NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|492542286|ref|WP_005879218|]
View 

MULTISPECIES: glycine cleavage system protein H [Enterococcus]

Protein Classification

glycine cleavage system protein H( domain architecture ID 10160151)

glycine cleavage system protein H plays a role in the degradation of glycine by shuttling the methylamine group of glycine from P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase).

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GCS_H cd06848
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ...
 8-99 2.03e-27

Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue.


:

Pssm-ID: 133457 [Multi-domain]  Cd Length: 96  Bit Score: 96.45  E-value: 2.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542286   8 KKNNLWILFNG-KEYCVGLTNEAQEELGDITFANLPKEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVNEKINEDIN 86
Cdd:cd06848    2 TKDHEWVKVEGdGIATVGITDYAQDLLGDIVFVELPEVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVEVNEALLDNPE 81

                         90
                 ....*....|...
gi 492542286  87 ILNDEDEMNAWIL 99
Cdd:cd06848   82 LINSDPYGEGWLV 94
 
Name Accession Description Interval E-value
GCS_H cd06848
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ...
 8-99 2.03e-27

Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue.


Pssm-ID: 133457 [Multi-domain]  Cd Length: 96  Bit Score: 96.45  E-value: 2.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542286   8 KKNNLWILFNG-KEYCVGLTNEAQEELGDITFANLPKEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVNEKINEDIN 86
Cdd:cd06848    2 TKDHEWVKVEGdGIATVGITDYAQDLLGDIVFVELPEVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVEVNEALLDNPE 81

                         90
                 ....*....|...
gi 492542286  87 ILNDEDEMNAWIL 99
Cdd:cd06848   82 LINSDPYGEGWLV 94
GcvH COG0509
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ...
 9-111 6.53e-26

Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; Glycine cleavage system protein H (lipoate-binding) is part of the Pathway/BioSystem: Glycine cleavage


Pssm-ID: 440275  Cd Length: 128  Bit Score: 93.26  E-value: 6.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542286   9 KNNLWILFNG-KEYCVGLTNEAQEELGDITFANLPKEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVNEKINEDINI 87
Cdd:COG0509   11 EDHEWVRVEGdGTATVGITDFAQDLLGDIVFVELPEVGTEVEAGEPFGVVESVKAVSDLYAPVSGEVVEVNEALEDDPEL 90

                         90       100
                 ....*....|....*....|....
gi 492542286  88 LNDEDEMNAWILSFKEVDPKEFEE 111
Cdd:COG0509   91 VNEDPYGEGWLFKIKPSDPAELDD 114
PRK01202 PRK01202
glycine cleavage system protein GcvH;
13-111 1.03e-23

glycine cleavage system protein GcvH;


Pssm-ID: 234918  Cd Length: 127  Bit Score: 87.91  E-value: 1.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542286  13 WILFNGKEYCVGLTNEAQEELGDITFANLPKEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVNEKINEDINILNDED 92
Cdd:PRK01202  16 WVRVEGDTATVGITDHAQEQLGDIVFVELPEVGDEVKAGETFGVVESVKAASDIYAPVSGEVVEVNEALEDSPELVNEDP 95

                         90
                 ....*....|....*....
gi 492542286  93 EMNAWILSFKEVDPKEFEE 111
Cdd:PRK01202  96 YGEGWLFKIKPSDESELDD 114
GCV_H pfam01597
Glycine cleavage H-protein; This is a family of glycine cleavage H-proteins, part of the ...
 9-112 7.81e-20

Glycine cleavage H-protein; This is a family of glycine cleavage H-proteins, part of the glycine cleavage multienzyme complex (GCV) found in bacteria and the mitochondria of eukaryotes. GCV catalyzes the catabolism of glycine in eukaryotes. A lipoyl group is attached to a completely conserved lysine residue. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.


