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Conserved domains on  [gi|42475958|ref|NP_077810|]
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5-aminolevulinate synthase, non-specific, mitochondrial precursor [Rattus norvegicus]

Protein Classification

glycine dehydrogenase; pyridoxal phosphate-dependent aminotransferase( domain architecture ID 11181659)

decarboxylating glycine dehydrogenase catalyzes the degradation of glycine as part of the glycine cleavage system| pyridoxal phosphate-dependent aminotransferase such as glutamate-pyruvate aminotransferase AlaA that catalyzes the transamination of pyruvate by glutamate, leading to the formation of L-alanine and 2-oxoglutarate

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) ...
 199-604 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: 681.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   199 FQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVIETVKQHGAG 278
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   279 AGGTRNISGTSKFHVELEQELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 358
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   359 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGASGGGIGDRDGVMPKM 438
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   439 DIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSNEgrALRRQHQRNVKLMRQMLM 518
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   519 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNFFLEKLLLTWKR 598
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 42475958   599 VGLELK 604
Cdd:TIGR01821 397 LGLPLS 402
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 2-140 3.15e-47

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: 161.89  E-value: 3.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958     2 ETVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMevgakpaPRTVSTSAAQCQQVKE-TPPANEKEKTAKAavqqapd 80
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEKEeTPVAGPTAKQAKA------- 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958    81 esqmaqtpdgtqLPPGHPSPSTSQSSGSKCPFLAAQLSQTGSSVFRKASLELQEDVQEMH 140
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 ...
 199-604 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: 681.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   199 FQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVIETVKQHGAG 278
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   279 AGGTRNISGTSKFHVELEQELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 358
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   359 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGASGGGIGDRDGVMPKM 438
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   439 DIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSNEgrALRRQHQRNVKLMRQMLM 518
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   519 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNFFLEKLLLTWKR 598
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 42475958   599 VGLELK 604
Cdd:TIGR01821 397 LGLPLS 402
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 245-592 0e+00

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: 525.59  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958 245 KQVSVWCSNDYLGMSRHPRVCGAVIETVKQHGAGAGGTRNISGTSKFHVELEQELADLHGKDAALLFSSCFVANDSTLFT 324
Cdd:cd06454   1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958 325 LakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQRSD-PSVPKIVAFETVHSMDGAVCPLEELCDVA 403
Cdd:cd06454  81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958 404 HEFGAITFVDEVHAVGLYGASGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPML 483
Cdd:cd06454 159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958 484 LAGALESVRILKSneGRALRRQHQRNVKLMRQMLMDAGLPVIHCPSHIIPVRVAD-AAKNTEICDELMtRHNIYVQAINY 562
Cdd:cd06454 239 AAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDdPAKAVAFSDALL-ERGIYVQAIRY 315

                       330       340       350
                ....*....|....*....|....*....|
gi 42475958 563 PTVPRGEELLRIAPTPHHTPQMMNFFLEKL 592
Cdd:cd06454 316 PTVPRGTARLRISLSAAHTKEDIDRLLEAL 345
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 199-610 2.55e-178

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 512.09  E-value: 2.55e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  199 FQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVIETVKQHGAG 278
Cdd:PRK13392   2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGPD--GPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  279 AGGTRNISGTSKFHVELEQELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 358
Cdd:PRK13392  80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  359 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGASGGGIGDRDGVMPKM 438
Cdd:PRK13392 160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  439 DIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKsnEGRALRRQHQRNVKLMRQMLM 518
Cdd:PRK13392 240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLK--TSQTERDAHQDRVAALKAKLN 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  519 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNFFLEKLLLTWKR 598
Cdd:PRK13392 318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397

                        410
                 ....*....|..
gi 42475958  599 VGLELKPHSSAE 610
Cdd:PRK13392 398 LELPRWREAAQA 409
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 201-598 1.15e-167

