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Conserved domains on  [gi|530419682|ref|XP_005261467|]
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2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial isoform X6 [Homo sapiens]

Protein Classification

PLP-dependent aminotransferase family protein( domain architecture ID 10797558)

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
2am3keto_CoA TIGR01822
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and ...
 27-444 0e+00

glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and bacterial (almost exclusively Proteobacterial) 2-amino-3-ketobutyrate--CoA ligase, now called glycine C-acetyltransferase. This enzyme can act in threonine catabolism. The closest homolog from Bacillus subtilis, and sequences like it, may be functionally equivalent but were not included in the model because of difficulty in finding reports of function. [Energy metabolism, Amino acids and amines]


:

Pssm-ID: 130881 [Multi-domain]  Cd Length: 393  Bit Score: 717.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682   27 LRGILEGELEGIRGAGTWKSERVITSRQGPHIRV-DGvsggpgtvifpglplphlsccihllsftSGILNFCANNYLGLS 105
Cdd:TIGR01822   1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVaDG----------------------------REVLNFCANNYLGLS 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  106 SHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNH 185
Cdd:TIGR01822  53 SHPDLIQAAKDALDEHGFGMSSVRFICGTQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNH 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  186 ASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKH--RLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATG 263
Cdd:TIGR01822 133 ASIIDGVRLCKAKRYRYANNDMADLEAQLKEARAAgaRHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATG 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  264 FLGPTGRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSN 343
Cdd:TIGR01822 213 FLGPTGRGSHELCGVMGRVDIITGTLGKALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASN 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  344 TIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHS 423
Cdd:TIGR01822 293 ELRDRLWANTRYFRERMEAAGFDIKPADHPIIPVMLYDAVLAQRFARRLLEEGIYVTGFFYPVVPKGQARIRVQISAAHT 372

                         410       420
                  ....*....|....*....|.
gi 530419682  424 EEDIDRCVEAFVEVGRLHGAL 444
Cdd:TIGR01822 373 EEQLDRAVEAFTRIGRELGVI 393
 
Name Accession Description Interval E-value
2am3keto_CoA TIGR01822
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and ...
 27-444 0e+00

glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and bacterial (almost exclusively Proteobacterial) 2-amino-3-ketobutyrate--CoA ligase, now called glycine C-acetyltransferase. This enzyme can act in threonine catabolism. The closest homolog from Bacillus subtilis, and sequences like it, may be functionally equivalent but were not included in the model because of difficulty in finding reports of function. [Energy metabolism, Amino acids and amines]


Pssm-ID: 130881 [Multi-domain]  Cd Length: 393  Bit Score: 717.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682   27 LRGILEGELEGIRGAGTWKSERVITSRQGPHIRV-DGvsggpgtvifpglplphlsccihllsftSGILNFCANNYLGLS 105
Cdd:TIGR01822   1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVaDG----------------------------REVLNFCANNYLGLS 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  106 SHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNH 185
Cdd:TIGR01822  53 SHPDLIQAAKDALDEHGFGMSSVRFICGTQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNH 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  186 ASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKH--RLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATG 263
Cdd:TIGR01822 133 ASIIDGVRLCKAKRYRYANNDMADLEAQLKEARAAgaRHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATG 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  264 FLGPTGRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSN 343
Cdd:TIGR01822 213 FLGPTGRGSHELCGVMGRVDIITGTLGKALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASN 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  344 TIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHS 423
Cdd:TIGR01822 293 ELRDRLWANTRYFRERMEAAGFDIKPADHPIIPVMLYDAVLAQRFARRLLEEGIYVTGFFYPVVPKGQARIRVQISAAHT 372

                         410       420
                  ....*....|....*....|.
gi 530419682  424 EEDIDRCVEAFVEVGRLHGAL 444
Cdd:TIGR01822 373 EEQLDRAVEAFTRIGRELGVI 393
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 31-444 0e+00

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 647.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  31 LEGELEGIRGAGTWKSERVITSRQGPHIRVdgvSGGpgtvifpglplphlsccihllsftSGILNFCANNYLGLSSHPEV 110
Cdd:PRK06939   9 LREELEEIKAEGLYKEERVITSPQGADITV---ADG------------------------KEVINFCANNYLGLANHPEL 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 111 IQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIID 190
Cdd:PRK06939  62 IAAAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIID 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 191 GIRLCKAHKYRYRHLDMADLEAKLQEAQK--HRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPT 268
Cdd:PRK06939 142 GVRLCKAKRYRYANNDMADLEAQLKEAKEagARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGEN 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 269 GRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQS 348
Cdd:PRK06939 222 GRGTVEHFGVMDRVDIITGTLGKALGGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDR 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 349 MAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDID 428
Cdd:PRK06939 302 LWENARYFREGMTAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLD 381

                        410
                 ....*....|....*.
gi 530419682 429 RCVEAFVEVGRLHGAL 444
Cdd:PRK06939 382 RAIDAFEKVGKELGVI 397
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 31-439 0e+00

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: 534.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  31 LEGELEGIRGAGTWKSERVITSRQGPHIRVDGvsggpgtvifpglplphlsccihllsftSGILNFCANNYLGLSSHPEV 110
Cdd:COG0156    5 LEAELAALKAAGLYRYLRVLESPQGPRVTIDG----------------------------REVLNFSSNDYLGLANHPRV 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 111 IQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIID 190
Cdd:COG0156   57 IEAAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIID 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 191 GIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGR 270
Cdd:COG0156  137 GARLSGAKVVRFRHNDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGR 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 271 GTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMA 350
Cdd:COG0156  217 GLVEHFGLEDRVDIIMGTLSKAL-GSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLW 295

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 351 AKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRC 430
Cdd:COG0156  296 ENIAYFREGLKELGFDLGPSESPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRL 375


                 ....*....
gi 530419682 431 VEAFVEVGR 439
Cdd:COG0156  376 LEALAEVGK 384
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 91-438 2.94e-158

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: 450.86  E-value: 2.94e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  91 SGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEA 170
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 171 LLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEA-QKHRLRLVATDGAFSMDGDIAPLQEICCLASR 249
Cdd:cd06454   81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 250 YGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVV 329
Cdd:cd06454  161 YGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAF-GAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 330 GCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGF-TISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVP 408
Cdd:cd06454  240 AAALAALEVLQGGPERRERLQENVRYLRRGLKELGFpVGGSPSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVP 319

                        330       340       350
                 ....*....|....*....|....*....|
gi 530419682 409 KGKARIRVQISAVHSEEDIDRCVEAFVEVG 438
Cdd:cd06454  320 RGTARLRISLSAAHTKEDIDRLLEALKEVG 349
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
91-434 2.07e-59

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 197.91  E-value: 2.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682   91 SGILNFCANNYLGLSShPEVIQAGLQALEefgaglSSVRFICGTQSIHKNLEAKIARFH--------QREDAILYPSCYD 162
Cdd:pfam00155   1 TDKINLGSNEYLGDTL-PAVAKAEKDALA------GGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  163 ANAGLFEALL-TPEDAVLSDELNHASIIDGIRLCKAHKYRYR-------HLDMADLEAKLQEAQKhrlrLVATDGAFSMD 234
Cdd:pfam00155  74 ANIEALIFLLaNPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK----VVLHTSPHNPT 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  235 GDIAPLQEICCLAS---RYGALVFMDECHATGFLGPTGRGTDeLLGVMDQV-TIINSTLGKALG--GASGGYTTGPGPLV 308
Cdd:pfam00155 150 GTVATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPnLLVVGSFSKAFGlaGWRVGYILGNAAVI 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  309 SLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRM 388
Cdd:pfam00155 229 SQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKEL 308

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 530419682  389 ADDMLKR-GIFVIGFSYPVVPkgkARIRVQISAvHSEEDIDRCVEAF 434
Cdd:pfam00155 309 AQVLLEEvGVYVTPGSSPGVP---GWLRITVAG-GTEEELEELLEAI 351
 
Name Accession Description Interval E-value
2am3keto_CoA TIGR01822
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and ...
 27-444 0e+00

glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and bacterial (almost exclusively Proteobacterial) 2-amino-3-ketobutyrate--CoA ligase, now called glycine C-acetyltransferase. This enzyme can act in threonine catabolism. The closest homolog from Bacillus subtilis, and sequences like it, may be functionally equivalent but were not included in the model because of difficulty in finding reports of function. [Energy metabolism, Amino acids and amines]


Pssm-ID: 130881 [Multi-domain]  Cd Length: 393  Bit Score: 717.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682   27 LRGILEGELEGIRGAGTWKSERVITSRQGPHIRV-DGvsggpgtvifpglplphlsccihllsftSGILNFCANNYLGLS 105
Cdd:TIGR01822   1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVaDG----------------------------REVLNFCANNYLGLS 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  106 SHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNH 185
Cdd:TIGR01822  53 SHPDLIQAAKDALDEHGFGMSSVRFICGTQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNH 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  186 ASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKH--RLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATG 263
Cdd:TIGR01822 133 ASIIDGVRLCKAKRYRYANNDMADLEAQLKEARAAgaRHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATG 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  264 FLGPTGRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSN 343
Cdd:TIGR01822 213 FLGPTGRGSHELCGVMGRVDIITGTLGKALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASN 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  344 TIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHS 423
Cdd:TIGR01822 293 ELRDRLWANTRYFRERMEAAGFDIKPADHPIIPVMLYDAVLAQRFARRLLEEGIYVTGFFYPVVPKGQARIRVQISAAHT 372

                         410       420
                  ....*....|....*....|.
gi 530419682  424 EEDIDRCVEAFVEVGRLHGAL 444
Cdd:TIGR01822 373 EEQLDRAVEAFTRIGRELGVI 393
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 31-444 0e+00

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 647.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  31 LEGELEGIRGAGTWKSERVITSRQGPHIRVdgvSGGpgtvifpglplphlsccihllsftSGILNFCANNYLGLSSHPEV 110
Cdd:PRK06939   9 LREELEEIKAEGLYKEERVITSPQGADITV---ADG------------------------KEVINFCANNYLGLANHPEL 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 111 IQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIID 190
Cdd:PRK06939  62 IAAAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIID 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 191 GIRLCKAHKYRYRHLDMADLEAKLQEAQK--HRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPT 268
Cdd:PRK06939 142 GVRLCKAKRYRYANNDMADLEAQLKEAKEagARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGEN 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 269 GRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQS 348
Cdd:PRK06939 222 GRGTVEHFGVMDRVDIITGTLGKALGGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDR 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 349 MAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDID 428
Cdd:PRK06939 302 LWENARYFREGMTAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLD 381

                        410
                 ....*....|....*.
gi 530419682 429 RCVEAFVEVGRLHGAL 444
Cdd:PRK06939 382 RAIDAFEKVGKELGVI 397
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 31-439 0e+00

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: 534.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  31 LEGELEGIRGAGTWKSERVITSRQGPHIRVDGvsggpgtvifpglplphlsccihllsftSGILNFCANNYLGLSSHPEV 110
Cdd:COG0156    5 LEAELAALKAAGLYRYLRVLESPQGPRVTIDG----------------------------REVLNFSSNDYLGLANHPRV 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 111 IQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIID 190
Cdd:COG0156   57 IEAAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIID 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 191 GIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGR 270
Cdd:COG0156  137 GARLSGAKVVRFRHNDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGR 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 271 GTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMA 350
Cdd:COG0156  217 GLVEHFGLEDRVDIIMGTLSKAL-GSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLW 295

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 351 AKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRC 430
Cdd:COG0156  296 ENIAYFREGLKELGFDLGPSESPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRL 375


                 ....*....
gi 530419682 431 VEAFVEVGR 439
Cdd:COG0156  376 LEALAEVGK 384
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 91-438 2.94e-158

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: 450.86  E-value: 2.94e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  91 SGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEA 170
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 171 LLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEA-QKHRLRLVATDGAFSMDGDIAPLQEICCLASR 249
Cdd:cd06454   81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 250 YGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVV 329
Cdd:cd06454  161 YGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAF-GAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 330 GCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGF-TISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVP 408
Cdd:cd06454  240 AAALAALEVLQGGPERRERLQENVRYLRRGLKELGFpVGGSPSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVP 319

                        330       340       350
                 ....*....|....*....|....*....|
gi 530419682 409 KGKARIRVQISAVHSEEDIDRCVEAFVEVG 438
Cdd:cd06454  320 RGTARLRISLSAAHTKEDIDRLLEALKEVG 349
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 93-434 7.48e-131

8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. This model represents 8-amino-7-oxononanoate synthase, the BioF protein of biotin biosynthesis. This model is based on a careful phylogenetic analysis to separate members of this family from 2-amino-3-ketobutyrate and other related pyridoxal phosphate-dependent enzymes. In several species, including Staphylococcus and Coxiella, a candidate 8-amino-7-oxononanoate synthase is confirmed by location in the midst of a biotin biosynthesis operon but scores below the trusted cutoff of this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273303 [Multi-domain]  Cd Length: 360  Bit Score: 381.62  E-value: 7.48e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682   93 ILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALL 172
Cdd:TIGR00858  18 LLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVISALV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  173 TPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGA 252
Cdd:TIGR00858  98 GKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSMDGDIAPLPQLVALAERYGA 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  253 LVFMDECHATGFLGPTGRGTDELLGVM-DQVTIINSTLGKALGGAsGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGC 331
Cdd:TIGR00858 178 WLMVDDAHGTGVLGEDGRGTLEHFGLKpEPVDIQVGTLSKALGSY-GAYVAGSQALIDYLINRARTLIFSTALPPAVAAA 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  332 ASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGK 411
Cdd:TIGR00858 257 ALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQQQGIFVGAIRPPTVPAGT 336

                         330       340
                  ....*....|....*....|...
gi 530419682  412 ARIRVQISAVHSEEDIDRCVEAF 434
Cdd:TIGR00858 337 SRLRLTLSAAHTPGDIDRLAEAL 359
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 31-438 9.38e-118

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 349.46  E-value: 9.38e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  31 LEGELEGIRGAGTWKSERVITSRQGPHIRVDGvsggpgtvifpglplphlsccihllsftSGILNFCANNYLGLSSHPEV 110
Cdd:PRK05958   7 LEAALAQRRAAGLYRSLRPREGGAGRWLVVDG----------------------------RRMLNFASNDYLGLARHPRL 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 111 IQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIID 190
Cdd:PRK05958  59 IAAAQQAARRYGAGSGGSRLVTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLID 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 191 GIRLCKAHKYRYRHLDMADLEAKLQEAQKHRlRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGR 270
Cdd:PRK05958 139 GARLSRARVRRYPHNDVDALEALLAKWRAGR-ALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGR 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 271 GTDELLGV-MDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSM 349
Cdd:PRK05958 218 GLAAEAGLaGEPDVILVGTLGKAL-GSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERL 296

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 350 AAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDR 429
Cdd:PRK05958 297 AALIARLRAGLRALGFQLMDSQSAIQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDR 376


                 ....*....
gi 530419682 430 CVEAFVEVG 438
Cdd:PRK05958 377 LLEALAEAL 385
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 96-439 3.99e-103

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: 312.43  E-value: 3.99e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682   96 FCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDAN-AGLFE-ALLT 173
Cdd:TIGR01821  50 WCSNDYLGMGQHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANdATLATlAKII 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  174 PEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGAL 253
Cdd:TIGR01821 130 PGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGAL 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  254 VFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCAS 333
Cdd:TIGR01821 210 TYLDEVHAVGLYGPRGGGIAERDGLMHRIDIIEGTLAKAF-GVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGAT 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  334 KALDLLMGSNTIVQSMAAKTQRFRSKMEAAGF-TISGASHpICPVMLGDARLASRMADDML-KRGIFVIGFSYPVVPKGK 411
Cdd:TIGR01821 289 ASIRHLKESQDLRRAHQENVKRLKNLLEALGIpVIPNPSH-IVPVIIGDAALCKKVSDLLLnKHGIYVQPINYPTVPRGT 367

                         330       340
                  ....*....|....*....|....*...
gi 530419682  412 ARIRVQISAVHSEEDIDRCVEAFVEVGR 439
Cdd:TIGR01821 368 ERLRITPTPAHTDKMIDDLVEALLLVWD 395
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 96-437 2.55e-91

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 282.51  E-value: 2.55e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  96 FCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEAL--LT 173
Cdd:PRK13392  51 WCSNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLgkLL 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 174 PEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGAL 253
Cdd:PRK13392 131 PGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNAL 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 254 VFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCAS 333
Cdd:PRK13392 211 TYVDEVHAVGLYGARGGGIAERDGLMDRIDMIQGTLAKAF-GCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGAT 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 334 KALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKR-GIFVIGFSYPVVPKGKA 412
Cdd:PRK13392 290 AAIRHLKTSQTERDAHQDRVAALKAKLNANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEhGIYIQPINYPTVPRGTE 369

                        330       340
                 ....*....|....*....|....*
gi 530419682 413 RIRVQISAVHSEEDIDRCVEAFVEV 437
Cdd:PRK13392 370 RLRITPTPLHDDEDIDALVAALVAI 394
PLN02483 PLN02483
serine palmitoyltransferase
 84-442 1.16e-65

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 218.48  E-value: 1.16e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  84 IHLLSFTSGILNFCANNYLGLSSH-----PEVIQAglqaLEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYP 158
Cdd:PLN02483  93 LKRTTKTRRCLNLGSYNYLGFAAAdeyctPRVIES----LKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFG 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 159 SCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEA------QKHRLR---LVATDG 229
Cdd:PLN02483 169 MGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQiaegqpRTHRPWkkiIVIVEG 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 230 AFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGV-MDQVTIINSTLGKALgGASGGYTTGPGPLV 308
Cdd:PLN02483 249 IYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVdPADVDIMMGTFTKSF-GSCGGYIAGSKELI 327

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 309 SLLRQRARPYLFSNSLPPAVVGCASKALDLLM---GSNTIVQSMAA---KTQRFRSKMEAAGFTISGAS-HPICPVML-G 380
Cdd:PLN02483 328 QYLKRTCPAHLYATSMSPPAVQQVISAIKVILgedGTNRGAQKLAQireNSNFFRSELQKMGFEVLGDNdSPVMPIMLyN 407

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530419682 381 DARLA--SRmadDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHG 442
Cdd:PLN02483 408 PAKIPafSR---ECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVG 468
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 93-434 1.61e-59

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 201.83  E-value: 1.61e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  93 ILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEAL- 171
Cdd:PLN02955 104 LLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVAIg 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 172 ------------LTPED-AVLSDELNHASIIDGIRLCK----AHKYRYRHLDMADLEAKLQEAQKHRlRLVATDGAFSMD 234
Cdd:PLN02955 184 svasllaasgkpLKNEKvAIFSDALNHASIIDGVRLAErqgnVEVFVYRHCDMYHLNSLLSSCKMKR-KVVVTDSLFSMD 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 235 GDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKAlGGASGGYTTGPGPLVSLLRQR 314
Cdd:PLN02955 263 GDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKA-AGCHGGFIACSKKWKQLIQSR 341

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 315 ARPYLFSNSLPPAVVGCASKAldLLMGSNTIVQSMAAkTQRFRSKMEAAGFTISGashPICPVMLGDARLASRMADDMLK 394
Cdd:PLN02955 342 GRSFIFSTAIPVPMAAAAYAA--VVVARKEKWRRKAI-WERVKEFKALSGVDISS---PIISLVVGNQEKALKASRYLLK 415

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 530419682 395 RGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAF 434
Cdd:PLN02955 416 SGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITAL 455
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
91-434 2.07e-59

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 197.91  E-value: 2.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682   91 SGILNFCANNYLGLSShPEVIQAGLQALEefgaglSSVRFICGTQSIHKNLEAKIARFH--------QREDAILYPSCYD 162
Cdd:pfam00155   1 TDKINLGSNEYLGDTL-PAVAKAEKDALA------GGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  163 ANAGLFEALL-TPEDAVLSDELNHASIIDGIRLCKAHKYRYR-------HLDMADLEAKLQEAQKhrlrLVATDGAFSMD 234
Cdd:pfam00155  74 ANIEALIFLLaNPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK----VVLHTSPHNPT 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  235 GDIAPLQEICCLAS---RYGALVFMDECHATGFLGPTGRGTDeLLGVMDQV-TIINSTLGKALG--GASGGYTTGPGPLV 308
Cdd:pfam00155 150 GTVATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPnLLVVGSFSKAFGlaGWRVGYILGNAAVI 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  309 SLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRM 388
Cdd:pfam00155 229 SQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKEL 308

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 530419682  389 ADDMLKR-GIFVIGFSYPVVPkgkARIRVQISAvHSEEDIDRCVEAF 434
Cdd:pfam00155 309 AQVLLEEvGVYVTPGSSPGVP---GWLRITVAG-GTEEELEELLEAI 351
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
47-437 2.90e-51

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 178.28  E-value: 2.90e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  47 ERVITSRQGPHIrVDGVSGGPGTVIFPGlplphlsccihllsftsgilnfcaNNYLGLSSHPEVIQAGLQALEEFGAGL- 125
Cdd:PRK07179  35 ERVNKNWNGKHL-VLGKTPGPDAIILQS------------------------NDYLNLSGHPDIIKAQIAALQEEGDSLv 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 126 -SSVrFICGTQSIHKnLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRH 204
Cdd:PRK07179  90 mSAV-FLHDDSPKPQ-FEKKLAAFTGFESCLLCQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRH 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 205 LDMADLEAKLQEaqkHRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTI 284
Cdd:PRK07179 168 NDVDHLRRQIER---HGPGIIVVDSVYSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHF 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 285 INSTLGKALGGaSGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAG 364
Cdd:PRK07179 245 ITASLAKAFAG-RAGIITCPRELAEYVPFVSYPAIFSSTLLPHEIAGLEATLEVIESADDRRARLHANARFLREGLSELG 323

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530419682 365 FTISGASHpICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDR----CVEAFVEV 437
Cdd:PRK07179 324 YNIRSESQ-IIALETGSERNTEVLRDALEERNVFGAVFCAPATPKNRNLIRLSLNADLTASDLDRvlevCREARDEV 399
PLN02822 PLN02822
serine palmitoyltransferase
 49-437 2.65e-50

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 177.24  E-value: 2.65e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  49 VITSRQGPHIRVDGvsggpgtvifpglplphlsccihllsftSGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSV 128
Cdd:PLN02822  95 VLESAAGPHTIING----------------------------KDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGP 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 129 RFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMA 208
Cdd:PLN02822 147 RGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDME 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 209 DLEAKLQE-------AQKHRlRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGV-MD 280
Cdd:PLN02822 227 SLRNTLEKltaenkrKKKLR-RYIVVEAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVpIE 305

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 281 QVTIINSTLGKALGGAsGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIV----QSMAAKTQRF 356
Cdd:PLN02822 306 KIDIITAAMGHALATE-GGFCTGSARVVDHQRLSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLaklkENIALLHKGL 384

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 357 RSKMEaagftISGASHPICPVML-----------GDARLASRMADDMLKR-GIFVIGFSYPVVPKGK--ARIRVQISAVH 422
Cdd:PLN02822 385 SDIPG-----LSIGSNTLSPIVFlhlekstgsakEDLSLLEHIADRMLKEdSVLVVVSKRSTLDKCRlpVGIRLFVSAGH 459

                        410
                 ....*....|....*
gi 530419682 423 SEEDIDRCVEAFVEV 437
Cdd:PLN02822 460 TESDILKASESLKRV 474
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 94-433 9.50e-43

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 155.06  E-value: 9.50e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  94 LNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLT 173
Cdd:PLN03227   1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 174 PEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADL----------EAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEI 243
Cdd:PLN03227  81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLrrvleqvraqDVALKRKPTDQRRFLVVEGLYKNTGTLAPLKEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 244 CCLASRYGALVFMDECHATGFLGPTGRGTDELLGV--MDQVTIINSTLGKALGGAsGGYTTGPGPLVSLLRQRARPYLFS 321
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLkpMVHAEIVTFSLENAFGSV-GGMTVGSEEVVDHQRLSGSGYCFS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 322 NSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRS-----------KMEAAGFTISGASHPICPVMLGDAR------- 383
Cdd:PLN03227 240 ASAPPFLAKADATATAGELAGPQLLNRLHDSIANLYStltnsshpyalKLRNRLVITSDPISPIIYLRLSDQEatrrtde 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530419682 384 --LASRMADDMLKRGIFVI--GFSYPVVPKGKAR--IRVQISAVHSEEDIDRCVEA 433
Cdd:PLN03227 320 tlILDQIAHHSLSEGVAVVstGGHVKKFLQLVPPpcLRVVANASHTREDIDKLLTV 375
PRK07505 PRK07505
hypothetical protein; Provisional
 93-443 4.26e-42

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 153.60  E-value: 4.26e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  93 ILNFCANNYLGLSSHPEVIQAGLQALEEFGA-GLSSVRFICGTQsIHKNLEAKIARFHQREdAILYPSCYDANAGLFEAL 171
Cdd:PRK07505  48 FVNFVSCSYLGLDTHPAIIEGAVDALKRTGSlHLSSSRTRVRSQ-ILKDLEEALSELFGAS-VLTFTSCSAAHLGILPLL 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 172 ----LTPEDAVLS--DELNHASIIDGIRLCkAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMdGDIAPLQEICC 245
Cdd:PRK07505 126 asghLTGGVPPHMvfDKNAHASLNILKGIC-ADETEVETIDHNDLDALEDICKTNKTVAYVADGVYSM-GGIAPVKELLR 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 246 LASRYGALVFMDECHATGFLGPTGRG--TDELLGVMDQVTIINSTLGKALGGASGGYTTGPGPLVSLLRQRARPYLFSNS 323
Cdd:PRK07505 204 LQEKYGLFLYIDDAHGLSIYGKNGEGyvRSELDYRLNERTIIAASLGKAFGASGGVIMLGDAEQIELILRYAGPLAFSQS 283

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 324 LPPAVVGCASKALDL-LMGSNTIVQ-SMAAKTQRFRSKMEAagfTISGASHPICPVMLGDARLASRMADDMLKRGIFVIG 401
Cdd:PRK07505 284 LNVAALGAILASAEIhLSEELDQLQqKLQNNIALFDSLIPT---EQSGSFLPIRLIYIGDEDTAIKAAKQLLDRGFYTSP 360

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 530419682 402 FSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGA 443
Cdd:PRK07505 361 VFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLKEILDEGLA 402
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 90-428 4.23e-24

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 102.94  E-value: 4.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  90 TSGILNFCANNYLGLSSHPEV---IQAGLQAL------EEFGAGLSsvRFICGTQSIHKNLEAKIARFHQREDAILYPSC 160
Cdd:PRK05937   3 ESLSIDFVTNDFLGFSRSDTLvheVEKRYRLYcrqfphAQLGYGGS--RAILGPSSLLDDLEHKIAHFHGAPEAFIVPSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 161 YDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLR--LVATDGAFSMDGDIA 238
Cdd:PRK05937  81 YMANLGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQRSFGriFIFVCSVYSFKGTLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 239 PLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGvMDQVTIINSTLGKALGgasggyTTGPGPLVSL-----LRQ 313
Cdd:PRK05937 161 PLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLG-YENFYAVLVTYSKALG------SMGAALLSSSevkqdLML 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 314 RARPYLFSNSLPPAVVGCASKALDLLMGSNTIvqsmaAKTQRFRSKMEAAGFTISGASHPICPVMLGDarLASRMADDML 393
Cdd:PRK05937 234 NSPPLRYSTGLPPHLLISIQVAYDFLSQEGEL-----ARKQLFRLKEYFAQKFSSAAPGCVQPIFLPG--ISEQELYSKL 306

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 530419682 394 KRGIFVIGFsypVVPKGKARIRVQISAVHSEEDID 428
Cdd:PRK05937 307 VETGIRVGV---VCFPTGPFLRVNLHAFNTEDEVD 338
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 138-303 2.68e-16

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: 76.27  E-value: 2.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 138 HKNLEAKIARFHQ--REDAILYPSCYDANAGLFEALLTPEDAVLSDELNHAS---IIDGIRLCKAHKYRYRHLDMADLEA 212
Cdd:cd01494    2 LEELEEKLARLLQpgNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrywVAAELAGAKPVPVPVDDAGYGGLDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 213 KLQEAQKHRLR--LVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGflgptGRGTDELLGVMDQVTIINSTLG 290
Cdd:cd01494   82 AILEELKAKPNvaLIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGG-----ASPAPGVLIPEGGADVVTFSLH 156

                        170
                 ....*....|...
gi 530419682 291 KALGGASGGYTTG 303
Cdd:cd01494  157 KNLGGEGGGVVIV 169
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 141-436 1.00e-10

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate 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. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 62.74  E-value: 1.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 141 LEAKIARFHQR--------EDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAhKYRYRHLD----MA 208
Cdd:cd00609   41 LREAIAEWLGRrggvdvppEEIVVTNGAQEALSLLLRALLNPGDEVLVPDPTYPGYEAAARLAGA-EVVPVPLDeeggFL 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 209 DLEAKLQEAQKHRLRLVA-------TDGAFSMDGdiapLQEICCLASRYGALVFMDECHatGFLGPTGRGTDELLGV-MD 280
Cdd:cd00609  120 LDLELLEAAKTPKTKLLYlnnpnnpTGAVLSEEE----LEELAELAKKHGILIISDEAY--AELVYDGEPPPALALLdAY 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 281 QVTIINSTLGKALGGAS--GGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCAsKALDLLMGS-NTIVQSMAAKTQRFR 357
Cdd:cd00609  194 ERVIVLRSFSKTFGLPGlrIGYLIAPPEELLERLKKLLPYTTSGPSTLSQAAAA-AALDDGEEHlEELRERYRRRRDALL 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 358 SKMEAAGFTI----SGASHpicpVMLG-----DARLASRMAddmLKRGIFVIGFSYPvVPKGKARIRvqISAVHSEEDID 428
Cdd:cd00609  273 EALKELGPLVvvkpSGGFF----LWLDlpegdDEEFLERLL---LEAGVVVRPGSAF-GEGGEGFVR--LSFATPEEELE 342


                 ....*...
gi 530419682 429 RCVEAFVE 436
Cdd:cd00609  343 EALERLAE 350
OAT_like cd00610
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP) ...
 102-437 1.05e-10

Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to ornithine aminotransferase, acetylornithine aminotransferase, alanine-glyoxylate aminotransferase, dialkylglycine decarboxylase, 4-aminobutyrate aminotransferase, beta-alanine-pyruvate aminotransferase, adenosylmethionine-8-amino-7-oxononanoate aminotransferase, and glutamate-1-semialdehyde 2,1-aminomutase. All the enzymes belonging to this family act on basic amino acids and their derivatives are involved in transamination or decarboxylation.


Pssm-ID: 99735 [Multi-domain]  Cd Length: 413  Bit Score: 63.36  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 102 LGLSSHPEVIQAGLQALEEFGAGLSSVRF-ICGTQSIhknlEA--KIARFHQREDAILypSCYDANAG-LFEAL-LTPED 176
Cdd:cd00610   73 LGFFYNEPAVELAELLLALTPEGLDKVFFvNSGTEAV----EAalKLARAYTGRKKII--SFEGAYHGrTLGALsLTGSK 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 177 A---VLSDELNHASIIDGirlckAHKYRYRHLDMADLEAkLQEAQKHRLRLVAtdgAFSMD------GDIAP----LQEI 243
Cdd:cd00610  147 KyrgGFGPLLPGVLHVPY-----PYRYRPPAELADDLEA-LEEALEEHPEEVA---AVIVEpiqgegGVIVPppgyLKAL 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 244 CCLASRYGALVFMDEChATGFlGPTGR-GTDELLGVM-DqvtIInsTLGKALGGAS--GGYTTGPGPLVSLlrqRARPYL 319
Cdd:cd00610  218 RELCRKHGILLIADEV-QTGF-GRTGKmFAFEHFGVEpD---IV--TLGKGLGGGLplGAVLGREEIMDAF---PAGPGL 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 320 FSNSL---PpavVGCA--SKALDLLMgSNTIVQSMAAKTQRFRSKMEAAgftisgASHPICPV-------MLG------- 380
Cdd:cd00610  288 HGGTFggnP---LACAaaLAVLEVLE-EEGLLENAAELGEYLRERLREL------AEKHPLVGdvrgrglMIGielvkdr 357

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530419682 381 -----DARLASRMADDMLKRGIFVIgfsypvvPKGKARIRVQISAVHSEEDIDRCVEAFVEV 437
Cdd:cd00610  358 atkppDKELAAKIIKAALERGLLLR-------PSGGNVIRLLPPLIITEEEIDEGLDALDEA 412
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
170-263 9.24e-06

Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 47.44  E-value: 9.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682 170 ALLTPEDAVLSDELNHASIIDGIR-LCKAHKYRYR--------HLDMADLEAKLQEaqkhRLRLVATDGAFSMDGDIAPL 240
Cdd:COG0520   98 GRLKPGDEILITEMEHHSNIVPWQeLAERTGAEVRvipldedgELDLEALEALLTP----RTKLVAVTHVSNVTGTVNPV 173

                         90       100
                 ....*....|....*....|...
gi 530419682 241 QEICCLASRYGALVFMDECHATG 263
Cdd:COG0520  174 KEIAALAHAHGALVLVDGAQSVP 196
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 172-429 1.30e-05

Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 47.24  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  172 LTPEDAVLSDELNHASIIDGI-RLCKAHKYRYR--------HLDMADLEAKLqeaqKHRLRLVATDGAFSMDGDIAPLQE 242
Cdd:pfam00266  85 LKPGDEIVITEMEHHANLVPWqELAKRTGARVRvlpldedgLLDLDELEKLI----TPKTKLVAITHVSNVTGTIQPVPE 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  243 ICCLASRYGALVFMDECHATG--------------------FLGPTGRG----TDELLGVMDqvtiinstlgKALGGasG 298
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGhrpidvqklgvdflafsghkLYGPTGIGvlygRRDLLEKMP----------PLLGG--G 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419682  299 GYTTGPGplVSLLRQRARPYLFSNSLPP--AVVGCAsKALDLLM--GSNTIVQSMAAKTQRFRSKMEAAGFTisgashpi 374
Cdd:pfam00266 229 GMIETVS--LQESTFADAPWKFEAGTPNiaGIIGLG-AALEYLSeiGLEAIEKHEHELAQYLYERLLSLPGI-------- 297

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530419682  375 cpVMLGDARLASRM---------ADDML---KRGIFVIGFSYPVVPKGKAR-----IRVQISAVHSEEDIDR 429
Cdd:pfam00266 298 --RLYGPERRASIIsfnfkgvhpHDVATlldESGIAVRSGHHCAQPLMVRLglggtVRASFYIYNTQEDVDR 367
 
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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