Pssm-ID: 396258  Cd Length: 122  Bit Score: 77.76  E-value: 7.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542286    9 KNNLWILFNG-KEYCVGLTNEAQEELGDITFANLPKEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVNEKINEDINI 87
Cdd:pfam01597   5 KEHEWVKVEGdGTATVGITDFAQAQLGDIVFVELPEVGTKVKKGESLAAIESVKAASPIYAPVSGEVVEVNEKLEDNPGL 84

                          90       100
                  ....*....|....*....|....*
gi 492542286   88 LNDEDEMNAWILSFKEVDPKEFEEI 112
Cdd:pfam01597  85 INKDPYEDGWIAKLKPSNLEELESL 109
gcvH TIGR00527
glycine cleavage system H protein; This model represents the glycine cleavage system H protein, ...
 13-111 2.74e-18

glycine cleavage system H protein; This model represents the glycine cleavage system H protein, which shuttles the methylamine group of glycine from the P protein to the T protein. The mature protein is about 130 residues long and contains a lipoyl group covalently bound to a conserved Lys residue. The genome of Aquifex aeolicus contains one protein scoring above the trusted cutoff and clustering with other bacterial H proteins, and four more proteins clustering together and scoring below the trusted cutoff; it seems doubtful that all of these homologs are authentic H protein. The Chlamydial homolog of H protein is nearly as divergent as the Aquifex outgroup, is not accompanied by P and T proteins, is not included in the seed alignment, and consequently also scores below the trusted cutoff. [Energy metabolism, Amino acids and amines]


Pssm-ID: 200024  Cd Length: 128  Bit Score: 74.10  E-value: 2.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542286   13 WILFNG-KEYCVGLTNEAQEELGDITFANLPKEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVNEKINEDINILNDE 91
Cdd:TIGR00527  14 WVRVEGdKTATVGITKFAQDELGDIVFVELPEVGAEVAAGESLGSVESVKAASDIYAPVDGTVVEVNTALEDSPELVNED 93

                          90       100
                  ....*....|....*....|
gi 492542286   92 DEMNAWILSFKEVDPKEFEE 111
Cdd:TIGR00527  94 PYGDGWLIKVKLSDGESEVE 113
 
Name Accession Description Interval E-value
GCS_H cd06848
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ...
 8-99 2.03e-27

Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue.


Pssm-ID: 133457 [Multi-domain]  Cd Length: 96  Bit Score: 96.45  E-value: 2.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542286   8 KKNNLWILFNG-KEYCVGLTNEAQEELGDITFANLPKEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVNEKINEDIN 86
Cdd:cd06848    2 TKDHEWVKVEGdGIATVGITDYAQDLLGDIVFVELPEVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVEVNEALLDNPE 81

                         90
                 ....*....|...
gi 492542286  87 ILNDEDEMNAWIL 99
Cdd:cd06848   82 LINSDPYGEGWLV 94
GcvH COG0509
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ...
 9-111 6.53e-26

Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; Glycine cleavage system protein H (lipoate-binding) is part of the Pathway/BioSystem: Glycine cleavage


Pssm-ID: 440275  Cd Length: 128  Bit Score: 93.26  E-value: 6.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542286   9 KNNLWILFNG-KEYCVGLTNEAQEELGDITFANLPKEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVNEKINEDINI 87
Cdd:COG0509   11 EDHEWVRVEGdGTATVGITDFAQDLLGDIVFVELPEVGTEVEAGEPFGVVESVKAVSDLYAPVSGEVVEVNEALEDDPEL 90

                         90       100
                 ....*....|....*....|....
gi 492542286  88 LNDEDEMNAWILSFKEVDPKEFEE 111
Cdd:COG0509   91 VNEDPYGEGWLFKIKPSDPAELDD 114
PRK01202 PRK01202
glycine cleavage system protein GcvH;
13-111 1.03e-23

glycine cleavage system protein GcvH;


Pssm-ID: 234918  Cd Length: 127  Bit Score: 87.91  E-value: 1.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542286  13 WILFNGKEYCVGLTNEAQEELGDITFANLPKEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVNEKINEDINILNDED 92
Cdd:PRK01202  16 WVRVEGDTATVGITDHAQEQLGDIVFVELPEVGDEVKAGETFGVVESVKAASDIYAPVSGEVVEVNEALEDSPELVNEDP 95

