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Conserved domains on  [gi|20072652|gb|AAH27241|]
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ALDH1L1 protein [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 1-203 1.75e-157

10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family represents the N-terminal hydrolase domain of the bifunctional protein 10-formyltetrahydrofolate dehydrogenase (FDH). This domain contains a 10-formyl-tetrahydrofolate (10-formyl-THF) binding site and shares sequence homology and structural topology with other enzymes utilizing this substrate. This domain functions as a hydrolase, catalyzing the conversion of 10-formyl-THF, a precursor for nucleotide biosynthesis, to tetrahydrofolate (THF). The overall FDH reaction mechanism is a coupling of two sequential reactions, a hydrolase and a formyl dehydrogenase, bridged by a substrate transfer step. The N-terminal hydrolase domain removes the formyl group from 10-formyl-THF and the C-terminal NADP-dependent dehydrogenase domain then reduces the formyl group to carbon dioxide. The two catalytic domains are connected by a third intermediate linker domain that transfers the formyl group, covalently attached to the sulfhydryl group of the phosphopantetheine arm, from the N-terminal domain to the C-terminal domain.


:

Pssm-ID: 187716 [Multi-domain]  Cd Length: 203  Bit Score: 445.74  E-value: 1.75e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGAEL 80
Cdd:cd08647   1 MKIAVIGQSLFGQEVYKELRKEGHEVVGVFTIPDKDGKADPLALEAEKDGVPVFKFPRWRAKGQAIPEVVAKYKALGAEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  81 NVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTV 160
Cdd:cd08647  81 NVLPFCSQFIPMEVIDAPKHGSIIYHPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTV 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 20072652 161 STLYNRFLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGI 203
Cdd:cd08647 161 DTLYNRFLYPEGIKAMVEAVRLIAEGKAPRIPQPEEGATYEGI 203
FDH_Hydrolase_C cd08703
The C-terminal subdomain of the hydrolase domain on the bi-functional protein ...
 206-306 7.18e-53

The C-terminal subdomain of the hydrolase domain on the bi-functional protein 10-formyltetrahydrofolate dehydrogenase; The family represents the C-terminal subdomain of the hydrolase domain on the bi-functional protein, 10-formyltetrahydrofolate dehydrogenase (FDH). FDH catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. The protein comprises two functional domains: the N-terminal hydrolase domain that removes a formyl group from 10-formyltetrahydrofolate and the C-terminal NADP-dependent dehydrogenase domain that reduces the formyl group to carbon dioxide. The hydrolase domain contains an N-terminal formyl transferase catalytic core subdomain and this C-terminal subdomain, which may be involved in substrate binding.


:

Pssm-ID: 187731 [Multi-domain]  Cd Length: 100  Bit Score: 173.69  E-value: 7.18e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652 206 KETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLNTSGLVPEGdALPIPGAHRPGVVTKAGLILFGNDDK 285
Cdd:cd08703   1 KELAKINWDQTAEALHNFIRGNDKVPGAWATIDGEQVTLFGSSLWKGGKPPGG-EVEVEGLERPGIVHKNGLLITGSDGK 79

                        90       100
                ....*....|....*....|.
gi 20072652 286 MLLVKNIQLEDGKMILASNFF 306
Cdd:cd08703  80 MVNVKRLQFEDGKMIPASKYG 100
ALDH-SF super family cl11961
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
 417-491 1.18e-27

NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


The actual alignment was detected with superfamily member cd07140:

Pssm-ID: 448367 [Multi-domain]  Cd Length: 486  Bit Score: 115.67  E-value: 1.18e-27
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20072652 417 TVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYR 491
Cdd:cd07140   1 TLKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYR 75
 
Name Accession Description Interval E-value
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 1-203 1.75e-157

10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family represents the N-terminal hydrolase domain of the bifunctional protein 10-formyltetrahydrofolate dehydrogenase (FDH). This domain contains a 10-formyl-tetrahydrofolate (10-formyl-THF) binding site and shares sequence homology and structural topology with other enzymes utilizing this substrate. This domain functions as a hydrolase, catalyzing the conversion of 10-formyl-THF, a precursor for nucleotide biosynthesis, to tetrahydrofolate (THF). The overall FDH reaction mechanism is a coupling of two sequential reactions, a hydrolase and a formyl dehydrogenase, bridged by a substrate transfer step. The N-terminal hydrolase domain removes the formyl group from 10-formyl-THF and the C-terminal NADP-dependent dehydrogenase domain then reduces the formyl group to carbon dioxide. The two catalytic domains are connected by a third intermediate linker domain that transfers the formyl group, covalently attached to the sulfhydryl group of the phosphopantetheine arm, from the N-terminal domain to the C-terminal domain.


Pssm-ID: 187716 [Multi-domain]  Cd Length: 203  Bit Score: 445.74  E-value: 1.75e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGAEL 80
Cdd:cd08647   1 MKIAVIGQSLFGQEVYKELRKEGHEVVGVFTIPDKDGKADPLALEAEKDGVPVFKFPRWRAKGQAIPEVVAKYKALGAEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  81 NVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTV 160
Cdd:cd08647  81 NVLPFCSQFIPMEVIDAPKHGSIIYHPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTV 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 20072652 161 STLYNRFLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGI 203
Cdd:cd08647 161 DTLYNRFLYPEGIKAMVEAVRLIAEGKAPRIPQPEEGATYEGI 203
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
1-309 7.93e-80

Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 251.18  E-value: 7.93e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKD---GK---ADPLGLEAEKDGVPVFKYSRWRAkgqalPDVVAKYQ 74
Cdd:COG0223   1 MRIVFMGTPDFAVPSLEALLAAGHEVVAVVTQPDRPagrGRkltPSPVKELALEHGIPVLQPESLKD-----PEFLEELR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  75 ALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEV 154
Cdd:COG0223  76 ALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPI 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652 155 LPDDTVSTLYNRfLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGAW 234
Cdd:COG0223 156 GPDDTAGSLHDK-LAELGAELLLETLDALEAGTLTPTPQDESGATYAPKISKEDGRIDWSRPAEEIHRLIRALNPWPGAF 234

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20072652 235 TEACEQKLTFFNSTLntsglvpegdaLPIPGAHRPGVVTKAG----LILFGndDKMLLVKNIQLEDGKMILASNFFKGA 309
Cdd:COG0223 235 TTLDGKRLKIWKARV-----------LEEAGGGAPGTILAVDkdglLVACG--DGALRLLELQPAGKKRMSAADFLRGY 300
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 1-180 6.78e-69

Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.