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: 483.78  E-value: 1.15e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958 201 YDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDytdslitkKQVSVWCSNDYLGMSRHPRVCGAVIETVKQHGAGAG 280
Cdd:COG0156   1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDG--------REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958 281 GTRNISGTSKFHVELEQELADLHGKDAALLFSSCFVANDSTLFTLAKmmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRH 360
Cdd:COG0156  73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958 361 NDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGASGGGIGDRDGVMPKMDI 440
Cdd:COG0156 151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDI 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958 441 ISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSNEgrALRRQHQRNVKLMRQMLMDA 520
Cdd:COG0156 231 IMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP--ELRERLWENIAYFREGLKEL 308

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42475958 521 GLPVIHCPSHIIPVRVADAAKNTEICDELMtRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNFFLEKLLLTWKR 598
Cdd:COG0156 309 GFDLGPSESPIVPVIVGDAERALALADALL-ERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
250-592 1.14e-71

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 235.28  E-value: 1.14e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   250 WCSNDYLGMsrhprVCGAVIETVKQhgAGAGGTRNISGTSKFHVELEQELADLHG--------KDAALLFSSCFVANDST 321
Cdd:pfam00155   6 LGSNEYLGD-----TLPAVAKAEKD--ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGANIEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   322 LFTLAKMmPGCEIYSDSGNHASMIQGIRNSRVPKYIFR-------HNDVNHLRELLQRSdpsvPKIVAFETVHSMDGAVC 394
Cdd:pfam00155  79 LIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNPTGTVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   395 PLEELCDVA---HEFGAITFVDEVHAVGLYGaSGGGIGDRDGVMPKMD-IISGTLGKAFGCVG---GYIASTSLLIDTVR 467
Cdd:pfam00155 154 TLEELEKLLdlaKEHNILLLVDEAYAGFVFG-SPDAVATRALLAEGPNlLVVGSFSKAFGLAGwrvGYILGNAAVISQLR 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   468 SYAAGFIFTTSLPPMLLAGALESvrILKSNEGRALRRQHQRNVKLMRQMLMDAGLPVIHCPSHIIPVRVADAAKNTEICD 547
Cdd:pfam00155 233 KLARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQ 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 42475958   548 ELMTRHNIYVQAINYPTVPrgeELLRIAPTpHHTPQMMNFFLEKL 592
Cdd:pfam00155 311 VLLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLEAI 351
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 2-140 3.15e-47

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: 161.89  E-value: 3.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958     2 ETVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMevgakpaPRTVSTSAAQCQQVKE-TPPANEKEKTAKAavqqapd 80
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEKEeTPVAGPTAKQAKA------- 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958    81 esqmaqtpdgtqLPPGHPSPSTSQSSGSKCPFLAAQLSQTGSSVFRKASLELQEDVQEMH 140
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 ...
 199-604 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: 681.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   199 FQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVIETVKQHGAG 278
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   279 AGGTRNISGTSKFHVELEQELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 358
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   359 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGASGGGIGDRDGVMPKM 438
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   439 DIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSNEgrALRRQHQRNVKLMRQMLM 518
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   519 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNFFLEKLLLTWKR 598
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 42475958   599 VGLELK 604
Cdd:TIGR01821 397 LGLPLS 402
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 245-592 0e+00

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: 525.59  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958 245 KQVSVWCSNDYLGMSRHPRVCGAVIETVKQHGAGAGGTRNISGTSKFHVELEQELADLHGKDAALLFSSCFVANDSTLFT 324
Cdd:cd06454   1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958 325 LakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQRSD-PSVPKIVAFETVHSMDGAVCPLEELCDVA 403
Cdd:cd06454  81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958 404 HEFGAITFVDEVHAVGLYGASGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPML 483
Cdd:cd06454 159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958 484 LAGALESVRILKSneGRALRRQHQRNVKLMRQMLMDAGLPVIHCPSHIIPVRVAD-AAKNTEICDELMtRHNIYVQAINY 562
Cdd:cd06454 239 AAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDdPAKAVAFSDALL-ERGIYVQAIRY 315

                       330       340       350
                ....*....|....*....|....*....|
gi 42475958 563 PTVPRGEELLRIAPTPHHTPQMMNFFLEKL 592
Cdd:cd06454 316 PTVPRGTARLRISLSAAHTKEDIDRLLEAL 345
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 199-610 2.55e-178