                         90
                 ....*....|....*....
gi 492542286  93 EMNAWILSFKEVDPKEFEE 111
Cdd:PRK01202  96 YGEGWLFKIKPSDESELDD 114
GCV_H pfam01597
Glycine cleavage H-protein; This is a family of glycine cleavage H-proteins, part of the ...
 9-112 7.81e-20

Glycine cleavage H-protein; This is a family of glycine cleavage H-proteins, part of the glycine cleavage multienzyme complex (GCV) found in bacteria and the mitochondria of eukaryotes. GCV catalyzes the catabolism of glycine in eukaryotes. A lipoyl group is attached to a completely conserved lysine residue. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.


Pssm-ID: 396258  Cd Length: 122  Bit Score: 77.76  E-value: 7.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542286    9 KNNLWILFNG-KEYCVGLTNEAQEELGDITFANLPKEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVNEKINEDINI 87
Cdd:pfam01597   5 KEHEWVKVEGdGTATVGITDFAQAQLGDIVFVELPEVGTKVKKGESLAAIESVKAASPIYAPVSGEVVEVNEKLEDNPGL 84

                          90       100
                  ....*....|....*....|....*
gi 492542286   88 LNDEDEMNAWILSFKEVDPKEFEEI 112
Cdd:pfam01597  85 INKDPYEDGWIAKLKPSNLEELESL 109
gcvH TIGR00527
glycine cleavage system H protein; This model represents the glycine cleavage system H protein, ...
 13-111 2.74e-18

glycine cleavage system H protein; This model represents the glycine cleavage system H protein, which shuttles the methylamine group of glycine from the P protein to the T protein. The mature protein is about 130 residues long and contains a lipoyl group covalently bound to a conserved Lys residue. The genome of Aquifex aeolicus contains one protein scoring above the trusted cutoff and clustering with other bacterial H proteins, and four more proteins clustering together and scoring below the trusted cutoff; it seems doubtful that all of these homologs are authentic H protein. The Chlamydial homolog of H protein is nearly as divergent as the Aquifex outgroup, is not accompanied by P and T proteins, is not included in the seed alignment, and consequently also scores below the trusted cutoff. [Energy metabolism, Amino acids and amines]


Pssm-ID: 200024  Cd Length: 128  Bit Score: 74.10  E-value: 2.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542286   13 WILFNG-KEYCVGLTNEAQEELGDITFANLPKEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVNEKINEDINILNDE 91
Cdd:TIGR00527  14 WVRVEGdKTATVGITKFAQDELGDIVFVELPEVGAEVAAGESLGSVESVKAASDIYAPVDGTVVEVNTALEDSPELVNED 93

                          90       100
                  ....*....|....*....|
gi 492542286   92 DEMNAWILSFKEVDPKEFEE 111
Cdd:TIGR00527  94 PYGDGWLIKVKLSDGESEVE 113
PRK13380 PRK13380
glycine cleavage system protein H; Provisional
 23-112 4.94e-15

glycine cleavage system protein H; Provisional


Pssm-ID: 237370  Cd Length: 144  Bit Score: 66.18  E-value: 4.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542286  23 VGLTNEAQEELGDITFANLPKEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVNEKINEDINILNDEDEMNAWILSFK 102
Cdd:PRK13380  33 VGITDYAQTMAGDVVFVRLKELGKKVEKGKPVATLESGKWAGPVPAPLTGEVVEVNEALEDSPELVNEDPYGEGWFFRFK 112

                         90
                 ....*....|
gi 492542286 103 EVDPKEFEEI 112
Cdd:PRK13380 113 PANPEELKQL 122
PRK00624 PRK00624
glycine cleavage system protein H; Provisional
 23-102 2.87e-11

glycine cleavage system protein H; Provisional


Pssm-ID: 167014  Cd Length: 114  Bit Score: 55.61  E-value: 2.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542286  23 VGLTNEAQEELGDITFANLPKEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVNEKINEDINILNDEDEMNAWILSFK 102
Cdd:PRK00624  21 LGLTSKMQENLGNILHIDLPSVGSFCKEGEVLVILESSKSAIEVLSPVSGEVIEVNTALEDDIQPINNAPESEGWFVVVQ 100
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 23-80 2.63e-09

Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.