Pssm-ID: 395436 [Multi-domain]  Cd Length: 181  Bit Score: 218.31  E-value: 6.78e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652     1 MKIAVI--GQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGA 78
Cdd:pfam00551   1 MKIAVLisGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652    79 ELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDD 158
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|..
gi 20072652   159 TVSTLYNRFLFPEGiKGMVQAV 180
Cdd:pfam00551 161 TAETLYNRVADLEH-KALPRVL 181
FDH_Hydrolase_C cd08703
The C-terminal subdomain of the hydrolase domain on the bi-functional protein ...
 206-306 7.18e-53

The C-terminal subdomain of the hydrolase domain on the bi-functional protein 10-formyltetrahydrofolate dehydrogenase; The family represents the C-terminal subdomain of the hydrolase domain on the bi-functional protein, 10-formyltetrahydrofolate dehydrogenase (FDH). FDH catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. The protein comprises two functional domains: the N-terminal hydrolase domain that removes a formyl group from 10-formyltetrahydrofolate and the C-terminal NADP-dependent dehydrogenase domain that reduces the formyl group to carbon dioxide. The hydrolase domain contains an N-terminal formyl transferase catalytic core subdomain and this C-terminal subdomain, which may be involved in substrate binding.


Pssm-ID: 187731 [Multi-domain]  Cd Length: 100  Bit Score: 173.69  E-value: 7.18e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652 206 KETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLNTSGLVPEGdALPIPGAHRPGVVTKAGLILFGNDDK 285
Cdd:cd08703   1 KELAKINWDQTAEALHNFIRGNDKVPGAWATIDGEQVTLFGSSLWKGGKPPGG-EVEVEGLERPGIVHKNGLLITGSDGK 79

                        90       100
                ....*....|....*....|.
gi 20072652 286 MLLVKNIQLEDGKMILASNFF 306
Cdd:cd08703  80 MVNVKRLQFEDGKMIPASKYG 100
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 1-310 3.92e-51

methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than methionyl-tRNA formyltransferase (fmt) itself are formyltetrahydrofolate dehydrogenases. The mitochondrial methionyl-tRNA formyltransferases are so divergent that, in a multiple alignment of bacterial fmt, mitochondrial fmt, and formyltetrahydrofolate dehydrogenases, the mitochondrial fmt appears the most different. However, because both bacterial and mitochondrial fmt are included in the seed alignment, all credible fmt sequences score higher than any non-fmt sequence. This enzyme modifies Met on initiator tRNA to f-Met. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273088 [Multi-domain]  Cd Length: 313  Bit Score: 176.44  E-value: 3.92e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652     1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDG------KADPLGLEAEKDGVPVFKYsrwraKGQALPDVVAKYQ 74
Cdd:TIGR00460   1 LRIVFFGTPTFSLPVLEELREDNFEVVGVVTQPDKPAgrgkklTPPPVKVLAEEKGIPVFQP-----EKQRQLEELPLVR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652    75 ALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEV 154
Cdd:TIGR00460  76 ELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   155 LPDDTVSTLYNRfLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGAW 234
Cdd:TIGR00460 156 EEEDNSGTLSDK-LSELGAQLLIETLKELPEGKNKPEPQDAEEATYAPKISKEQERIDWNQSAEELLNKIRALNPWPTAW 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   235 TEACEQKLTFFnstlntsglvpEGDALPIPG-AHRPGVV---TKAGLILFGNDDKMLLVKNIQLEDGKMILASNFFKGAA 310
Cdd:TIGR00460 235 LTFEGKNIKIH-----------KAKVIDLSTyKAKPGEIvyhNKKGILVACGKDGILLLLSLQPPGKKVMRAEDFYNGSR 303
ALDH_F1L_FTFDH cd07140
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...
 417-491 1.18e-27

10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.


Pssm-ID: 143458 [Multi-domain]  Cd Length: 486  Bit Score: 115.67  E-value: 1.18e-27
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20072652 417 TVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYR 491
Cdd:cd07140   1 TLKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYR 75
PRK06988 PRK06988
formyltransferase;
46-305 9.12e-27

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 110.17  E-value: 9.12e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   46 AEKDGVPVFKYSrwrakGQALPDVVAKYQALGAELnVLPFCSQF-IPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLI 124
Cdd:PRK06988  51 AAEHGIPVITPA-----DPNDPELRAAVAAAAPDF-IFSFYYRHmIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  125 HGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNrflfpegiKGMVQAVRLIAE-------GKAPRLPQPEEG 197
Cdd:PRK06988 125 NGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTAAQVFD--------KVTVAAEQTLWRvlpallaGEAPHLPNDLAQ 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  198 ATYEGIQKKETAKINWDQPAEAIHNWIRG-NDKVPGAWTEACEQKLTFFNSTLNTSGlvPEGDALPIPGAHrpgVVTKAG 276
Cdd:PRK06988 197 GSYFGGRKPEDGRIDWSKPAAQVYNLIRAvAPPYPGAFTDLGGTRFVVARARLAAPG--AAAARDLPPGLH---VSDNAL 271

                        250       260       270
                 ....*....|....*....|....*....|.
gi 20072652  277 LILFGNDDKMLL--VKNIQLEDGKMILASNF 305
Cdd:PRK06988 272 FGVCGDGRAVSIleLRRQQDGGETVVTPAQF 302
Formyl_trans_C pfam02911
Formyl transferase, C-terminal domain;
205-309 5.76e-18

Formyl transferase, C-terminal domain;


