NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|957949423|gb|ALQ33533|]
View 

fumarate hydratase isoform 6, partial [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Lyase_I_like super family cl00013
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ...
 51-118 1.29e-32

Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase, which catalyze similar beta-elimination reactions; Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively.


The actual alignment was detected with superfamily member cd01362:

Pssm-ID: 469578 [Multi-domain]  Cd Length: 455  Bit Score: 119.91  E-value: 1.29e-32
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 957949423  51 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIAN 118
Cdd:cd01362    1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGG--ERMPRELIRALGLLKKAAAQANAELGlLDEEKAD 67
Lyase_I_like super family cl00013
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ...
 115-155 7.27e-18

Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase, which catalyze similar beta-elimination reactions; Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively.


The actual alignment was detected with superfamily member PRK00485:

Pssm-ID: 469578 [Multi-domain]  Cd Length: 464  Bit Score: 78.98  E-value: 7.27e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 957949423 115 KIANTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 155
Cdd:PRK00485 423 KIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGPG 463
 
Name Accession Description Interval E-value
Fumarase_classII cd01362
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ...
 51-118 1.29e-32

Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial fumarase, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.


Pssm-ID: 176465 [Multi-domain]  Cd Length: 455  Bit Score: 119.91  E-value: 1.29e-32
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 957949423  51 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIAN 118
Cdd:cd01362    1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGG--ERMPRELIRALGLLKKAAAQANAELGlLDEEKAD 67
FumC COG0114
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ...
 49-118 1.40e-31

Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 439884 [Multi-domain]  Cd Length: 461  Bit Score: 117.05  E-value: 1.40e-31
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 957949423  49 SFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIAN 118
Cdd:COG0114    3 ETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGG--ERMPREFIRALALIKKAAARANAELGlLDAEKAD 71
fumC PRK00485
fumarate hydratase; Reviewed
 49-118 4.08e-30

fumarate hydratase; Reviewed


Pssm-ID: 234779 [Multi-domain]  Cd Length: 464  Bit Score: 113.26  E-value: 4.08e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 957949423  49 SFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIAN 118
Cdd:PRK00485   3 ETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGG--ERMPRELIRALALLKKAAARVNAELGlLDAEKAD 71
fumC PRK00485
fumarate hydratase; Reviewed
 115-155 7.27e-18

fumarate hydratase; Reviewed


Pssm-ID: 234779 [Multi-domain]  Cd Length: 464  Bit Score: 78.98  E-value: 7.27e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 957949423 115 KIANTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 155
Cdd:PRK00485 423 KIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGPG 463
Fumarase_classII cd01362
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ...
 115-151 6.41e-15

Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial fumarase, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.


Pssm-ID: 176465 [Multi-domain]  Cd Length: 455  Bit Score: 70.61  E-value: 6.41e-15
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 957949423 115 KIANTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDM 151
Cdd:cd01362  419 KIAKKAHKEGLTLKEAALELGYLTEEEFDRLVDPEKM 455
FumaraseC_C pfam10415
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ...
 115-151 2.56e-14

Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to L-malate as part of the Kreb's cycle. The full-length protein forms a tetramer with visible globular shape. FumaraseC_C is the C-terminal 65 residues referred to as domain 3. The core of the molecule consists of a bundle of 20 alpha-helices from the five-helix bundle of domain 2. The projections from the core of the tetramer are generated from domains 1 and 3 of each subunit. FumaraseC_C does not appear to be part of either the active site or the activation site but is helical in structure forming a little bundle.


Pssm-ID: 463083 [Multi-domain]  Cd Length: 52  Bit Score: 63.11  E-value: 2.56e-14
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 957949423  115 KIANTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDM 151
Cdd:pfam10415  16 EIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
Lyase_1 pfam00206
Lyase;
58-122 1.14e-10

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 58.15  E-value: 1.14e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 957949423   58 GELKVPNDKYYGAQTVRSTMNFKIGGVTermptpvIKAFGILKRAAAEVNQDYgldPKIANTAHK 122
Cdd:pfam00206   1 GRFTVPADALMGIFTDRSRFNFRLGEED-------IKGLAALKKAAAKANVIL---KEEAAAIIK 55
 
Name Accession Description Interval E-value
Fumarase_classII cd01362
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ...
 51-118 1.29e-32

Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial fumarase, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.


Pssm-ID: 176465 [Multi-domain]  Cd Length: 455  Bit Score: 119.91  E-value: 1.29e-32
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 957949423  51 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIAN 118
Cdd:cd01362    1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGG--ERMPRELIRALGLLKKAAAQANAELGlLDEEKAD 67
FumC COG0114
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ...
 49-118 1.40e-31

Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 439884 [Multi-domain]  Cd Length: 461  Bit Score: 117.05  E-value: 1.40e-31
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 957949423  49 SFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIAN 118
Cdd:COG0114    3 ETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGG--ERMPREFIRALALIKKAAARANAELGlLDAEKAD 71
Aspartase_like cd01596
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ...
 51-118 1.88e-30

aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains aspartase (L-aspartate ammonia-lyase), fumarase class II enzymes, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.


Pssm-ID: 176468 [Multi-domain]  Cd Length: 450  Bit Score: 113.67  E-value: 1.88e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 957949423  51 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIAN 118
Cdd:cd01596    1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISG--ERMPPELIRALALVKKAAALANAELGlLDEEKAD 67
fumC PRK00485
fumarate hydratase; Reviewed
 49-118 4.08e-30

fumarate hydratase; Reviewed


Pssm-ID: 234779 [Multi-domain]  Cd Length: 464  Bit Score: 113.26  E-value: 4.08e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 957949423  49 SFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIAN 118
Cdd:PRK00485   3 ETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGG--ERMPRELIRALALLKKAAARVNAELGlLDAEKAD 71
PLN00134 PLN00134
fumarate hydratase; Provisional
 57-118 2.11e-26

fumarate hydratase; Provisional


Pssm-ID: 215069 [Multi-domain]  Cd Length: 458  Bit Score: 102.85  E-value: 2.11e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 957949423  57 FGELKVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIAN 118
Cdd:PLN00134   1 MGPIQVPADKLWGAQTQRSLQNFEIGGERERMPEPIVRAFGIVKKAAAKVNMEYGlLDPDIGK 63
AspA COG1027
Aspartate ammonia-lyase [Amino acid transport and metabolism];
51-118 9.18e-19

Aspartate ammonia-lyase [Amino acid transport and metabolism];


Pssm-ID: 440650 [Multi-domain]  Cd Length: 460  Bit Score: 81.64  E-value: 9.18e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 957949423  51 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIAN 118
Cdd:COG1027    1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPISDHPELIRALAMVKKAAALANRELGlLDKEKAD 69
Aspartase cd01357
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ...
 51-118 1.72e-18

Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), Bacillus aspartase and related proteins. It is a member of the Lyase class I family, which includes both aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid.


Pssm-ID: 176462 [Multi-domain]  Cd Length: 450  Bit Score: 80.64  E-value: 1.72e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 957949423  51 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIAN 118
Cdd:cd01357    1 RIEHDLLGEREVPADAYYGIQTLRALENFPISG--LKIHPELIRALAMVKKAAALANAELGlLDEEKAE 67
aspA PRK12273
aspartate ammonia-lyase; Provisional
 48-118 1.77e-18

aspartate ammonia-lyase; Provisional


Pssm-ID: 237031 [Multi-domain]  Cd Length: 472  Bit Score: 80.94  E-value: 1.77e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 957949423  48 NSFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIAN 118
Cdd:PRK12273   3 MNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKISDYPELIRALAMVKKAAALANKELGlLDEEKAD 74
fumC PRK00485
fumarate hydratase; Reviewed
 115-155 7.27e-18

fumarate hydratase; Reviewed


Pssm-ID: 234779 [Multi-domain]  Cd Length: 464  Bit Score: 78.98  E-value: 7.27e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 957949423 115 KIANTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 155
Cdd:PRK00485 423 KIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGPG 463
PRK13353 PRK13353
aspartate ammonia-lyase; Provisional
 47-119 3.78e-17

aspartate ammonia-lyase; Provisional


Pssm-ID: 183992 [Multi-domain]  Cd Length: 473  Bit Score: 76.95  E-value: 3.78e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 957949423  47 QNSFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVteRMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANT 119
Cdd:PRK13353   2 NKNMRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGY--KIHPELIRAFAQVKKAAALANADLGlLPRRIAEA 73
PRK12425 PRK12425
class II fumarate hydratase;
51-117 1.19e-16

class II fumarate hydratase;


Pssm-ID: 171490 [Multi-domain]  Cd Length: 464  Bit Score: 75.73  E-value: 1.19e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 957949423  51 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIA 117
Cdd:PRK12425   3 RTETDSLGPIEVPEDAYWGAQTQRSLINFAIGK--ERMPLAVLHALALIKKAAARVNDRNGdLPADIA 68
PLN00134 PLN00134
fumarate hydratase; Provisional
 115-154 4.80e-15

fumarate hydratase; Provisional


Pssm-ID: 215069 [Multi-domain]  Cd Length: 458  Bit Score: 70.87  E-value: 4.80e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 957949423 115 KIANTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGP 154
Cdd:PLN00134 415 AVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTGP 454
Fumarase_classII cd01362
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ...
 115-151 6.41e-15

Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial fumarase, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.


Pssm-ID: 176465 [Multi-domain]  Cd Length: 455  Bit Score: 70.61  E-value: 6.41e-15
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 957949423 115 KIANTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDM 151
Cdd:cd01362  419 KIAKKAHKEGLTLKEAALELGYLTEEEFDRLVDPEKM 455
FumaraseC_C pfam10415
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ...
 115-151 2.56e-14

Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to L-malate as part of the Kreb's cycle. The full-length protein forms a tetramer with visible globular shape. FumaraseC_C is the C-terminal 65 residues referred to as domain 3. The core of the molecule consists of a bundle of 20 alpha-helices from the five-helix bundle of domain 2. The projections from the core of the tetramer are generated from domains 1 and 3 of each subunit. FumaraseC_C does not appear to be part of either the active site or the activation site but is helical in structure forming a little bundle.


Pssm-ID: 463083 [Multi-domain]  Cd Length: 52  Bit Score: 63.11  E-value: 2.56e-14
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 957949423  115 KIANTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDM 151
Cdd:pfam10415  16 EIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
PRK14515 PRK14515
aspartate ammonia-lyase; Provisional
 47-111 1.68e-12

aspartate ammonia-lyase; Provisional


Pssm-ID: 237743 [Multi-domain]  Cd Length: 479  Bit Score: 63.87  E-value: 1.68e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 957949423  47 QNSFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVteRMPTPVIKAFGILKRAAAEVNQDYG 111
Cdd:PRK14515   8 KNGVRIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGY--KIHEGLIKAFAIVKKAAALANTDVG 70
PRK12425 PRK12425
class II fumarate hydratase;
115-154 5.81e-12

class II fumarate hydratase;


Pssm-ID: 171490 [Multi-domain]  Cd Length: 464  Bit Score: 62.25  E-value: 5.81e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 957949423 115 KIANTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGP 154
Cdd:PRK12425 421 EIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENMLEA 460
Lyase_1 pfam00206
Lyase;
58-122 1.14e-10

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 58.15  E-value: 1.14e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 957949423   58 GELKVPNDKYYGAQTVRSTMNFKIGGVTermptpvIKAFGILKRAAAEVNQDYgldPKIANTAHK 122
Cdd:pfam00206   1 GRFTVPADALMGIFTDRSRFNFRLGEED-------IKGLAALKKAAAKANVIL---KEEAAAIIK 55
Aspartase_like cd01596
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ...
 115-147 1.16e-09

aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains aspartase (L-aspartate ammonia-lyase), fumarase class II enzymes, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.


Pssm-ID: 176468 [Multi-domain]  Cd Length: 450  Bit Score: 55.51  E-value: 1.16e-09
                         10        20        30
                 ....*....|....*....|....*....|...
gi 957949423 115 KIANTAHKNGSTLKETAIELGYLTAEQFDEWVK 147
Cdd:cd01596  418 EIAKEALKEGRTLREAALELGLLTEEELDEILD 450
aspA PRK12273
aspartate ammonia-lyase; Provisional
 115-155 6.20e-04

aspartate ammonia-lyase; Provisional


Pssm-ID: 237031 [Multi-domain]  Cd Length: 472  Bit Score: 38.95  E-value: 6.20e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 957949423 115 KIANTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 155
Cdd:PRK12273 425 EIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTHPG 465
 
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