNSLETVLDS 241
Cdd:cd00614    45 LEKKLAALEGGEAALAFSSGMAAISTVLLALLKAGDHVVASDdlyGGTYRlFERLLPKLGIEVTFV---DPDDPEALEAA 121


                  ....*.
gi 1625600651 242 INREAK 247
Cdd:cd00614   122 IKPETK 127
PRK06234 PRK06234
methionine gamma-lyase; Provisional
 166-213 4.33e-03

methionine gamma-lyase; Provisional


Pssm-ID: 168478 [Multi-domain]  Cd Length: 400  Bit Score: 39.42  E-value: 4.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1625600651 166 LEKSIAQTLGTESAIIYSQGFATITSVIPTFAKRGDIIVADE---GCSFAI 213
Cdd:PRK06234   69 VENKLALLEGGEAAVVAASGMGAISSSLWSALKAGDHVVASDtlyGCTFAL 119
 
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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