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 512.09  E-value: 2.55e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  199 FQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVIETVKQHGAG 278
Cdd:PRK13392   2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGPD--GPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  279 AGGTRNISGTSKFHVELEQELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 358
Cdd:PRK13392  80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  359 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGASGGGIGDRDGVMPKM 438
Cdd:PRK13392 160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  439 DIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKsnEGRALRRQHQRNVKLMRQMLM 518
Cdd:PRK13392 240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLK--TSQTERDAHQDRVAALKAKLN 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  519 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNFFLEKLLLTWKR 598
Cdd:PRK13392 318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397

                        410
                 ....*....|..
gi 42475958  599 VGLELKPHSSAE 610
Cdd:PRK13392 398 LELPRWREAAQA 409
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 201-598 1.15e-167

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: 483.78  E-value: 1.15e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958 201 YDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDytdslitkKQVSVWCSNDYLGMSRHPRVCGAVIETVKQHGAGAG 280
Cdd:COG0156   1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDG--------REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958 281 GTRNISGTSKFHVELEQELADLHGKDAALLFSSCFVANDSTLFTLAKmmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRH 360
Cdd:COG0156  73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958 361 NDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGASGGGIGDRDGVMPKMDI 440
Cdd:COG0156 151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDI 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958 441 ISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSNEgrALRRQHQRNVKLMRQMLMDA 520
Cdd:COG0156 231 IMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP--ELRERLWENIAYFREGLKEL 308

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42475958 521 GLPVIHCPSHIIPVRVADAAKNTEICDELMtRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNFFLEKLLLTWKR 598
Cdd:COG0156 309 GFDLGPSESPIVPVIVGDAERALALADALL-ERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 245-592 1.90e-101

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: 313.44  E-value: 1.90e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   245 KQVSVWCSNDYLGMSRHPRVCGAVIETVKQHGAGAGGTRNISGTSKFHVELEQELADLHGKDAALLFSSCFVANDSTLFT 324
Cdd:TIGR00858  16 RRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVISA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   325 LAKmmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAH 404
Cdd:TIGR00858  96 LVG--KGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSMDGDIAPLPQLVALAE 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   405 EFGAITFVDEVHAVGLYGASGGGIGDRDGVMPKMDIIS-GTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPML 483
Cdd:TIGR00858 174 RYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDIQvGTLSKALGSYGAYVAGSQALIDYLINRARTLIFSTALPPAV 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   484 LAGALESVRILKsnEGRALRRQHQRNVKLMRQMLMDAGLPVIHCPSHIIPVRVADAAKNTEICDELMtRHNIYVQAINYP 563
Cdd:TIGR00858 254 AAAALAALELIQ--EEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQ-QQGIFVGAIRPP 330

                         330       340
                  ....*....|....*....|....*....
gi 42475958   564 TVPRGEELLRIAPTPHHTPQMMNFFLEKL 592
Cdd:TIGR00858 331 TVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 205-592 2.43e-100

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 311.32  E-value: 2.43e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  205 FEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDytdslitkKQVSVWCSNDYLGMSRHPRVCGAVIETVKQHGAGAGGTRN 284
Cdd:PRK05958   7 LEAALAQRRAAGLYRSLRPREGGAGRWLVVDG--------RRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  285 ISGTSKFHVELEQELADLHGKDAALLFSSCFVANDSTLFTLakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVN 364
Cdd:PRK05958  79 VTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTAL--AGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  365 HLRELLQRSDPSvPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGASGGGIGDRDGV-MPKMDIISG 443
Cdd:PRK05958 157 ALEALLAKWRAG-RALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLaGEPDVILVG 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  444 TLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSNEGralRRQH-QRNVKLMRQMLMDAGL 522
Cdd:PRK05958 236 TLGKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPE---RRERlAALIARLRAGLRALGF 312

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  523 PVIHCPSHIIPVRVADAAKNTEICDELMTRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNFFLEKL 592
Cdd:PRK05958 313 QLMDSQSAIQPLIVGDNERALALAAALQEQ-GFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEAL 381
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 204-604 2.10e-94

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 296.34  E-value: 2.10e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  204 FFEKKIDEKKNDHTY---RVFKTVNRrAQIfpmaddytdSLITKKQVSVWCSNDYLGMSRHPRVCGAVIETVKQHGAGAG 280
Cdd:PRK06939   8 QLREELEEIKAEGLYkeeRVITSPQG-ADI---------TVADGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  281 GTRNISGTSKFHVELEQELADLHGKDAALLFSSCFVANDSTLFTLakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRH 360
Cdd:PRK06939  78 SVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETL--LGKEDAIISDALNHASIIDGVRLCKAKRYRYAN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  361 NDVNHLRELLQRSDPSVP--KIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGASGGGIGDRDGVMPKM 438
Cdd:PRK06939 156 NDMADLEAQLKEAKEAGArhKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRV 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  439 DIISGTLGKAF-GCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKsnEGRALRRQHQRNVKLMRQML 517
Cdd:PRK06939 236 DIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLE--ESDELRDRLWENARYFREGM 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  518 MDAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQMmnffLEKLLLTWK 597
Cdd:PRK06939 314 TAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLLEE-GVYVIGFSFPVVPKGQARIRTQMSAAHTKEQ----LDRAIDAFE 388


                 ....*..
gi 42475958  598 RVGLELK 604
Cdd:PRK06939 389 KVGKELG 395
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
250-592 1.14e-71

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 235.28  E-value: 1.14e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   250 WCSNDYLGMsrhprVCGAVIETVKQhgAGAGGTRNISGTSKFHVELEQELADLHG--------KDAALLFSSCFVANDST 321
Cdd:pfam00155   6 LGSNEYLGD-----TLPAVAKAEKD--ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGANIEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   322 LFTLAKMmPGCEIYSDSGNHASMIQGIRNSRVPKYIFR-------HNDVNHLRELLQRSdpsvPKIVAFETVHSMDGAVC 394
Cdd:pfam00155  79 LIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNPTGTVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   395 PLEELCDVA---HEFGAITFVDEVHAVGLYGaSGGGIGDRDGVMPKMD-IISGTLGKAFGCVG---GYIASTSLLIDTVR 467
Cdd:pfam00155 154 TLEELEKLLdlaKEHNILLLVDEAYAGFVFG-SPDAVATRALLAEGPNlLVVGSFSKAFGLAGwrvGYILGNAAVISQLR 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958   468 SYAAGFIFTTSLPPMLLAGALESvrILKSNEGRALRRQHQRNVKLMRQMLMDAGLPVIHCPSHIIPVRVADAAKNTEICD 547
Cdd:pfam00155 233 KLARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQ 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 42475958   548 ELMTRHNIYVQAINYPTVPrgeELLRIAPTpHHTPQMMNFFLEKL 592
Cdd:pfam00155 311 VLLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLEAI 351
PLN02483 PLN02483
serine palmitoyltransferase
 252-610 1.15e-51

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 185.74  E-value: 1.15e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  252 SNDYLGMSRHPRVCGA-VIETVKQHGAGAGGTRNISGTSKFHVELEQELADLHGKDAALLFSSCFVANDSTLFTLakMMP 330
Cdd:PLN02483 107 SYNYLGFAAADEYCTPrVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPAL--IGK 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  331 GCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQ--------RSDPSVPKI-VAFETVHSMDGAVCPLEELCD 401
Cdd:PLN02483 185 GGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLReqiaegqpRTHRPWKKIiVIVEGIYSMEGELCKLPEIVA 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  402 VAHEFGAITFVDEVHAVGLYGASGGGIGDRDGVMPK-MDIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLP 480
Cdd:PLN02483 265 VCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPAdVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYATSMS 344

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  481 PMLLAGALESVRIL----KSNEGRALRRQHQRNVKLMRQMLMDAGLPVI-HCPSHIIPVRVADAAKNTEICDELMTRhNI 555
Cdd:PLN02483 345 PPAVQQVISAIKVIlgedGTNRGAQKLAQIRENSNFFRSELQKMGFEVLgDNDSPVMPIMLYNPAKIPAFSRECLKQ-NV 423

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 42475958  556 YVQAINYPTVPRGEELLRIAPTPHHTPQMMNFFLEKLLLTWKRVGLELKPHSSAE 610
Cdd:PLN02483 424 AVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPAEPKK 478
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 245-583 4.34e-48

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 175.63  E-value: 4.34e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  245 KQVSVWCSNDYLGMSRHPRVCGAVIETVKQHGAGAGGTRNISGTSKFHVELEQELADLHGKDAALLFSSCFVANDSTLFT 324
Cdd:PLN02955 102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVA 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  325 L--------AKMMP----GCEIYSDSGNHASMIQGIR----NSRVPKYIFRHNDVNHLRELLQRSDPSvPKIVAFETVHS 388
Cdd:PLN02955 182 IgsvasllaASGKPlkneKVAIFSDALNHASIIDGVRlaerQGNVEVFVYRHCDMYHLNSLLSSCKMK-RKVVVTDSLFS 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  389 MDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGASGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSLLIDTVRS 468
Cdd:PLN02955 261 MDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQS 340

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  469 YAAGFIFTTSLPPMLLAGALESVRILKSNEGRalRRQHQRNVKLMRQMlmdAGLPVihcPSHIIPVRVADAAKNTEICDE 548
Cdd:PLN02955 341 RGRSFIFSTAIPVPMAAAAYAAVVVARKEKWR--RKAIWERVKEFKAL---SGVDI---SSPIISLVVGNQEKALKASRY 412

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 42475958  549 LMtRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQ 583
Cdd:PLN02955 413 LL-KSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTE 446
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 2-140 3.15e-47

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: 161.89  E-value: 3.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958     2 ETVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMevgakpaPRTVSTSAAQCQQVKE-TPPANEKEKTAKAavqqapd 80
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEKEeTPVAGPTAKQAKA------- 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958    81 esqmaqtpdgtqLPPGHPSPSTSQSSGSKCPFLAAQLSQTGSSVFRKASLELQEDVQEMH 140
Cdd:pfam09029  67 ------------LPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
252-605 3.70e-47

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 171.35  E-value: 3.70e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  252 SNDYLGMSRHPRVCGAVIETVKQHGAG----AGGTRNISGTSKFhvelEQELADLHGKDAALLFSSCFVANDSTLFTLAK 327
Cdd:PRK07179  61 SNDYLNLSGHPDIIKAQIAALQEEGDSlvmsAVFLHDDSPKPQF----EKKLAAFTGFESCLLCQSGWAANVGLLQTIAD 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  328 mmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQRSDPSvpkIVAFETVHSMDGAVCPLEELCDVAHEFG 407
Cdd:PRK07179 137 --PNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPG---IIVVDSVYSTTGTIAPLADIVDIAEEFG 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  408 AITFVDEVHAVGLYGASGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSLLIDTVR--SYAAgfIFTTSLPPMLLA 485
Cdd:PRK07179 212 CVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPfvSYPA--IFSSTLLPHEIA 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  486 GALESVRILKSNEGRalRRQHQRNVKLMRQMLMDAGLPvIHCPSHIIPVrVADAAKNTEIC-DELMTRhNIYVQAINYPT 564
Cdd:PRK07179 290 GLEATLEVIESADDR--RARLHANARFLREGLSELGYN-IRSESQIIAL-ETGSERNTEVLrDALEER-NVFGAVFCAPA 364

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 42475958  565 VPRGEELLRIAPTPHHTPQMMNFFLEKLLLTWKRVGLELKP 605
Cdd:PRK07179 365 TPKNRNLIRLSLNADLTASDLDRVLEVCREARDEVDLWFWK 405
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 249-555 8.09e-35

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 136.19  E-value: 8.09e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  249 VWCSNDYLGMSRHPRVCGAVIETVKQHGAGAGGTRNISGTSKFHVELEQELADLHGKDAALLFSSCFVANDSTLFTLAKM 328
Cdd:PLN03227   2 NFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAKR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  329 mpGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELL----------QRSDPSVPKIVAFETVHSMDGAVCPLEE 398
Cdd:PLN03227  82 --GDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLeqvraqdvalKRKPTDQRRFLVVEGLYKNTGTLAPLKE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  399 LCDVAHEFGAITFVDEVHAVGLYGASGGGIGDRDGVMP--KMDIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFT 476
Cdd:PLN03227 160 LVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKPmvHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  477 TSLPPMLLAGALESVRILKSNEgRALRRQHQrNVKLMRQMLMDAGLPVIHCP-----------SHIIPVRVADAAKnTEI 545
Cdd:PLN03227 240 ASAPPFLAKADATATAGELAGP-QLLNRLHD-SIANLYSTLTNSSHPYALKLrnrlvitsdpiSPIIYLRLSDQEA-TRR 316

                        330
                 ....*....|
gi 42475958  546 CDELMTRHNI 555
Cdd:PLN03227 317 TDETLILDQI 326
PLN02822 PLN02822
serine palmitoyltransferase
 242-497 2.61e-33

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 133.71  E-value: 2.61e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  242 ITKKQVSVWCSNDYLGMSRHPRVCGAVIETVKQHGAGAGGTRNISGTSKFHVELEQELADLHGKDAALLFSSCFVANDST 321
Cdd:PLN02822 106 INGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSV 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  322 LFTLAKMmpGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQ-------RSDPSVPKIVAfETVHSMDGAVC 394
Cdd:PLN02822 186 IPAFCKK--GDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEkltaenkRKKKLRRYIVV-EAIYQNSGQIA 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  395 PLEELCDVAHEFGAITFVDEVHAVGLYGASGGGIGDRDGVMP-KMDIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGF 473
Cdd:PLN02822 263 PLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIeKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGY 342

                        250       260
                 ....*....|....*....|....
gi 42475958  474 IFTTSLPPMLLAGALESVRILKSN 497
Cdd:PLN02822 343 VFSASLPPYLASAAITAIDVLEDN 366
PRK07505 PRK07505
hypothetical protein; Provisional
 251-583 1.01e-29

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 121.63  E-value: 1.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  251 CSNDYLGMSRHPRVCGAVIETVKqhgagAGGTRNISgTSKFHV------ELEQELADLHGKDAaLLFSSCFVANDSTLFT 324
Cdd:PRK07505  52 VSCSYLGLDTHPAIIEGAVDALK-----RTGSLHLS-SSRTRVrsqilkDLEEALSELFGASV-LTFTSCSAAHLGILPL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  325 LAK--MMPGCEIYS--DSGNHASM--IQGIRNSRVPKYIFRHNDVNHLRELLQRSdpsvpKIVAF--ETVHSMdGAVCPL 396
Cdd:PRK07505 125 LASghLTGGVPPHMvfDKNAHASLniLKGICADETEVETIDHNDLDALEDICKTN-----KTVAYvaDGVYSM-GGIAPV 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  397 EELCDVAHEFGAITFVDEVHAVGLYGASGGG--IGDRDGVMPKMDIISGTLGKAFGCVGGYIA-STSLLIDTVRSYAAGF 473
Cdd:PRK07505 199 KELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyvRSELDYRLNERTIIAASLGKAFGASGGVIMlGDAEQIELILRYAGPL 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  474 IFTTSLPPMLLAGALESVRILKSNEGRALRRQHQRNVKLMRQMLMD--AGLPVihcpshiiPVRVA---DAAKNTEICDE 548
Cdd:PRK07505 279 AFSQSLNVAALGAILASAEIHLSEELDQLQQKLQNNIALFDSLIPTeqSGSFL--------PIRLIyigDEDTAIKAAKQ 350

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 42475958  549 LMTRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQ 583
Cdd:PRK07505 351 LLDR-GFYTSPVFFPVVAKGRAGLRIMFRASHTND 384
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 252-544 2.62e-24

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 105.25  E-value: 2.62e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  252 SNDYLGMSRHPRVCGAVIETVKQH-------GAGAGGTRNISGTSKFHVELEQELADLHGKDAALLFSSCFVANDSTLFT 324
Cdd:PRK05937  11 TNDFLGFSRSDTLVHEVEKRYRLYcrqfphaQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLCAH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  325 LAKMMPgcEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQ--RSDPSVPKIVAFETVHSMDGAVCPLEELCDV 402
Cdd:PRK05937  91 LSSVTD--YVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLEscRQRSFGRIFIFVCSVYSFKGTLAPLEQIIAL 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  403 AHEFGAITFVDEVHAVGLYGASGGGIGDRDGVMPKMDIISgTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPM 482
Cdd:PRK05937 169 SKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGYENFYAVLV-TYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGLPPH 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958  483 LLAGALESVRILkSNEGRALRRQ--------HQR-----------------NVKLMRQMLMDAGLPV-IHCPSHIIPVRV 536
Cdd:PRK05937 248 LLISIQVAYDFL-SQEGELARKQlfrlkeyfAQKfssaapgcvqpiflpgiSEQELYSKLVETGIRVgVVCFPTGPFLRV 326


                 ....*...
gi 42475958  537 ADAAKNTE 544
Cdd:PRK05937 327 NLHAFNTE 334
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 291-454 3.38e-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: 3.38e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958 291 FHVELEQELADL--HGKDAALLFSSCFVANDSTLFTLAkmMPGCEIYSDSGNHAS--MIQGIRNSRVPKYIFRHNDVNHL 366
Cdd:cd01494   1 KLEELEEKLARLlqPGNDKAVFVPSGTGANEAALLALL--GPGDEVIVDANGHGSryWVAAELAGAKPVPVPVDDAGYGG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958 367 RELLQRSD---PSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGASGGGIGDRDGvmpkmDIISG 443
Cdd:cd01494  79 LDVAILEElkaKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGA-----DVVTF 153

                       170
                ....*....|.
gi 42475958 444 TLGKAFGCVGG 454
Cdd:cd01494 154 SLHKNLGGEGG 164
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 396-575 1.10e-06

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: 51.19  E-value: 1.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958 396 LEELCDVAHEFGAITFVDEVHA----VGLYGASGGGIGDRDGVmpkmdIISGTLGKAFGCVG---GY-IASTSLLIDTVR 467
Cdd:cd00609 154 LEELAELAKKHGILIISDEAYAelvyDGEPPPALALLDAYERV-----IVLRSFSKTFGLPGlriGYlIAPPEELLERLK 228

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958 468 SYAagfIFTTSLPPMLLAGALEsvRILKSNEG--RALRRQHQRNVKLMRQMLMDAGLPVIHCPS---HI-IPVRVADAAk 541
Cdd:cd00609 229 KLL---PYTTSGPSTLSQAAAA--AALDDGEEhlEELRERYRRRRDALLEALKELGPLVVVKPSggfFLwLDLPEGDDE- 302

                       170       180       190
                ....*....|....*....|....*....|....
gi 42475958 542 ntEICDELMTRHNIYVQAINYPtVPRGEELLRIA 575
Cdd:cd00609 303 --EFLERLLLEAGVVVRPGSAF-GEGGEGFVRLS 333
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 292-413 1.14e-06

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: 51.05  E-value: 1.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958 292 HVELEQELADLHGKDAALLFSSCFVANDSTLFTLAK-----MMPGCeIYSDSGNHASMIQ---GIRNSRVPKyifrhNDV 363
Cdd:cd00614  42 VDALEKKLAALEGGEAALAFSSGMAAISTVLLALLKagdhvVASDD-LYGGTYRLFERLLpklGIEVTFVDP-----DDP 115

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 42475958 364 NHLRELLQRSdpsvPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVD 413
Cdd:cd00614 116 EALEAAIKPE----TKLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVD 161
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
362-429 6.40e-06

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 48.98  E-value: 6.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42475958 362 DVNHLRELLqrsDPSVpKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVG------------LYGASG---- 425
Cdd:COG0520 143 DLEALEALL---TPRT-KLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPhlpvdvqalgcdFYAFSGhkly 218


                ....*.
gi 42475958 426 --GGIG 429
Cdd:COG0520 219 gpTGIG 224
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 378-419 7.31e-03

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: 39.15  E-value: 7.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 42475958   378 PKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVG 419
Cdd:pfam00266 140 TKLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIG 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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