Pssm-ID: 460744 [Multi-domain]  Cd Length: 99  Bit Score: 78.86  E-value: 5.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   205 KKETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLntsglvpegdaLPIPGAHRPG--VVTKAGLILFGN 282
Cdd:pfam02911   3 KKEDGRIDWNQPAEEIHRLIRALDPWPGAYTFLNGKRVKLLKASV-----------LDQESGAAPGtiVTVDKGGLLVAC 71

                          90       100
                  ....*....|....*....|....*..
gi 20072652   283 DDKMLLVKNIQLEDGKMILASNFFKGA 309
Cdd:pfam02911  72 GDGALLILELQLEGKKPMSAEDFLNGF 98
PLN02766 PLN02766
coniferyl-aldehyde dehydrogenase
 414-491 2.97e-09

coniferyl-aldehyde dehydrogenase


Pssm-ID: 215410 [Multi-domain]  Cd Length: 501  Bit Score: 59.06  E-value: 2.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  414 NKRTVRMPH----QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLM 489
Cdd:PLN02766   9 GASGVKVPEikftKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIM 88


                 ..
gi 20072652  490 YR 491
Cdd:PLN02766  89 MK 90
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
 421-492 4.44e-06

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation


Pssm-ID: 440636 [Multi-domain]  Cd Length: 479  Bit Score: 48.97  E-value: 4.44e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20072652 421 PHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRA 492
Cdd:COG1012   5 EYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAF--PAWAATPPAERAAILLRA 74
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
 430-492 1.13e-03

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.


Pssm-ID: 425500 [Multi-domain]  Cd Length: 459  Bit Score: 41.36  E-value: 1.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20072652   430 FVDAEGaKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRA 492
Cdd:pfam00171   1 WVDSES-ETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP--AWRKTPAAERAAILRKA 60
 
Name Accession Description Interval E-value
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 1-203 1.75e-157

10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family represents the N-terminal hydrolase domain of the bifunctional protein 10-formyltetrahydrofolate dehydrogenase (FDH). This domain contains a 10-formyl-tetrahydrofolate (10-formyl-THF) binding site and shares sequence homology and structural topology with other enzymes utilizing this substrate. This domain functions as a hydrolase, catalyzing the conversion of 10-formyl-THF, a precursor for nucleotide biosynthesis, to tetrahydrofolate (THF). The overall FDH reaction mechanism is a coupling of two sequential reactions, a hydrolase and a formyl dehydrogenase, bridged by a substrate transfer step. The N-terminal hydrolase domain removes the formyl group from 10-formyl-THF and the C-terminal NADP-dependent dehydrogenase domain then reduces the formyl group to carbon dioxide. The two catalytic domains are connected by a third intermediate linker domain that transfers the formyl group, covalently attached to the sulfhydryl group of the phosphopantetheine arm, from the N-terminal domain to the C-terminal domain.


Pssm-ID: 187716 [Multi-domain]  Cd Length: 203  Bit Score: 445.74  E-value: 1.75e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGAEL 80
Cdd:cd08647   1 MKIAVIGQSLFGQEVYKELRKEGHEVVGVFTIPDKDGKADPLALEAEKDGVPVFKFPRWRAKGQAIPEVVAKYKALGAEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  81 NVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTV 160
Cdd:cd08647  81 NVLPFCSQFIPMEVIDAPKHGSIIYHPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTV 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 20072652 161 STLYNRFLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGI 203
Cdd:cd08647 161 DTLYNRFLYPEGIKAMVEAVRLIAEGKAPRIPQPEEGATYEGI 203
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
1-309 7.93e-80

Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 251.18  E-value: 7.93e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKD---GK---ADPLGLEAEKDGVPVFKYSRWRAkgqalPDVVAKYQ 74
Cdd:COG0223   1 MRIVFMGTPDFAVPSLEALLAAGHEVVAVVTQPDRPagrGRkltPSPVKELALEHGIPVLQPESLKD-----PEFLEELR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  75 ALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEV 154
Cdd:COG0223  76 ALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPI 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652 155 LPDDTVSTLYNRfLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGAW 234
Cdd:COG0223 156 GPDDTAGSLHDK-LAELGAELLLETLDALEAGTLTPTPQDESGATYAPKISKEDGRIDWSRPAEEIHRLIRALNPWPGAF 234

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20072652 235 TEACEQKLTFFNSTLntsglvpegdaLPIPGAHRPGVVTKAG----LILFGndDKMLLVKNIQLEDGKMILASNFFKGA 309
Cdd:COG0223 235 TTLDGKRLKIWKARV-----------LEEAGGGAPGTILAVDkdglLVACG--DGALRLLELQPAGKKRMSAADFLRGY 300
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 1-180 6.78e-69

Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.


Pssm-ID: 395436 [Multi-domain]  Cd Length: 181  Bit Score: 218.31  E-value: 6.78e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652     1 MKIAVI--GQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGA 78
Cdd:pfam00551   1 MKIAVLisGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652    79 ELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDD 158
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|..
gi 20072652   159 TVSTLYNRFLFPEGiKGMVQAV 180
Cdd:pfam00551 161 TAETLYNRVADLEH-KALPRVL 181
FDH_Hydrolase_C cd08703
The C-terminal subdomain of the hydrolase domain on the bi-functional protein ...
 206-306 7.18e-53

The C-terminal subdomain of the hydrolase domain on the bi-functional protein 10-formyltetrahydrofolate dehydrogenase; The family represents the C-terminal subdomain of the hydrolase domain on the bi-functional protein, 10-formyltetrahydrofolate dehydrogenase (FDH). FDH catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. The protein comprises two functional domains: the N-terminal hydrolase domain that removes a formyl group from 10-formyltetrahydrofolate and the C-terminal NADP-dependent dehydrogenase domain that reduces the formyl group to carbon dioxide. The hydrolase domain contains an N-terminal formyl transferase catalytic core subdomain and this C-terminal subdomain, which may be involved in substrate binding.