Pssm-ID: 133456 [Multi-domain]  Cd Length: 73  Bit Score: 49.75  E-value: 2.63e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492542286  23 VGLTNEAQEeLGDITFAN-LPKEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVNEK 80
Cdd:cd06663    2 ILIPDLAQH-LGDGTVVKwLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVK 59
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 43-87 4.00e-07

Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 43.93  E-value: 4.00e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 492542286  43 KEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVNEKINEDINI 87
Cdd:cd06849   23 KEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPV 67
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 43-87 4.32e-07

Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 43.90  E-value: 4.32e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 492542286  43 KEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVNEKINEDINI 87
Cdd:COG0508   25 KEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPV 69
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 43-77 2.42e-06

Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.


Pssm-ID: 395290 [Multi-domain]  Cd Length: 73  Bit Score: 41.82  E-value: 2.42e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 492542286   43 KEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSV 77
Cdd:pfam00364  22 KVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEI 56
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 32-85 1.09e-05

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 42.55  E-value: 1.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 492542286   32 ELGDITFAN----LPKEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVNEKINEDI 85
Cdd:TIGR01348 123 DIGDIEKVTvievLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSV 180
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 43-74 1.28e-05

branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 42.47  E-value: 1.28e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 492542286  43 KEGQTFKSGEPLIEVEAEKAVNEFASPLSGTI 74
Cdd:PRK11856  25 KVGDTVKEGQPLAEVETDKATVEIPSPVAGTV 56
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 41-85 2.44e-05

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 41.78  E-value: 2.44e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 492542286   41 LPKEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVNEKINEDI 85
Cdd:TIGR01348  20 LVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTL 64
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 41-74 7.03e-05

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 40.31  E-value: 7.03e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 492542286  41 LPKEGQTFKSGEPLIEVEAEKAVNEFASPLSGTI 74
Cdd:PRK14875  23 LVQEGDEVEKGDELLDVETDKITNEVEAPAAGTL 56
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 43-78 5.35e-04

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 35.47  E-value: 5.35e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 492542286  43 KEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVN 78
Cdd:cd06850   16 KEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEIL 51
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 41-77 9.73e-04

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 37.11  E-value: 9.73e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 492542286  41 LPKEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSV 77
Cdd:PRK11855  22 LVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEI 58
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 32-84 2.13e-03

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 35.95  E-value: 2.13e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 492542286  32 ELGDITFAN----LPKEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVneKINED 84
Cdd:PRK11855 126 DIGEITEVEviewLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEI--KVKVG 180
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 41-84 4.43e-03

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 34.98  E-value: 4.43e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 492542286  41 LPKEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVneKINED 84
Cdd:PRK11854 225 MVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEI--KVNVG 266
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 31-80 5.48e-03

2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]


Pssm-ID: 273565 [Multi-domain]  Cd Length: 403  Bit Score: 34.71  E-value: 5.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 492542286   31 EELGDITFAN-LPKEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVNEK 80
Cdd:TIGR01347  10 ESITEGTVAEwHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFK 60
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
43-80 6.24e-03

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 34.91  E-value: 6.24e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 492542286  43 KEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVNEK 80
Cdd:PRK14040 541 TEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVK 578
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 41-84 6.90e-03

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 34.59  E-value: 6.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 492542286  41 LPKEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSVneKINED 84
Cdd:PRK11854 124 LVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEI--KVNVG 165
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 41-93 7.95e-03

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 34.51  E-value: 7.95e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492542286  41 LPKEGQTFKSGEPLIEVEAEKAVNEFASPLSGTISSV-------NEKINEDINILNDEDE 93
Cdd:PRK11892  23 LKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKIlvpegteGVKVNTPIAVLLEEGE 82
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH