|
Name |
Accession |
Description |
Interval |
E-value |
| SAHH |
cd00401 |
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ... |
11-412 |
0e+00 |
|
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine hydrolase (SAHH, AdoHycase) catalyzes the hydrolysis of S-adenosyl-L-homocysteine (AdoHyc) to form adenosine (Ado) and homocysteine (Hcy). The equilibrium lies far on the side of AdoHyc synthesis, but in nature the removal of Ado and Hyc is sufficiently fast, so that the net reaction is in the direction of hydrolysis. Since AdoHyc is a potent inhibitor of S-adenosyl-L-methionine dependent methyltransferases, AdoHycase plays a critical role in the modulation of the activity of various methyltransferases. The enzyme forms homotetramers, with each monomer binding one molecule of NAD+.
Pssm-ID: 240619 [Multi-domain] Cd Length: 402 Bit Score: 638.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 11 KQGKISYEWARSHMQILDNTINRLKKSKPLKGITLGFCLHITKETSVLLIGAKELGANVACCGGNPLTTQDDIAAFLALQ 90
Cdd:cd00401 1 EFGRKEIEWAEQEMPVLMALRERYAKEKPLKGARIAGCLHMTAQTAVLIETLKALGAEVRWCSCNPLSTQDDVAAALAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 91 GIHTYCWAGQSPKEYDWCIQQVLNHKPQILTDDGSDMNIKAHFDKKYNSLKIFGATEETTAGVNRIRAVEKDGKLRYPVI 170
Cdd:cd00401 81 GIPVFAWKGETEEEYWWCIEQALDHGPNLIIDDGGDLTHLLHTKRPDLLKKIIGGSEETTTGVHRLRAMEKEGKLLFPAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 171 SVNDAYTKHMFDNKYGTGQSTIDGYLRAMNLLLASKRIVVAGYGWVGKGVAANFRGMNAKVIVTEVNPVRALEAHMDGFD 250
Cdd:cd00401 161 AVNDAVTKHKFDNRYGTGQSTIDGIKRATNVLIAGKVVVVAGYGWVGKGCAMRARGLGARVIVTEVDPICALQAAMDGFE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 251 VMPMSQAAKIGEIFITTTGMTSIIRKEHILTMKDGAVLGNVGHFDVEVDSKFLLKQSKSVRRVRPYLDECVLKNGKKVYL 330
Cdd:cd00401 241 VMPMEEAAKIGDIFVTATGNKDVIRGEHFEKMKDGAILCNAGHFDVEIDVAALEELAVEKREIRPQVDEYTLPDGRRIIL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 331 IGEGRIANLTAAEGHPPEVMAQSFSNQLLSILYILKNHNKMPKKVIGVPKEIDKQIAIDALKAMNVKIDKLTKEQIKYMG 410
Cdd:cd00401 321 LAEGRLVNLACATGHPSFVMDMSFANQALAQIELWKNRDKLEPGVYVLPKELDEEVARLKLEALGIKLDKLTEEQAEYLG 400
|
..
