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Conserved domains on  [gi|1209969496|ref|XP_021389342|]
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5-aminolevulinate synthase, nonspecific, mitochondrial [Lonchura striata]

Protein Classification

Preseq_ALAS and KBL_like domain-containing protein( domain architecture ID 11181659)

Preseq_ALAS and KBL_like domain-containing protein

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) ...
 191-596 0e+00

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 TIGR01821:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 402  Bit Score: 637.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 191 FQYDQFFEKKIDEKKKDHTYRVFKTVNRKAQIFPMADDYTDSliTKKEVSVWCSNDYLGMSRHPRVCGAVMETLKQHGAG 270
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 271 AGGTRNISGTSKFHVDLEKELADLHGKDAALLFSSCFVANDSTLFTLAKMLPGCEIYSDSGNHASMIQGICNSRVPKHIF 350
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 351 RHNDVNHLRELLKKSDPSTPKIVAFETVHSMDGAVCPLEELCDVAHEHGAITFVDEVHAVGLYGARGGGIGDRDGVMHKM 430
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 431 DIISGTLGKAFGCVGGYISSTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRTLKsaEGQALRRQHQRNVKLMRQMLM 510
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLK--ESQDLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 511 DAGLPVVHCPSHIIPVRVADAAKNTEICDKLMSQHSIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSYFIEKLLATWKD 590
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 1209969496 591 VGLELK 596
Cdd:TIGR01821 397 LGLPLS 402
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 2-130 6.23e-49

5-aminolevulinate synthase presequence; The N terminal presequence domain found in 5-aminolevulinate synthase exists as an amphipathic helix, with a positively charged surface provided by lysine residues and no stable helix at the N-terminus. The domain is essential for the import process by which ALAS is transported into the mitochondria: translocase of the outer membrane (Tom) and translocase of the inner membrane protein complexes appear responsible for recognition and import through the mitochondrial membrane. The protein Tom20 is anchored to the mitochondrial outer membrane, and its interaction with presequences is thought to be the recognition step which allows subsequent import.


:

Pssm-ID: 462658  Cd Length: 114  Bit Score: 166.13  E-value: 6.23e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496   2 EAVVRRCPFLARVSQAFLQKAGPSLLLYAQHCPRMMeaappaARALATSAARGQQA-EEESPAGREAKNVKEvaqqnadg 80
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM------TRALSTSSANLQGEkEETPVAGPTAKQAKA-------- 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1209969496  81 tqLPAGHPPASASQSTATKCPFLAAQMNHKKSNVFCKASLELQEDVQEVQ 130
Cdd:pfam09029  67 --LPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
 
Name Accession Description Interval E-value
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 191-596 0e+00

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: 637.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 191 FQYDQFFEKKIDEKKKDHTYRVFKTVNRKAQIFPMADDYTDSliTKKEVSVWCSNDYLGMSRHPRVCGAVMETLKQHGAG 270
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 271 AGGTRNISGTSKFHVDLEKELADLHGKDAALLFSSCFVANDSTLFTLAKMLPGCEIYSDSGNHASMIQGICNSRVPKHIF 350
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 351 RHNDVNHLRELLKKSDPSTPKIVAFETVHSMDGAVCPLEELCDVAHEHGAITFVDEVHAVGLYGARGGGIGDRDGVMHKM 430
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 431 DIISGTLGKAFGCVGGYISSTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRTLKsaEGQALRRQHQRNVKLMRQMLM 510
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLK--ESQDLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 511 DAGLPVVHCPSHIIPVRVADAAKNTEICDKLMSQHSIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSYFIEKLLATWKD 590
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 1209969496 591 VGLELK 596
Cdd:TIGR01821 397 LGLPLS 402
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 237-588 1.13e-175

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: 502.48  E-value: 1.13e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 237 KEVSVWCSNDYLGMSRHPRVCGAVMETLKQHGAGAGGTRNISGTSKFHVDLEKELADLHGKDAALLFSSCFVANDSTLFT 316
Cdd:cd06454     1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 317 LakMLPGCEIYSDSGNHASMIQGICNSRVPKHIFRHNDVNHLRELLKKSD-PSTPKIVAFETVHSMDGAVCPLEELCDVA 395
Cdd:cd06454    81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 396 HEHGAITFVDEVHAVGLYGARGGGIGDRDGVMHKMDIISGTLGKAFGCVGGYISSTSSLIDTVRSYAAGFIFTTSLPPML 475
Cdd:cd06454   159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 476 LAGALESVRTLKSaeGQALRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVAD-AAKNTEICDKLMsQHSIYVQAINY 554
Cdd:cd06454   239 AAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDdPAKAVAFSDALL-ERGIYVQAIRY 315

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1209969496 555 PTVPRGEELLRIAPTPHHTPQMMSYFIEKLLATW 588
Cdd:cd06454   316 PTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 191-602 1.31e-167

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 484.36  E-value: 1.31e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 191 FQYDQFFEKKIDEKKKDHTYRVFKTVNRKAQIFPMADDYTDSliTKKEVSVWCSNDYLGMSRHPRVCGAVMETLKQHGAG 270
Cdd:PRK13392    2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGPD--GPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 271 AGGTRNISGTSKFHVDLEKELADLHGKDAALLFSSCFVANDSTLFTLAKMLPGCEIYSDSGNHASMIQGICNSRVPKHIF 350
Cdd:PRK13392   80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 351 RHNDVNHLRELLKKSDPSTPKIVAFETVHSMDGAVCPLEELCDVAHEHGAITFVDEVHAVGLYGARGGGIGDRDGVMHKM 430
Cdd:PRK13392  160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 431 DIISGTLGKAFGCVGGYISSTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRTLKsaEGQALRRQHQRNVKLMRQMLM 510
Cdd:PRK13392  240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLK--TSQTERDAHQDRVAALKAKLN 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 511 DAGLPVVHCPSHIIPVRVADAAKNTEICDKLMSQHSIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSYFIEKLLATWKD 590
Cdd:PRK13392  318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397

                         410
                  ....*....|..
gi 1209969496 591 VGLELKPHSSAE 602
Cdd:PRK13392  398 LELPRWREAAQA 409
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 193-590 2.61e-152

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: 444.49  E-value: 2.61e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 193 YDQFFEKKIDEKKKDHTYRVFKTVNRKAQIFPMADDytdslitkKEVSVWCSNDYLGMSRHPRVCGAVMETLKQHGAGAG 272
Cdd:COG0156     1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDG--------REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 273 GTRNISGTSKFHVDLEKELADLHGKDAALLFSSCFVANDSTLFTLAKmlPGCEIYSDSGNHASMIQGICNSRVPKHIFRH 352
Cdd:COG0156    73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 353 NDVNHLRELLKKSDPSTPKIVAFETVHSMDGAVCPLEELCDVAHEHGAITFVDEVHAVGLYGARGGGIGDRDGVMHKMDI 432
Cdd:COG0156   151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDI 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 433 ISGTLGKAFGCVGGYISSTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRTLKsaEGQALRRQHQRNVKLMRQMLMDA 512
Cdd:COG0156   231 IMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILR--EEPELRERLWENIAYFREGLKEL 308

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1209969496 513 GLPVVHCPSHIIPVRVADAAKNTEICDKLMsQHSIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSYFIEKLLATWKD 590
Cdd:COG0156   309 GFDLGPSESPIVPVIVGDAERALALADALL-ERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
242-584 6.96e-71

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 232.97  E-value: 6.96e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 242 WCSNDYLGMsrhprVCGAVMETLKQhgAGAGGTRNISGTSKFHVDLEKELADLHG--------KDAALLFSSCFVANDST 313
Cdd:pfam00155   6 LGSNEYLGD-----TLPAVAKAEKD--ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGANIEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 314 LFTLAKMlPGCEIYSDSGNHASMIQGICNSRVPKHIFR-------HNDVNHLRELLKKSdpstPKIVAFETVHSMDGAVC 386
Cdd:pfam00155  79 LIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNPTGTVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 387 PLEELCDVA---HEHGAITFVDEVHAVGLYGARGGGIGDRDGVMHKMDIISGTLGKAFGCVG---GYISSTSSLIDTVRS 460
Cdd:pfam00155 154 TLEELEKLLdlaKEHNILLLVDEAYAGFVFGSPDAVATRALLAEGPNLLVVGSFSKAFGLAGwrvGYILGNAAVISQLRK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 461 YAAGFIFTTSLPPMLLAGALESvrTLKSAEGQALRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKNTEICDK 540
Cdd:pfam00155 234 LARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQV 311

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1209969496 541 LMSQHSIYVQAINYPTVPrgeELLRIAPTpHHTPQMMSYFIEKL 584
Cdd:pfam00155 312 LLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLEAI 351
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 2-130 6.23e-49

5-aminolevulinate synthase presequence; The N terminal presequence domain found in 5-aminolevulinate synthase exists as an amphipathic helix, with a positively charged surface provided by lysine residues and no stable helix at the N-terminus. The domain is essential for the import process by which ALAS is transported into the mitochondria: translocase of the outer membrane (Tom) and translocase of the inner membrane protein complexes appear responsible for recognition and import through the mitochondrial membrane. The protein Tom20 is anchored to the mitochondrial outer membrane, and its interaction with presequences is thought to be the recognition step which allows subsequent import.


Pssm-ID: 462658  Cd Length: 114  Bit Score: 166.13  E-value: 6.23e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496   2 EAVVRRCPFLARVSQAFLQKAGPSLLLYAQHCPRMMeaappaARALATSAARGQQA-EEESPAGREAKNVKEvaqqnadg 80
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM------TRALSTSSANLQGEkEETPVAGPTAKQAKA-------- 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1209969496  81 tqLPAGHPPASASQSTATKCPFLAAQMNHKKSNVFCKASLELQEDVQEVQ 130
Cdd:pfam09029  67 --LPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
 
Name Accession Description Interval E-value
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 191-596 0e+00

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: 637.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 191 FQYDQFFEKKIDEKKKDHTYRVFKTVNRKAQIFPMADDYTDSliTKKEVSVWCSNDYLGMSRHPRVCGAVMETLKQHGAG 270
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 271 AGGTRNISGTSKFHVDLEKELADLHGKDAALLFSSCFVANDSTLFTLAKMLPGCEIYSDSGNHASMIQGICNSRVPKHIF 350
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 351 RHNDVNHLRELLKKSDPSTPKIVAFETVHSMDGAVCPLEELCDVAHEHGAITFVDEVHAVGLYGARGGGIGDRDGVMHKM 430
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 431 DIISGTLGKAFGCVGGYISSTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRTLKsaEGQALRRQHQRNVKLMRQMLM 510
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLK--ESQDLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 511 DAGLPVVHCPSHIIPVRVADAAKNTEICDKLMSQHSIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSYFIEKLLATWKD 590
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 1209969496 591 VGLELK 596
Cdd:TIGR01821 397 LGLPLS 402
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 237-588 1.13e-175

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: 502.48  E-value: 1.13e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 237 KEVSVWCSNDYLGMSRHPRVCGAVMETLKQHGAGAGGTRNISGTSKFHVDLEKELADLHGKDAALLFSSCFVANDSTLFT 316
Cdd:cd06454     1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 317 LakMLPGCEIYSDSGNHASMIQGICNSRVPKHIFRHNDVNHLRELLKKSD-PSTPKIVAFETVHSMDGAVCPLEELCDVA 395
Cdd:cd06454    81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 396 HEHGAITFVDEVHAVGLYGARGGGIGDRDGVMHKMDIISGTLGKAFGCVGGYISSTSSLIDTVRSYAAGFIFTTSLPPML 475
Cdd:cd06454   159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 476 LAGALESVRTLKSaeGQALRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVAD-AAKNTEICDKLMsQHSIYVQAINY 554
Cdd:cd06454   239 AAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDdPAKAVAFSDALL-ERGIYVQAIRY 315

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1209969496 555 PTVPRGEELLRIAPTPHHTPQMMSYFIEKLLATW 588
Cdd:cd06454   316 PTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 191-602 1.31e-167

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 484.36  E-value: 1.31e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 191 FQYDQFFEKKIDEKKKDHTYRVFKTVNRKAQIFPMADDYTDSliTKKEVSVWCSNDYLGMSRHPRVCGAVMETLKQHGAG 270
Cdd:PRK13392    2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGPD--GPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 271 AGGTRNISGTSKFHVDLEKELADLHGKDAALLFSSCFVANDSTLFTLAKMLPGCEIYSDSGNHASMIQGICNSRVPKHIF 350
Cdd:PRK13392   80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 351 RHNDVNHLRELLKKSDPSTPKIVAFETVHSMDGAVCPLEELCDVAHEHGAITFVDEVHAVGLYGARGGGIGDRDGVMHKM 430
Cdd:PRK13392  160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 431 DIISGTLGKAFGCVGGYISSTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRTLKsaEGQALRRQHQRNVKLMRQMLM 510
Cdd:PRK13392  240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLK--TSQTERDAHQDRVAALKAKLN 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 511 DAGLPVVHCPSHIIPVRVADAAKNTEICDKLMSQHSIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSYFIEKLLATWKD 590
Cdd:PRK13392  318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397

                         410
                  ....*....|..
gi 1209969496 591 VGLELKPHSSAE 602
Cdd:PRK13392  398 LELPRWREAAQA 409
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 193-590 2.61e-152

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: 444.49  E-value: 2.61e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 193 YDQFFEKKIDEKKKDHTYRVFKTVNRKAQIFPMADDytdslitkKEVSVWCSNDYLGMSRHPRVCGAVMETLKQHGAGAG 272
Cdd:COG0156     1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDG--------REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 273 GTRNISGTSKFHVDLEKELADLHGKDAALLFSSCFVANDSTLFTLAKmlPGCEIYSDSGNHASMIQGICNSRVPKHIFRH 352
Cdd:COG0156    73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 353 NDVNHLRELLKKSDPSTPKIVAFETVHSMDGAVCPLEELCDVAHEHGAITFVDEVHAVGLYGARGGGIGDRDGVMHKMDI 432
Cdd:COG0156   151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDI 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 433 ISGTLGKAFGCVGGYISSTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRTLKsaEGQALRRQHQRNVKLMRQMLMDA 512
Cdd:COG0156   231 IMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILR--EEPELRERLWENIAYFREGLKEL 308

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1209969496 513 GLPVVHCPSHIIPVRVADAAKNTEICDKLMsQHSIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSYFIEKLLATWKD 590
Cdd:COG0156   309 GFDLGPSESPIVPVIVGDAERALALADALL-ERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 237-584 3.60e-93

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: 291.48  E-value: 3.60e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 237 KEVSVWCSNDYLGMSRHPRVCGAVMETLKQHGAGAGGTRNISGTSKFHVDLEKELADLHGKDAALLFSSCFVANDSTLFT 316
Cdd:TIGR00858  16 RRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVISA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 317 LAKmlPGCEIYSDSGNHASMIQGICNSRVPKHIFRHNDVNHLRELLKKSDPSTPKIVAFETVHSMDGAVCPLEELCDVAH 396
Cdd:TIGR00858  96 LVG--KGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSMDGDIAPLPQLVALAE 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 397 EHGAITFVDEVHAVGLYGARGGGIGDRDGVMHKMDIIS-GTLGKAFGCVGGYISSTSSLIDTVRSYAAGFIFTTSLPPML 475
Cdd:TIGR00858 174 RYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDIQvGTLSKALGSYGAYVAGSQALIDYLINRARTLIFSTALPPAV 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 476 LAGALESVRTLksaEGQALRRQH-QRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKNTEICDKLMSQhSIYVQAINY 554
Cdd:TIGR00858 254 AAAALAALELI---QEEPWRREKlLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQQQ-GIFVGAIRP 329

                         330       340       350
                  ....*....|....*....|....*....|
gi 1209969496 555 PTVPRGEELLRIAPTPHHTPQMMSYFIEKL 584
Cdd:TIGR00858 330 PTVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 243-592 1.78e-91

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 288.21  E-value: 1.78e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 243 CSNDYLGMSRHPRVCGAVMETLKQHGAGAGGTRNISGTSKFHVDLEKELADLHGKDAALLFSSCFVANDSTLFTLAKmlP 322
Cdd:PRK05958   45 ASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAG--K 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 323 GCEIYSDSGNHASMIQGICNSRVPKHIFRHNDVNHLRELLKKSDPStPKIVAFETVHSMDGAVCPLEELCDVAHEHGAIT 402
Cdd:PRK05958  123 GDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAKWRAG-RALIVTESVFSMDGDLAPLAELVALARRHGAWL 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 403 FVDEVHAVGLYGARGG-GIGDRDGVMHKMDIISGTLGKAFGCVGGYISSTSSLIDTVRSYAAGFIFTTSLPPMLLAGALE 481
Cdd:PRK05958  202 LVDEAHGTGVLGPQGRgLAAEAGLAGEPDVILVGTLGKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARA 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 482 SVRTLKSAEGqalRRQH-QRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKNTEICDKLmSQHSIYVQAINYPTVPRG 560
Cdd:PRK05958  282 ALRILRREPE---RRERlAALIARLRAGLRALGFQLMDSQSAIQPLIVGDNERALALAAAL-QEQGFWVGAIRPPTVPAG 357

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1209969496 561 EELLRIAPTPHHTPQMmsyfIEKLLATWKDVG 592
Cdd:PRK05958  358 TSRLRITLTAAHTEAD----IDRLLEALAEAL 385
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 237-596 2.35e-87

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 277.85  E-value: 2.35e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 237 KEVSVWCSNDYLGMSRHPRVCGAVMETLKQHGAGAGGTRNISGTSKFHVDLEKELADLHGKDAALLFSSCFVANDSTLFT 316
Cdd:PRK06939   42 KEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFET 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 317 LakMLPGCEIYSDSGNHASMIQGICNSRVPKHIFRHNDVNHLRELLKKSDPSTP--KIVAFETVHSMDGAVCPLEELCDV 394
Cdd:PRK06939  122 L--LGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKEAKEAGArhKLIATDGVFSMDGDIAPLPEICDL 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 395 AHEHGAITFVDEVHAVGLYGARGGGIGDRDGVMHKMDIISGTLGKAF-GCVGGYISSTSSLIDTVRSYAAGFIFTTSLPP 473
Cdd:PRK06939  200 ADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAP 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 474 MLLAGALESVRTLKsaEGQALRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKNTEICDKLMsQHSIYVQAIN 553
Cdd:PRK06939  280 AIVAASIKVLELLE--ESDELRDRLWENARYFREGMTAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLL-EEGVYVIGFS 356

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1209969496 554 YPTVPRGEELLRIAPTPHHTPQMmsyfIEKLLATWKDVGLELK 596
Cdd:PRK06939  357 FPVVPKGQARIRTQMSAAHTKEQ----LDRAIDAFEKVGKELG 395
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
242-584 6.96e-71

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 232.97  E-value: 6.96e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 242 WCSNDYLGMsrhprVCGAVMETLKQhgAGAGGTRNISGTSKFHVDLEKELADLHG--------KDAALLFSSCFVANDST 313
Cdd:pfam00155   6 LGSNEYLGD-----TLPAVAKAEKD--ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGANIEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 314 LFTLAKMlPGCEIYSDSGNHASMIQGICNSRVPKHIFR-------HNDVNHLRELLKKSdpstPKIVAFETVHSMDGAVC 386
Cdd:pfam00155  79 LIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNPTGTVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 387 PLEELCDVA---HEHGAITFVDEVHAVGLYGARGGGIGDRDGVMHKMDIISGTLGKAFGCVG---GYISSTSSLIDTVRS 460
Cdd:pfam00155 154 TLEELEKLLdlaKEHNILLLVDEAYAGFVFGSPDAVATRALLAEGPNLLVVGSFSKAFGLAGwrvGYILGNAAVISQLRK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 461 YAAGFIFTTSLPPMLLAGALESvrTLKSAEGQALRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKNTEICDK 540
Cdd:pfam00155 234 LARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQV 311

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1209969496 541 LMSQHSIYVQAINYPTVPrgeELLRIAPTpHHTPQMMSYFIEKL 584
Cdd:pfam00155 312 LLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLEAI 351
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 2-130 6.23e-49

5-aminolevulinate synthase presequence; The N terminal presequence domain found in 5-aminolevulinate synthase exists as an amphipathic helix, with a positively charged surface provided by lysine residues and no stable helix at the N-terminus. The domain is essential for the import process by which ALAS is transported into the mitochondria: translocase of the outer membrane (Tom) and translocase of the inner membrane protein complexes appear responsible for recognition and import through the mitochondrial membrane. The protein Tom20 is anchored to the mitochondrial outer membrane, and its interaction with presequences is thought to be the recognition step which allows subsequent import.


Pssm-ID: 462658  Cd Length: 114  Bit Score: 166.13  E-value: 6.23e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496   2 EAVVRRCPFLARVSQAFLQKAGPSLLLYAQHCPRMMeaappaARALATSAARGQQA-EEESPAGREAKNVKEvaqqnadg 80
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM------TRALSTSSANLQGEkEETPVAGPTAKQAKA-------- 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1209969496  81 tqLPAGHPPASASQSTATKCPFLAAQMNHKKSNVFCKASLELQEDVQEVQ 130
Cdd:pfam09029  67 --LPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
PLN02483 PLN02483
serine palmitoyltransferase
 244-602 8.84e-43

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 161.08  E-value: 8.84e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 244 SNDYLGMSRHPRVCGA-VMETLKQHGAGAGGTRNISGTSKFHVDLEKELADLHGKDAALLFSSCFVANDSTLFTLakMLP 322
Cdd:PLN02483  107 SYNYLGFAAADEYCTPrVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPAL--IGK 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 323 GCEIYSDSGNHASMIQGICNSRVPKHIFRHNDVNHLRELLKKS----DPSTPK-----IVAFETVHSMDGAVCPLEELCD 393
Cdd:PLN02483  185 GGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQiaegQPRTHRpwkkiIVIVEGIYSMEGELCKLPEIVA 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 394 VAHEHGAITFVDEVHAVGLYGARGGGIGDRDGVMHK-MDIISGTLGKAFGCVGGYISSTSSLIDTVRSYAAGFIFTTSLP 472
Cdd:PLN02483  265 VCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPAdVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYATSMS 344

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 473 PMLLAGALESVRTLKSAEG-----QALRRQHQrNVKLMRQMLMDAGLPVV-HCPSHIIPVRVADAAKNTEICDKLMSQHS 546
Cdd:PLN02483  345 PPAVQQVISAIKVILGEDGtnrgaQKLAQIRE-NSNFFRSELQKMGFEVLgDNDSPVMPIMLYNPAKIPAFSRECLKQNV 423

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1209969496 547 IYVQaINYPTVPRGEELLRIAPTPHHTPQMMSYFIEKLLATWKDVGLELKPHSSAE 602
Cdd:PLN02483  424 AVVV-VGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPAEPKK 478
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 237-575 9.94e-41

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 154.83  E-value: 9.94e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 237 KEVSVWCSNDYLGMSRHPRVCGAVMETLKQHGAGAGGTRNISGTSKFHVDLEKELADLHGKDAALLFSSCFVANDSTLFT 316
Cdd:PLN02955  102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVA 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 317 L---AKMLPGCE---------IYSDSGNHASMIQGIC----NSRVPKHIFRHNDVNHLRELLKkSDPSTPKIVAFETVHS 380
Cdd:PLN02955  182 IgsvASLLAASGkplknekvaIFSDALNHASIIDGVRlaerQGNVEVFVYRHCDMYHLNSLLS-SCKMKRKVVVTDSLFS 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 381 MDGAVCPLEELCDVAHEHGAITFVDEVHAVGLYGARGGGIGDRDGVMHKMDIISGTLGKAFGCVGGYISSTSSLIDTVRS 460
Cdd:PLN02955  261 MDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQS 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 461 YAAGFIFTTSLPPMLLAGALESVRTlksAEGQALRRQHQRN-VKLMRQMlmdAGLPVvhcPSHIIPVRVADAAKNTEICD 539
Cdd:PLN02955  341 RGRSFIFSTAIPVPMAAAAYAAVVV---ARKEKWRRKAIWErVKEFKAL---SGVDI---SSPIISLVVGNQEKALKASR 411

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1209969496 540 KLMsQHSIYVQAINYPTVPRGEELLRIAPTPHHTPQ 575
Cdd:PLN02955  412 YLL-KSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTE 446
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
244-597 2.95e-40

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 152.09  E-value: 2.95e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 244 SNDYLGMSRHPRVCGAVMETLKQHGagaggtRNISGTSKFHVD------LEKELADLHGKDAALLFSSCFVANDSTLFTL 317
Cdd:PRK07179   61 SNDYLNLSGHPDIIKAQIAALQEEG------DSLVMSAVFLHDdspkpqFEKKLAAFTGFESCLLCQSGWAANVGLLQTI 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 318 AKmlPGCEIYSDSGNHASMIQGICNSRVPKHIFRHNDVNHLRELLKKSDPStpkIVAFETVHSMDGAVCPLEELCDVAHE 397
Cdd:PRK07179  135 AD--PNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPG---IIVVDSVYSTTGTIAPLADIVDIAEE 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 398 HGAITFVDEVHAVGLYGARGGGIGDRDGVMHKMDIISGTLGKAFGCVGGYISSTSSLIDTVR--SYAAgfIFTTSLPPML 475
Cdd:PRK07179  210 FGCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPfvSYPA--IFSSTLLPHE 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 476 LAGALESVRTLKSAEGqalRRQH-QRNVKLMRQMLMDAGLPvVHCPSHIIPVrVADAAKNTEICDKLMSQHSIYVQAINY 554
Cdd:PRK07179  288 IAGLEATLEVIESADD---RRARlHANARFLREGLSELGYN-IRSESQIIAL-ETGSERNTEVLRDALEERNVFGAVFCA 362

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1209969496 555 PTVPRGEELLRIAPTPHHTPQMMSYFIEKLLATWKDVGLELKP 597
Cdd:PRK07179  363 PATPKNRNLIRLSLNADLTASDLDRVLEVCREARDEVDLWFWK 405
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 241-547 5.33e-32

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 128.10  E-value: 5.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 241 VWCSNDYLGMSRHPRVCGAVMETLKQHGAGAGGTRNISGTSKFHVDLEKELADLHGKDAALLFSSCFVANDSTLFTLAKM 320
Cdd:PLN03227    2 NFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAKR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 321 lpGCEIYSDSGNHASMIQGICNSRVPKHIFRHNDVNHLRELL----------KKSDPSTPKIVAFETVHSMDGAVCPLEE 390
Cdd:PLN03227   82 --GDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLeqvraqdvalKRKPTDQRRFLVVEGLYKNTGTLAPLKE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 391 LCDVAHEHGAITFVDEVHAVGLYG--ARGGGIGDRDGVMHKMDIISGTLGKAFGCVGGYISSTSSLIDTVRSYAAGFIFT 468
Cdd:PLN03227  160 LVALKEEFHYRLILDESFSFGTLGksGRGSLEHAGLKPMVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 469 TSLPPMLLAGALESVRTLKsAEGQALRRQHQrNVKLMRQMLMDAGLPVVHCP-----------SHIIPVRVADAAKnTEI 537
Cdd:PLN03227  240 ASAPPFLAKADATATAGEL-AGPQLLNRLHD-SIANLYSTLTNSSHPYALKLrnrlvitsdpiSPIIYLRLSDQEA-TRR 316

                         330
                  ....*....|
gi 1209969496 538 CDKLMSQHSI 547
Cdd:PLN03227  317 TDETLILDQI 326
PLN02822 PLN02822
serine palmitoyltransferase
 234-559 1.11e-29

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 122.93  E-value: 1.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 234 ITKKEVSVWCSNDYLGMSRHPRVCGAVMETLKQHGAGAGGTRNISGTSKFHVDLEKELADLHGKDAALLFSscfvandST 313
Cdd:PLN02822  106 INGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYS-------YG 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 314 LFTLAKMLPG-CE----IYSDSGNHASMIQGICNSRVPKHIFRHNDVNHLRELLKK---SDPSTPKI---VAFETVHSMD 382
Cdd:PLN02822  179 LSTIFSVIPAfCKkgdiIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKltaENKRKKKLrryIVVEAIYQNS 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 383 GAVCPLEELCDVAHEHGAITFVDEVHAVGLYGARGGGIGDRDGV-MHKMDIISGTLGKAFGCVGGYISSTSSLIDTVRSY 461
Cdd:PLN02822  259 GQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVpIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLS 338

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 462 AAGFIFTTSLPPMLLAGALESVRTLKsaEGQALRRQHQRNVKLMRQMLMD-AGL--------PVVHCpsHIIPVR---VA 529
Cdd:PLN02822  339 SSGYVFSASLPPYLASAAITAIDVLE--DNPSVLAKLKENIALLHKGLSDiPGLsigsntlsPIVFL--HLEKSTgsaKE 414

                         330       340       350
                  ....*....|....*....|....*....|
gi 1209969496 530 DAAKNTEICDKLMSQHSIYVQAINYPTVPR 559
Cdd:PLN02822  415 DLSLLEHIADRMLKEDSVLVVVSKRSTLDK 444
PRK07505 PRK07505
hypothetical protein; Provisional
 243-594 4.43e-28

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 116.62  E-value: 4.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 243 CSNDYLGMSRHPRVCGAVMETLKqhgagAGGTRNISgTSKFHV------DLEKELADLHGKDAaLLFSSCFVANDSTLFT 316
Cdd:PRK07505   52 VSCSYLGLDTHPAIIEGAVDALK-----RTGSLHLS-SSRTRVrsqilkDLEEALSELFGASV-LTFTSCSAAHLGILPL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 317 LAK-MLPGCE----IYsDSGNHASM--IQGICNSRVPKHIFRHNDVNHLRELLKKSDpsTPKIVAfETVHSMdGAVCPLE 389
Cdd:PRK07505  125 LASgHLTGGVpphmVF-DKNAHASLniLKGICADETEVETIDHNDLDALEDICKTNK--TVAYVA-DGVYSM-GGIAPVK 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 390 ELCDVAHEHGAITFVDEVHAVGLYGargggIGDRDGVMHKMD-------IISGTLGKAFGCVGGYIS-STSSLIDTVRSY 461
Cdd:PRK07505  200 ELLRLQEKYGLFLYIDDAHGLSIYG-----KNGEGYVRSELDyrlnertIIAASLGKAFGASGGVIMlGDAEQIELILRY 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 462 AAGFIFTTSLPPMLLAGALESVRTLKSAEGQALRRQHQRNVKLMRQMLMD--AGLPVvhcpshiiPVRVA---DAAKNTE 536
Cdd:PRK07505  275 AGPLAFSQSLNVAALGAILASAEIHLSEELDQLQQKLQNNIALFDSLIPTeqSGSFL--------PIRLIyigDEDTAIK 346

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1209969496 537 ICDKLMSQhSIYVQAINYPTVPRGEELLRIAPTPHHTPQMmsyfIEKLLATWKDVGLE 594
Cdd:PRK07505  347 AAKQLLDR-GFYTSPVFFPVVAKGRAGLRIMFRASHTNDE----IKRLCSLLKEILDE 399
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 244-536 1.52e-21

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 96.77  E-value: 1.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 244 SNDYLGMSRHPRVCGAVMETLKQH-------GAGAGGTRNISGTSKFHVDLEKELADLHGKDAALLFSSCFVANDSTLFT 316
Cdd:PRK05937   11 TNDFLGFSRSDTLVHEVEKRYRLYcrqfphaQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLCAH 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 317 LAKMLPgcEIYSDSGNHASMIQGICNSRVPKHIFRHNDVNHLRELLKKSDP-STPKIVAFE-TVHSMDGAVCPLEELCDV 394
Cdd:PRK05937   91 LSSVTD--YVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQrSFGRIFIFVcSVYSFKGTLAPLEQIIAL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 395 AHEHGAITFVDEVHAVGLYGARGGGIGDRDGVMHKMDIISgTLGKAFGCVGGYISSTSSLIDTVRSYAAGFIFTTSLPPM 474
Cdd:PRK05937  169 SKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGYENFYAVLV-TYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGLPPH 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 475 LLAgALESVRTLKSAEGQALRRQ--------HQR-----------------NVKLMRQMLMDAGLPV-VHCPSHIIPVRV 528
Cdd:PRK05937  248 LLI-SIQVAYDFLSQEGELARKQlfrlkeyfAQKfssaapgcvqpiflpgiSEQELYSKLVETGIRVgVVCFPTGPFLRV 326


                  ....*...
gi 1209969496 529 ADAAKNTE 536
Cdd:PRK05937  327 NLHAFNTE 334
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 283-446 4.07e-13

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: 67.79  E-value: 4.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 283 FHVDLEKELADL--HGKDAALLFSSCFVANDSTLFTLAKmlPGCEIYSDSGNHAS--MIQGICNSRVPKHI------FRH 352
Cdd:cd01494     1 KLEELEEKLARLlqPGNDKAVFVPSGTGANEAALLALLG--PGDEVIVDANGHGSryWVAAELAGAKPVPVpvddagYGG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 353 NDVNHLRELLKKSdpsTPKIVAFETVHSMDGAVCPLEELCDVAHEHGAITFVDEVHAVGLYGARGGGIGDrdgvmHKMDI 432
Cdd:cd01494    79 LDVAILEELKAKP---NVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPE-----GGADV 150

                         170
                  ....*....|....
gi 1209969496 433 ISGTLGKAFGCVGG 446
Cdd:cd01494   151 VTFSLHKNLGGEGG 164
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 287-501 5.77e-09

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: 58.37  E-value: 5.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 287 LEKELADLHGKDAALLFSSCFVANDSTLFTLAK----MLPGCEIYSDSGNHASMIQ---GICNSRVpkhifrhnDVNHLR 359
Cdd:cd00614    45 LEKKLAALEGGEAALAFSSGMAAISTVLLALLKagdhVVASDDLYGGTYRLFERLLpklGIEVTFV--------DPDDPE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 360 ELLKKSDPSTpKIVAFETVHSMDGAVCPLEELCDVAHEHGAITFVDEVHAVGLY------GArgggigdrDGVMHkmdii 433
Cdd:cd00614   117 ALEAAIKPET-KLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVDNTFATPYLqrplelGA--------DIVVH----- 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1209969496 434 SGTlgKAFG----CVGGYIS-STSSLIDTVRS--YAAGfiftTSLPPMLLAGALESVRTLKsaegqaLR-RQHQRN 501
Cdd:cd00614   183 SAT--KYIGghsdVIAGVVVgSGEALIQRLRFlrLALG----TILSPFDAWLLLRGLKTLP------LRmERHSEN 246
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 388-567 1.66e-07

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: 53.50  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 388 LEELCDVAHEHGAITFVDEVHAvGLYGARGGGIGDRDGVMHKMDIISGTLGKAFGCVG---GYISSTSSLIdtVRSYAAG 464
Cdd:cd00609   154 LEELAELAKKHGILIISDEAYA-ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYLIAPPEEL--LERLKKL 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 465 FIFTTSLPPMLLAGALESVRTLKSAEGQALRRQHQRNVKLMRQMLMDAGLPVVHCPS---HI-IPVRVADAAkntEICDK 540
Cdd:cd00609   231 LPYTTSGPSTLSQAAAAAALDDGEEHLEELRERYRRRRDALLEALKELGPLVVVKPSggfFLwLDLPEGDDE---EFLER 307

                         170       180
                  ....*....|....*....|....*..
gi 1209969496 541 LMSQHSIYVQAINYPtVPRGEELLRIA 567
Cdd:cd00609   308 LLLEAGVVVRPGSAF-GEGGEGFVRLS 333
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
354-411 1.98e-07

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 53.60  E-value: 1.98e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1209969496 354 DVNHLRELLkksDPSTpKIVAFETVHSMDGAVCPLEELCDVAHEHGAITFVDEVHAVG 411
Cdd:COG0520   143 DLEALEALL---TPRT-KLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVP 196
Cys_Met_Meta_PP pfam01053
Cys/Met metabolism PLP-dependent enzyme; This family includes enzymes involved in cysteine and ...
 287-405 1.32e-06

Cys/Met metabolism PLP-dependent enzyme; This family includes enzymes involved in cysteine and methionine metabolism. The following are members: Cystathionine gamma-lyase, Cystathionine gamma-synthase, Cystathionine beta-lyase, Methionine gamma-lyase, OAH/OAS sulfhydrylase, O-succinylhomoserine sulfhydrylase All of these members participate is slightly different reactions. All these enzymes use PLP (pyridoxal-5'-phosphate) as a cofactor.


Pssm-ID: 395837 [Multi-domain]  Cd Length: 376  Bit Score: 51.08  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 287 LEKELADLHGKDAALLFSSCFVANDSTLFTLAKmlPGCEIYSDS----GNHAsmiqgICNSRVPKH--IFRHNDVNHLRE 360
Cdd:pfam01053  52 LEERIAALEGGAAALAFSSGMAAITAAILALLK--AGDHIVATDdlygGTYR-----LFNKVLPRFgiEVTFVDTSDPED 124

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1209969496 361 LLKKSDPSTpKIVAFETVHSMDGAVCPLEELCDVAHEHGAITFVD 405
Cdd:pfam01053 125 LEAAIKPNT-KAVYLETPTNPLLKVVDIEAIAKLAKKHGILVVVD 168
MetC COG0626
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; ...
 287-501 9.51e-06

Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; Cystathionine beta-lyase/cystathionine gamma-synthase is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 440391 [Multi-domain]  Cd Length: 389  Bit Score: 48.12  E-value: 9.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 287 LEKELADLHGKDAALLFSSCFVANDSTLFTLAKmlPGCEI-YSDS---GNHAsmiqgICNSRVPK-----HIFRHNDVNH 357
Cdd:COG0626    63 LEEALAALEGGEAALAFASGMAAISAVLLALLK--AGDHVvASDDlygGTRR-----LLDKVLARfgievTFVDPTDLAA 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 358 LRELLKksdPSTpKIVAFETVHSMDGAVCPLEELCDVAHEHGAITFVDEVHAVGLY------GArgggigdrDGVMHkmd 431
Cdd:COG0626   136 VEAAIR---PNT-KLVFLETPSNPTLEVVDIAAIAAIAHAAGALLVVDNTFATPLLqrplelGA--------DIVVH--- 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 432 iiSGTlgKAFG----CVGGYISSTSSLI-DTVRSY--AAGFI---FTTSLppmllagALESVRTLksaegqALR-RQHQR 500
Cdd:COG0626   201 --SAT--KYLGghsdVLGGAVVGRDEELaERLRFLqnALGAVlspFDAWL-------LLRGLKTL------ALRmERHCE 263


                  .
gi 1209969496 501 N 501
Cdd:COG0626   264 N 264
PucG COG0075
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
 354-597 9.69e-05

Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439845 [Multi-domain]  Cd Length: 376  Bit Score: 45.08  E-value: 9.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 354 DVNHLRELLKKsDPStPKIVAFetVHSmD---GAVCPLEELCDVAHEHGAITFVDEVHAVGlygargggigdrdgVMH-K 429
Cdd:COG0075   112 DPEEVEEALAA-DPD-IKAVAV--VHN-EtstGVLNPLEEIGALAKEHGALLIVDAVSSLG--------------GVPlD 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 430 MD------IISGTlGKAFGCVGG------------------YISSTSSLIDTVRSYAAGFIFTTSlPPMLLAGALESVRT 485
Cdd:COG0075   173 MDewgidvVVSGS-QKCLMLPPGlafvavseraleaiearkLPSYYLDLKLWLKYWEKGQTPYTP-PVSLLYALREALDL 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209969496 486 LKsAEG-QALRRQHQRNVKLMRQMLMDAGLPVV---HCPSHII-PVRVADAAKNTEICDKLMSQHSIYVqAINYPTVprG 560
Cdd:COG0075   251 IL-EEGlENRFARHRRLAEALRAGLEALGLELFaeeEYRSPTVtAVRVPEGVDAAALRKRLKERYGIEI-AGGLGPL--K 326

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1209969496 561 EELLRIAPTPHHTPQMMSYFIEKLLATWKDVGLELKP 597
Cdd:COG0075   327 GKIFRIGHMGYVNPEDVLRTLAALEEALRELGVPVEL 363
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 354-411 5.54e-04

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: 42.62  E-value: 5.54e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1209969496 354 DVNHLRELLKKsdpsTPKIVAFETVHSMDGAVCPLEELCDVAHEHGAITFVDEVHAVG 411
Cdd:pfam00266 128 DLDELEKLITP----KTKLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIG 181
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 354-411 2.41e-03

Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.


Pssm-ID: 99746 [Multi-domain]  Cd Length: 373  Bit Score: 40.53  E-value: 2.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1209969496 354 DVNHLRELLkksDPSTpKIVAFETVHSMDGAVCPLEELCDVAHEHGAITFVDEVHAVG 411
Cdd:cd06453   128 DLEALEKLL---TERT-KLVAVTHVSNVLGTINPVKEIGEIAHEAGVPVLVDGAQSAG 181
 
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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