Pssm-ID: 187731 [Multi-domain]  Cd Length: 100  Bit Score: 173.69  E-value: 7.18e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652 206 KETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLNTSGLVPEGdALPIPGAHRPGVVTKAGLILFGNDDK 285
Cdd:cd08703   1 KELAKINWDQTAEALHNFIRGNDKVPGAWATIDGEQVTLFGSSLWKGGKPPGG-EVEVEGLERPGIVHKNGLLITGSDGK 79

                        90       100
                ....*....|....*....|.
gi 20072652 286 MLLVKNIQLEDGKMILASNFF 306
Cdd:cd08703  80 MVNVKRLQFEDGKMIPASKYG 100
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 3-182 3.73e-52

Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The proteins of this superfamily contain a formyltransferase domain that hydrolyzes the removal of a formyl group from its substrate as part of a multistep transfer mechanism, and this alignment model represents the catalytic core of the formyltransferase domain. This family includes the following known members; Glycinamide Ribonucleotide Transformylase (GART), Formyl-FH4 Hydrolase, Methionyl-tRNA Formyltransferase, ArnA, and 10-Formyltetrahydrofolate Dehydrogenase (FDH). Glycinamide Ribonucleotide Transformylase (GART) catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Methionyl-tRNA Formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA, which plays important role in translation initiation. ArnA is required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. 10-formyltetrahydrofolate dehydrogenase (FDH) catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. Members of this family are multidomain proteins. The formyltransferase domain is located at the N-terminus of FDH, Methionyl-tRNA Formyltransferase and ArnA, and at the C-terminus of Formyl-FH4 Hydrolase. Prokaryotic Glycinamide Ribonucleotide Transformylase (GART) is a single domain protein while eukaryotic GART is a trifunctional protein that catalyzes the second, third and fifth steps in de novo purine biosynthesis.


Pssm-ID: 187712 [Multi-domain]  Cd Length: 173  Bit Score: 174.40  E-value: 3.73e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   3 IAVIGQSLFGQEVYCHLR-KEGHEVVGVFTVPDKDGKADPLGLEAEKDGVpvfkysrWRAKGQALPDVVAKYQALGAELN 81
Cdd:cd08369   1 IVILGSGNIGQRVLKALLsKEGHEIVGVVTHPDSPRGTAQLSLELVGGKV-------YLDSNINTPELLELLKEFAPDLI 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  82 VLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVS 161
Cdd:cd08369  74 VSINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAG 153

                       170       180
                ....*....|....*....|.
gi 20072652 162 TLYNRfLFPEGIKGMVQAVRL 182
Cdd:cd08369 154 TLYQR-LIELGPKLLKEALQK 173
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 1-310 3.92e-51

methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than methionyl-tRNA formyltransferase (fmt) itself are formyltetrahydrofolate dehydrogenases. The mitochondrial methionyl-tRNA formyltransferases are so divergent that, in a multiple alignment of bacterial fmt, mitochondrial fmt, and formyltetrahydrofolate dehydrogenases, the mitochondrial fmt appears the most different. However, because both bacterial and mitochondrial fmt are included in the seed alignment, all credible fmt sequences score higher than any non-fmt sequence. This enzyme modifies Met on initiator tRNA to f-Met. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273088 [Multi-domain]  Cd Length: 313  Bit Score: 176.44  E-value: 3.92e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652     1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDG------KADPLGLEAEKDGVPVFKYsrwraKGQALPDVVAKYQ 74
Cdd:TIGR00460   1 LRIVFFGTPTFSLPVLEELREDNFEVVGVVTQPDKPAgrgkklTPPPVKVLAEEKGIPVFQP-----EKQRQLEELPLVR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652    75 ALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEV 154
Cdd:TIGR00460  76 ELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   155 LPDDTVSTLYNRfLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGAW 234
Cdd:TIGR00460 156 EEEDNSGTLSDK-LSELGAQLLIETLKELPEGKNKPEPQDAEEATYAPKISKEQERIDWNQSAEELLNKIRALNPWPTAW 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   235 TEACEQKLTFFnstlntsglvpEGDALPIPG-AHRPGVV---TKAGLILFGNDDKMLLVKNIQLEDGKMILASNFFKGAA 310
Cdd:TIGR00460 235 LTFEGKNIKIH-----------KAKVIDLSTyKAKPGEIvyhNKKGILVACGKDGILLLLSLQPPGKKVMRAEDFYNGSR 303
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 1-200 1.77e-46

Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA formyltransferase (Met-tRNA-FMT), N-terminal formyltransferase domain. Met-tRNA-FMT transfers a formyl group from N-10 formyltetrahydrofolate to the amino terminal end of a methionyl-aminoacyl-tRNA acyl moiety, yielding formyl-Met-tRNA. Formyl-Met-tRNA plays essential role in protein translation initiation by forming complex with IF2. The formyl group plays a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. The N-terminal domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187715 [Multi-domain]  Cd Length: 204  Bit Score: 160.69  E-value: 1.77e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKD---GK---ADPLGLEAEKDGVPVFKYSRWRAkgqalPDVVAKYQ 74
Cdd:cd08646   1 MRIVFMGTPDFAVPSLEALLKSGHEVVAVVTQPDKPrgrGKkltPSPVKELALELGLPVLQPEKLKD-----EEFLEELK 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  75 ALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEV 154
Cdd:cd08646  76 ALKPDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPI 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 20072652 155 LPDDTVSTLYNRfLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATY 200
Cdd:cd08646 156 DPDDTAGELLDK-LAELGADLLLEVLDDIEAGKLNPVPQDESEATY 200
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 1-201 9.62e-44

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187724 [Multi-domain]  Cd Length: 192  Bit Score: 153.00  E-value: 9.62e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKAdplgLEAEKDGVPVFKysrwrakGQALPDVVAKYQALGAEL 80
Cdd:cd08822   1 MKIAIAGQKWFGTAVLEALRARGIALLGVAAPEEGDRLA----AAARTAGSRGLP-------RAGVAVLPADAIPPGTDL 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  81 NVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTV 160
Cdd:cd08822  70 IVAAHCHAFISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDTA 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 20072652 161 STLYNRFLFPEGIKGMVQAV-RLIAEGKAPRLPQPEEGATYE 201
Cdd:cd08822 150 AELWRRALAPMGVKLLTQVIdALLRGGNLPAQPQDERLATWE 191
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 2-166 1.31e-31

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187720 [Multi-domain]  Cd Length: 180  Bit Score: 120.06  E-value: 1.31e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   2 KIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADP----LGLEAEKDGVPVFKYSRWRAkgqalPDVVAKYQALG 77
Cdd:cd08651   1 RIVFIGCVEFSLIALEAILEAGGEVVGVITLDDSSSNNDSdyldLDSFARKNGIPYYKFTDIND-----EEIIEWIKEAN 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  78 AELNvlpFC---SQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEV 154
Cdd:cd08651  76 PDII---FVfgwSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPI 152

                       170
                ....*....|..
gi 20072652 155 LPDDTVSTLYNR 166
Cdd:cd08651 153 DKDDTANSLYDK 164
ALDH_F1L_FTFDH cd07140
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...
 417-491 1.18e-27

10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.


Pssm-ID: 143458 [Multi-domain]  Cd Length: 486  Bit Score: 115.67  E-value: 1.18e-27
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20072652 417 TVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYR 491
Cdd:cd07140   1 TLKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYR 75
PRK06988 PRK06988
formyltransferase;
46-305 9.12e-27

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 110.17  E-value: 9.12e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   46 AEKDGVPVFKYSrwrakGQALPDVVAKYQALGAELnVLPFCSQF-IPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLI 124
Cdd:PRK06988  51 AAEHGIPVITPA-----DPNDPELRAAVAAAAPDF-IFSFYYRHmIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  125 HGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNrflfpegiKGMVQAVRLIAE-------GKAPRLPQPEEG 197
Cdd:PRK06988 125 NGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTAAQVFD--------KVTVAAEQTLWRvlpallaGEAPHLPNDLAQ 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  198 ATYEGIQKKETAKINWDQPAEAIHNWIRG-NDKVPGAWTEACEQKLTFFNSTLNTSGlvPEGDALPIPGAHrpgVVTKAG 276
Cdd:PRK06988 197 GSYFGGRKPEDGRIDWSKPAAQVYNLIRAvAPPYPGAFTDLGGTRFVVARARLAAPG--AAAARDLPPGLH---VSDNAL 271

                        250       260       270
                 ....*....|....*....|....*....|.
gi 20072652  277 LILFGNDDKMLL--VKNIQLEDGKMILASNF 305
Cdd:PRK06988 272 FGVCGDGRAVSIleLRRQQDGGETVVTPAQF 302
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 1-202 7.63e-22

ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-L-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal dehydrogenase domain of ArnA catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O), while the N-terminal formyltransferase domain of ArnA catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the catalytic core of the N-terminal formyltransferase domain. The formyltransferase also contains a smaller C-terminal domain the may be involved in substrate binding. ArnA forms a hexameric structure, in which the dehydrogenase domains are arranged at the center of the particle with the transformylase domains on the outside of the particle.


Pssm-ID: 187713 [Multi-domain]  Cd Length: 203  Bit Score: 93.18  E-value: 7.63e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKA---DPLGLEAEKDGVPVFkysrwRAKGQALPDVVAKYQALG 77
Cdd:cd08644   1 MKAVVFAYHEVGYRCLEALLAAGFEVVAVFTHTDNPGENiwfGSVAQLAREHGIPVF-----TPDDINHPEWVERLRALK 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  78 AELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPD 157
Cdd:cd08644  76 PDLIFSFYYRHMISEDILEIARLGAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPD 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 20072652 158 DTVSTLYNRFLFPEGIKgMVQAVRLIAEGKAPRLPQPEEGATYEG 202
Cdd:cd08644 156 DTAKSLFHKLCVAARRL-LARTLPALKAGKARERPQDETQASYFG 199
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 19-248 2.74e-21

bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA;


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 97.36  E-value: 2.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   19 LRKEGHEVVGVFTVPDKDGKADPLG----LEAEKdGVPVF-----KYSRWRAKGQAL-PDVVAK--YQALGAElnvlpfc 86
Cdd:PRK08125  19 LLAAGYEIAAVFTHTDNPGENHFFGsvarLAAEL-GIPVYapedvNHPLWVERIRELaPDVIFSfyYRNLLSD------- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   87 sqfipmEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNR 166
Cdd:PRK08125  91 ------EILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTALTLHHK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  167 FLFPEGiKGMVQAVRLIAEGKAPRLPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRG-NDKVPGAWTEACEQKLTFF 245
Cdd:PRK08125 165 LCHAAR-QLLEQTLPAIKHGNIPEIPQDESQATYFGRRTPADGLIDWHKPASTLHNLVRAvTDPWPGAFSYVGEQKFTVW 243


                 ...
gi 20072652  246 NST 248
Cdd:PRK08125 244 SSR 246
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 25-187 2.09e-19

Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440068 [Multi-domain]  Cd Length: 202  Bit Score: 86.24  E-value: 2.09e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  25 EVVGVFTvpdkDgKADPLGLE-AEKDGVPVF-----KYSRWRAKGQALPDVVAKYQAlgaELNVL---------PFCSQF 89
Cdd:COG0299  30 EIVLVIS----N-RPDAYGLErARAAGIPTFvldhkDFPSREAFDAALLEALDAYGP---DLVVLagfmriltpEFVRAF 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  90 ipmeiisaprHGSII-YHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRFL 168
Cdd:COG0299 102 ----------PGRIInIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDDTEETLAARIL 171

                       170
                ....*....|....*....
gi 20072652 169 fPEGIKGMVQAVRLIAEGK 187
Cdd:COG0299 172 -EQEHRLYPEAIRLLAEGR 189
Formyl_trans_C pfam02911
Formyl transferase, C-terminal domain;
205-309 5.76e-18

Formyl transferase, C-terminal domain;


Pssm-ID: 460744 [Multi-domain]  Cd Length: 99  Bit Score: 78.86  E-value: 5.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   205 KKETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLntsglvpegdaLPIPGAHRPG--VVTKAGLILFGN 282
Cdd:pfam02911   3 KKEDGRIDWNQPAEEIHRLIRALDPWPGAYTFLNGKRVKLLKASV-----------LDQESGAAPGtiVTVDKGGLLVAC 71

                          90       100
                  ....*....|....*....|....*..
gi 20072652   283 DDKMLLVKNIQLEDGKMILASNFFKGA 309
Cdd:pfam02911  72 GDGALLILELQLEGKKPMSAEDFLNGF 98
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 25-233 3.22e-17

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 82.82  E-value: 3.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   25 EVVGVFTVPDKDGK------ADPLGLEAEKDGVP---VFKYSRWRAkgqalPDVVAKYQALGAELNVLPFCSQFIPMEII 95
Cdd:PLN02285  37 EVAAVVTQPPARRGrgrklmPSPVAQLALDRGFPpdlIFTPEKAGE-----EDFLSALRELQPDLCITAAYGNILPQKFL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   96 SAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRfLFPEGIKG 175
Cdd:PLN02285 112 DIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAGPVIAQERVEVDEDIKAPELLPL-LFELGTKL 190

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  176 MVQAVRLIAEGKAPR--LPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGA 233
Cdd:PLN02285 191 LLRELPSVLDGSAKDkaTPQDDSKATHAPKISPEESWLSFDEEARVLHNKVRAFAGWPGT 250
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
 420-491 1.47e-16

ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.


Pssm-ID: 143410  Cd Length: 476  Bit Score: 81.87  E-value: 1.47e-16
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20072652 420 MPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYR 491
Cdd:cd07091   2 QPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNK 73
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 38-174 2.73e-16

Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities.


Pssm-ID: 187714 [Multi-domain]  Cd Length: 183  Bit Score: 76.66  E-value: 2.73e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  38 KADPLGLE-AEKDGVPVF-----KYSRWRAKGQALPDVVAKYQAlgaELNVL---------PFCSQFipmeiisaprHGS 102
Cdd:cd08645  36 NPDAYGLErAKKAGIPTFvinrkDFPSREEFDEALLELLKEYKV---DLIVLagfmrilspEFLEAF----------PGR 102

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20072652 103 II-YHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRF------LFPEGIK 174
Cdd:cd08645 103 IInIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDTPETLAERIhalehrLYPEAIK 181
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 67-181 1.34e-15

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187721 [Multi-domain]  Cd Length: 152  Bit Score: 74.17  E-value: 1.34e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  67 PDVVAKYQALGAELNVLPFCSqFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGD-KKGGFSIFWADDGLDTGD 145
Cdd:cd08653  37 PEVVAALRALAPDVVSVYGCG-IIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGDpDNVGVTVHLVDAGIDTGD 115

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 20072652 146 LLLQKECEVLPDDTVSTLYNRfLFPEGIKGMVQAVR 181
Cdd:cd08653 116 VLAQARPPLAAGDTLLSLYLR-LYRAGVELMVEAIA 150
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 18-163 2.49e-13

N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins involved in the synthesis of Oxazolomycin; This family represents the N-terminal formyl transferase catalytic core domain present in a subgroup of non-ribosomal peptide synthetases. In Streptomyces albus a member of this family has been shown to be involved in the synthesis of oxazolomycin (OZM). OZM is a hybrid peptide-polyketide antibiotic and exhibits potent antitumor and antiviral activities. It is a multi-domain protein consisting of a formyl transferase domain, a Flavin-utilizing monoxygenase domain, a LuxE domain functioning as an acyl protein synthetase and a pp-binding domain, which may function as an acyl carrier. It shows sequence similarity with other peptide-polyketide biosynthesis proteins.


Pssm-ID: 187718 [Multi-domain]  Cd Length: 166  Bit Score: 68.05  E-value: 2.49e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  18 HLRKEGHEVVGVFTvPDkdgkadplgleaekdgvPVFKysRWrAKGQALPdVVAKYQALGAELNVLPFCSQF-------I 90
Cdd:cd08649  17 QLLAAGHRIAAVVS-TD-----------------PAIR--AW-AAAEGIA-VLEPGEALEELLSDEPFDWLFsivnlriL 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20072652  91 PMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTL 163
Cdd:cd08649  75 PSEVLALPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDTALSL 147
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 38-178 2.57e-13

phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 161973 [Multi-domain]  Cd Length: 190  Bit Score: 68.55  E-value: 2.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652    38 KADPLGLE-AEKDGVPVFKYSR--WRAKGQALPDVVAKYQALGAELNVlpfCSQFipMEIISAP---RHGSIIY--HPSL 109
Cdd:TIGR00639  37 KPDAYGLErAAQAGIPTFVLSLkdFPSREAFDQAIIEELRAHEVDLVV---LAGF--MRILGPTflsRFAGRILniHPSL 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20072652   110 LPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRF------LFPEGIKGMVQ 178
Cdd:TIGR00639 112 LPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDTEETLEQRIhkqehrIYPLAIAWFAQ 186
Met_tRNA_FMT_C cd08704
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl ...
 207-302 1.14e-12

C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl transferase and other proteins with diverse enzymatic activities. Proteins found in this family include methionyl-tRNA formyltransferase, ArnA, and 10-formyltetrahydrofolate dehydrogenase. Methionyl-tRNA formyltransferases constitute the majority of the family and also demonstrate greater sequence diversity. Although most proteins with formyltransferase activity contain the C-terminal domain, some formyltransferases ( for example, prokaryotic glycinamide ribonucleotide transformylase (GART)) only have the core catalytic domain, indicating that the C-terminal domain is not a requirement for catalytic activity and may be involved in substrate binding. For example, the C-terminal domain of methionyl-tRNA formyltransferase is involved in the tRNA binding.


Pssm-ID: 187732 [Multi-domain]  Cd Length: 87  Bit Score: 63.70  E-value: 1.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652 207 ETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQKLTFFNSTlntsgLVPEGDALPIPGAhrpGVVTKAGLILFGNDDkM 286
Cdd:cd08704   1 EEGRIDWSKSAEEIHNLIRALNPWPGAYTTLNGKRLKILKAE-----VLEESGEAAPGTI---LAVDKKGLLVACGDG-A 71

                        90
                ....*....|....*.
gi 20072652 287 LLVKNIQLEDGKMILA 302
Cdd:cd08704  72 LEILELQPEGKKRMSA 87
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 84-184 1.03e-11

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187725 [Multi-domain]  Cd Length: 177  Bit Score: 63.62  E-value: 1.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  84 PFCSQF---IPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTV 160
Cdd:cd08823  75 VVVFTFpyrIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFTPIHPDDTY 154

                        90       100
                ....*....|....*....|....
gi 20072652 161 STLYNRfLFPEGIKGMVQAVRLIA 184
Cdd:cd08823 155 GLLCSR-LAMLAVGLLEELYQNLA 177
FMT_core_HypX_N cd08650
HypX protein, N-terminal hydrolase domain; The family represents the N-terminal hydrolase ...
 13-180 6.79e-11

HypX protein, N-terminal hydrolase domain; The family represents the N-terminal hydrolase domain of HypX protein. HypX is involved in the maturation process of active [NiFe] hydrogenase. [NiFe] hydrogenases function in H2 metabolism in a variety of microorganisms, enabling them to use H2 as a source of reducing equivalent under aerobic and anaerobic conditions. [NiFe] hydrogenases consist of a large and a small subunit. The large subunit contains [NiFe] active site, which is synthesized as a precursor without the [NiFe] active site. This precursor then undergoes a complex post-translational maturation process that requires the presence of a number of accessory proteins. HypX has been shown to be involved in this maturation process and have been proposed to participate in the generation and transport of the CO and CN ligands. However, HypX is not present in all hydrogen-metabolizing bacteria. Furthermore, hypX deletion mutants have a reduced but detectable level of hydrogenase activity. Thus, HypX might not be a determining factor in the matur ation process. Members of this group have an N-terminal formyl transferase domain and a C-terminal enoyl-CoA hydratase/isomerase domain.


Pssm-ID: 187719 [Multi-domain]  Cd Length: 151  Bit Score: 60.32  E-value: 6.79e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  13 QEVYCHLRKEGHEVVGVFTVPDkdgkadplglEAEKDGVPVFKysrwrakgqalPDVVakyqalgaelnVLPFCSQFIPM 92
Cdd:cd08650  15 QRAFLELRERGHEVSVEYALSD----------DEMREAVALFA-----------PDLI-----------ICPFLKKRIPE 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  93 EIISapRHGSIIYHPSLlPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRFLFPEG 172
Cdd:cd08650  63 EIWS--NYPCLIVHPGI-VGDRGPSSLDWAILEGEKEWGVTVLQAVEEMDAGPIWATRNFPLRRAATKSSLYRGEVTDAA 139


                ....*...
gi 20072652 173 IKGMVQAV 180
Cdd:cd08650 140 VKAVLEAV 147
ALDH_F2BC cd07142
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...
 421-491 1.66e-09

Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.


Pssm-ID: 143460  Cd Length: 476  Bit Score: 59.82  E-value: 1.66e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20072652 421 PHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYR 491
Cdd:cd07142   3 HTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLR 73
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 85-164 1.75e-09

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187722 [Multi-domain]  Cd Length: 173  Bit Score: 57.07  E-value: 1.75e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  85 FCSQF---IPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVS 161
Cdd:cd08820  74 ISVQYhwiLPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSDCTVI 153


                ...
gi 20072652 162 TLY 164
Cdd:cd08820 154 SLY 156
PLN02766 PLN02766
coniferyl-aldehyde dehydrogenase
 414-491 2.97e-09

coniferyl-aldehyde dehydrogenase


Pssm-ID: 215410 [Multi-domain]  Cd Length: 501  Bit Score: 59.06  E-value: 2.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  414 NKRTVRMPH----QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLM 489
Cdd:PLN02766   9 GASGVKVPEikftKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIM 88


                 ..
gi 20072652  490 YR 491
Cdd:PLN02766  89 MK 90
ALDH_ALD2-YMR170C cd07144
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ...
 415-491 1.09e-08

Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.


Pssm-ID: 143462  Cd Length: 484  Bit Score: 57.42  E-value: 1.09e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20072652 415 KRTVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgRWGKISARDRGRLMYR 491
Cdd:cd07144   1 GKSYDQPTGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFES-WWSKVTGEERGELLDK 76
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
 422-491 2.75e-08

NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.


Pssm-ID: 143459  Cd Length: 481  Bit Score: 56.20  E-value: 2.75e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20072652 422 HQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGR-WGKISARDRGRLMYR 491
Cdd:cd07141   7 TKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSpWRTMDASERGRLLNK 77
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
 423-491 4.15e-08

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259 [Multi-domain]  Cd Length: 538  Bit Score: 55.58  E-value: 4.15e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20072652  423 QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYR 491
Cdd:PLN02466  59 QLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLR 127
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
86-215 4.16e-07

dTDP-4-amino-4,6-dideoxyglucose formyltransferase;


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 51.06  E-value: 4.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   86 CSQFIPMEIISAPRhgSIIYHPSLLPRHRGASAINWTLIHGDKKGGfSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYN 165
Cdd:PRK07579  74 CKQRFPAKLVNGVR--CINIHPGFNPYNRGWFPQVFSIINGLKIGA-TIHEMDEQLDHGPIIAQREVEIESWDSSGSVYA 150

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 20072652  166 RFLFPEgIKGMVQAVRLIAEGKAPRLpQPEEGATYEGIQK-KETAKINWDQ 215
Cdd:PRK07579 151 RVMDIE-RELVLEHFDAIRDGSYTAK-KPATEGNLNSKKDfKQLREIDLDE 199
ALDH_BADH-GbsA cd07119
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...
 425-491 8.09e-07

Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.


Pssm-ID: 143437  Cd Length: 482  Bit Score: 51.54  E-value: 8.09e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20072652 425 FIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYR 491
Cdd:cd07119   1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFR 67
Arna_FMT_C cd08702
C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with ...
 210-305 3.29e-06

C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with 4-amino-4-deoxy-l-arabinose; Domain found in ArnA with similarity to the C-terminal domain of Formyltransferase. ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal domain of ArnA is a dehydrogenase domain that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the N-terminal domain is a formyltransferase domain that catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the C-terminal subdomain of the formyltransferase domain, downstream of the N-terminal subdomain containing the catalytic center. ArnA forms a hexameric structure (a dimer of trimers), in which the dehydrogenase domains are arranged at the center with the transformylase domains on the outside of the complex.


Pssm-ID: 187730  Cd Length: 92  Bit Score: 45.31  E-value: 3.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652 210 KINWDQPAEAIHNWIRG-NDKVPGAWTEACEQKLTFFNSTlntsgLVPEGDALPIPGAhrpgVVTKAG---LILFGndDK 285
Cdd:cd08702   4 LIDWRMSAREIYNLVRAvTKPYPGAFTFVGGQKIKIWKAR-----PVDDAFYNGEPGK----VLSVDGdplIVACG--DG 72

                        90       100
                ....*....|....*....|
gi 20072652 286 MLLVKNIQLEDGKMILASNF 305
Cdd:cd08702  73 ALEILEAELDGGLPLAGEQL 92
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
 421-492 4.44e-06

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation


Pssm-ID: 440636 [Multi-domain]  Cd Length: 479  Bit Score: 48.97  E-value: 4.44e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20072652 421 PHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRA 492
Cdd:COG1012   5 EYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAF--PAWAATPPAERAAILLRA 74
ALDH_AldA_AN0554 cd07143
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ...
 417-491 1.54e-05

Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.


Pssm-ID: 143461  Cd Length: 481  Bit Score: 47.52  E-value: 1.54e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20072652 417 TVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGrWG-KISARDRGRLMYR 491
Cdd:cd07143   2 KYEQPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETD-WGlKVSGSKRGRCLSK 76
PRK13252 PRK13252
betaine aldehyde dehydrogenase; Provisional
 419-492 5.65e-05

betaine aldehyde dehydrogenase; Provisional


Pssm-ID: 183918  Cd Length: 488  Bit Score: 45.64  E-value: 5.65e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20072652  419 RMP-HQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRA 492
Cdd:PRK13252   3 RQPlQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQK--IWAAMTAMERSRILRRA 75
ALDH_F6_MMSDH cd07085
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...
 423-491 6.56e-05

Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.


Pssm-ID: 143404 [Multi-domain]  Cd Length: 478  Bit Score: 45.20  E-value: 6.56e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20072652 423 QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYR 491
Cdd:cd07085   2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFP--AWSATPVLKRQQVMFK 68
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 46-171 1.70e-04

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 42.76  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652   46 AEKDGVPVFKYSRWRAKGQALP--DVVAKYQALGAELNVLPFCSQFIPMEIISA-PRhgSII-YHPSLLPRH--RGASAI 119
Cdd:PLN02331  45 ARENGIPVLVYPKTKGEPDGLSpdELVDALRGAGVDFVLLAGYLKLIPVELVRAyPR--SILnIHPALLPAFggKGYYGI 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 20072652  120 NwtlIH------GDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRFLFPE 171
Cdd:PLN02331 123 K---VHkaviasGARYSGPTVHFVDEHYDTGRILAQRVVPVLATDTPEELAARVLHEE 177
ALDH_ACDHII_AcoD-like cd07559
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...
 422-489 3.12e-04

Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.


Pssm-ID: 143471 [Multi-domain]  Cd Length: 480  Bit Score: 43.10  E-value: 3.12e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20072652 422 HQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLM 489
Cdd:cd07559   1 YDNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK--TWGKTSVAERANIL 66
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
 430-492 1.13e-03

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.


Pssm-ID: 425500 [Multi-domain]  Cd Length: 459  Bit Score: 41.36  E-value: 1.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20072652   430 FVDAEGaKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRA 492
Cdd:pfam00171   1 WVDSES-ETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP--AWRKTPAAERAAILRKA 60
PRK13473 PRK13473
aminobutyraldehyde dehydrogenase;
420-491 1.28e-03

aminobutyraldehyde dehydrogenase;


Pssm-ID: 237391  Cd Length: 475  Bit Score: 41.43  E-value: 1.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20072652  420 MPHQLFIGGEFVDAEGAkTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYR 491
Cdd:PRK13473   1 MQTKLLINGELVAGEGE-KQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFP--EWSQTTPKERAEALLK 69
FMT_core_like_1 cd08821
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 84-225 4.33e-03

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187723 [Multi-domain]  Cd Length: 211  Bit Score: 38.45  E-value: 4.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072652  84 PFCSQFIPMEIISapRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLpdDTVSTL 163
Cdd:cd08821  51 PHWSWIIPKEIFE--NFECVVFHMTDLPYGRGGSPLQNLIVRGHYETKISALKMEKGLDTGPIYLKRDLSLK--GTAEEI 126

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20072652 164 YNRflFPEGIKGMVqaVRLIAEGKAPrLPQPEEGATYEGiQKKETAKINWDQPAEAIHNWIR 225
Cdd:cd08821 127 YER--ASKISLKMI--PELVTKKPKP-IKQEGEPVTFKR-RTPEQSNISNEANLEKIYDFIR 182
ALDH_AldA-Rv0768 cd07139
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...
 424-491 5.43e-03

Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.


Pssm-ID: 143457 [Multi-domain]  Cd Length: 471  Bit Score: 39.10  E-value: 5.43e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20072652 424 LFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYR 491
Cdd:cd07139   1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRR 68
ALDH_AldH-CAJ73105 cd07131
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...
 425-492 9.31e-03

Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.


Pssm-ID: 143449 [Multi-domain]  Cd Length: 478  Bit Score: 38.48  E-value: 9.31e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20072652 425 FIGGEFVDAEGAKTSETINPTDGS-VICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRA 492
Cdd:cd07131   2 YIGGEWVDSASGETFDSRNPADLEeVVGTFPLSTASDVDAAVEAAREAF--PEWRKVPAPRRAEYLFRA 68
 
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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