gi 663532394 411 SW 412
Cdd:cd00401 401 SW 402
|
|
| SAM1 |
COG0499 |
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism]; |
1-412 |
0e+00 |
|
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
Pssm-ID: 440265 [Multi-domain] Cd Length: 420 Bit Score: 628.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 1 MSKVKNPKLAKQGKISYEWARSHMQILDNTINRLKKSKPLKGITLGFCLHITKETSVLLIGAKELGANVACCGGNPLTTQ 80
Cdd:COG0499 5 DYKVKDISLAEWGRKEIEWAEREMPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGGAEVRWASCNPLSTQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 81 DDIAAFLALQGIHTYCWAGQSPKEYDWCIQQVLNHKPQILTDDGSDMNIKAHfdKKYNSL--KIFGATEETTAGVNRIRA 158
Cdd:COG0499 85 DDVAAALAAAGIPVFAWKGETLEEYYWCIEQALDHGPNIILDDGGDLTLLLH--KERPELlaGIIGGTEETTTGVHRLRA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 159 VEKDGKLRYPVISVNDAYTKHMFDNKYGTGQSTIDGYLRAMNLLLASKRIVVAGYGWVGKGVAANFRGMNAKVIVTEVNP 238
Cdd:COG0499 163 MAKEGALKFPAIAVNDAVTKSLFDNRYGTGQSLLDGIKRATNVLIAGKTVVVAGYGWCGKGVAMRARGLGARVIVTEVDP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 239 VRALEAHMDGFDVMPMSQAAKIGEIFITTTGMTSIIRKEHILTMKDGAVLGNVGHFDVEVDSKFLLKQSKSVRRVRPYLD 318
Cdd:COG0499 243 ICALEAAMDGFRVMPMEEAAKLGDIFVTATGNKDVITAEHFEAMKDGAILANAGHFDVEIDVAALEKLAVEKREIRPQVD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 319 ECVLKNGKKVYLIGEGRIANLTAAEGHPPEVMAQSFSNQLLSILYILKNHNKMPKKVIGVPKEIDKQIAIDALKAMNVKI 398
Cdd:COG0499 323 EYTLPDGRRIYLLAEGRLVNLAAATGHPSEVMDMSFANQALAQIYLVKNGDKLEPGVYVLPKELDEEVARLKLEALGVKI 402
|
410
....*....|....
gi 663532394 399 DKLTKEQIKYMGSW 412
Cdd:COG0499 403 DTLTEEQAEYLGSW 416
|
|
| PRK05476 |
PRK05476 |
S-adenosyl-L-homocysteine hydrolase; Provisional |
1-412 |
0e+00 |
|
S-adenosyl-L-homocysteine hydrolase; Provisional
Pssm-ID: 235488 [Multi-domain] Cd Length: 425 Bit Score: 587.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 1 MSKVKNPKLAKQGKISYEWARSHMQILDNTINRLKKSKPLKGITLGFCLHITKETSVLLIGAKELGANVACCGGNPLTTQ 80
Cdd:PRK05476 7 DYKVADISLADWGRKEIEWAETEMPGLMAIREEFAAEKPLKGARIAGCLHMTIQTAVLIETLKALGAEVRWASCNPFSTQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 81 DDIAAFLALQGIHTYCWAGQSPKEYDWCIQQVLN-HKPQILTDDGSDMNIKAHfdKKYNSL--KIFGATEETTAGVNRIR 157
Cdd:PRK05476 87 DDVAAALAAAGIPVFAWKGETLEEYWECIERALDgHGPNMILDDGGDLTLLVH--TERPELlaNIKGVTEETTTGVHRLY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 158 AVEKDGKLRYPVISVNDAYTKHMFDNKYGTGQSTIDGYLRAMNLLLASKRIVVAGYGWVGKGVAANFRGMNAKVIVTEVN 237
Cdd:PRK05476 165 AMAKDGALKFPAINVNDSVTKSKFDNRYGTGESLLDGIKRATNVLIAGKVVVVAGYGDVGKGCAQRLRGLGARVIVTEVD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 238 PVRALEAHMDGFDVMPMSQAAKIGEIFITTTGMTSIIRKEHILTMKDGAVLGNVGHFDVEVDSKFLLKQSKSVRRVRPYL 317
Cdd:PRK05476 245 PICALQAAMDGFRVMTMEEAAELGDIFVTATGNKDVITAEHMEAMKDGAILANIGHFDNEIDVAALEELAVKWREIKPQV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 318 DECVLKNGKKVYLIGEGRIANLTAAEGHPPEVMAQSFSNQLLSILYILKNHNKMPKKVIGVPKEIDKQIAIDALKAMNVK 397
Cdd:PRK05476 325 DEYTLPDGKRIILLAEGRLVNLGAATGHPSEVMDMSFANQALAQIELFTNRGKLEPGVYVLPKELDEEVARLKLKALGVK 404
|
410
....*....|....*
gi 663532394 398 IDKLTKEQIKYMGSW 412
Cdd:PRK05476 405 LDELTEEQAEYIGVW 419
|
|
| ahcY |
TIGR00936 |
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ... |
11-412 |
0e+00 |
|
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the regeneration of the methyl donor S-adenosylmethionine. Species that lack this enzyme are likely to have adenosylhomocysteine nucleosidase (EC 3.2.2.9), an enzyme which also acts as 5'-methyladenosine nucleosidase (see TIGR01704). [Energy metabolism, Amino acids and amines]
Pssm-ID: 213572 Cd Length: 407 Bit Score: 565.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 11 KQGKISYEWARSHMQILDNTINRLKKSKPLKGITLGFCLHITKETSVLLIGAKELGANVACCGGNPLTTQDDIAAFLA-L 89
Cdd:TIGR00936 1 AEGRKKIEWAEREMPVLMRIRERFSEEKPLKGARIAACLHVTVETAVLIETLVAGGAEVAWTSCNPLSTQDDVAAALAkG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 90 QGIHTYCWAGQSPKEYDWCIQQVLNHKPQILTDDGSDMNIKAHfdKKYNSL--KIFGATEETTAGVNRIRAVEKDGKLRY 167
Cdd:TIGR00936 81 AGIPVFAWRGETNEEYYWAIEQVLDHEPNIIIDDGADLIFLLH--TERPELleKIIGGSEETTTGVIRLRAMEAEGVLKF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 168 PVISVNDAYTKHMFDNKYGTGQSTIDGYLRAMNLLLASKRIVVAGYGWVGKGVAANFRGMNAKVIVTEVNPVRALEAHMD 247
Cdd:TIGR00936 159 PAINVNDAYTKSLFDNRYGTGQSTIDGILRATNLLIAGKTVVVAGYGWCGKGIAMRARGMGARVIVTEVDPIRALEAAMD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 248 GFDVMPMSQAAKIGEIFITTTGMTSIIRKEHILTMKDGAVLGNVGHFDVEVDSKFLLKQSKSVRRVRPYLDECVLKNGKK 327
Cdd:TIGR00936 239 GFRVMTMEEAAKIGDIFITATGNKDVIRGEHFENMKDGAIVANIGHFDVEIDVKALEELAVEKVNVRPQVDEYILKDGRR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 328 VYLIGEGRIANLTAAEGHPPEVMAQSFSNQLLSILYILKNHNKMPKKVIGVPKEIDKQIAIDALKAMNVKIDKLTKEQIK 407
Cdd:TIGR00936 319 IYLLAEGRLVNLAAAEGHPSEVMDMSFANQALAAEYLWKNHDKLEPGVYRLPKELDEMVARLKLEAMGIEIDELTEEQKE 398
|
....*
gi 663532394 408 YMGSW 412
Cdd:TIGR00936 399 YLGSW 403
|
|
| AdoHcyase |
smart00996 |
S-adenosyl-L-homocysteine hydrolase; |
3-410 |
7.53e-126 |
|
S-adenosyl-L-homocysteine hydrolase;
Pssm-ID: 214963 [Multi-domain] Cd Length: 426 Bit Score: 370.34 E-value: 7.53e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 3 KVKNPKLAKQGKISYEWARSHMQILDNTINRLKKSKPLKGITLGFCLHITKETSVLLIGAKELGANVACCGGNPLTTQDD 82
Cdd:smart00996 1 KVADISLADWGRKEIEIAETEMPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 83 IAAFLALQGIHTYCWAGQSPKEYDWCIQQVLNH----KPQILTDDGSDMNIKAHfdKKYNSL--KIFGATEETTAGVNRI 156
Cdd:smart00996 81 AAAAIAAAGVPVFAWKGETLEEYWWCIEQTLTWpdgwGPNMILDDGGDATLLVH--KKYPRMlkKIRGVSEETTTGVHRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 157 RAVEKDGKLRYPVISVNDAYTKHMFDNKYGTGQSTIDGYLRAMNLLLASKRIVVAGYGWVGKGVAANFRGMNAKVIVTEV 236
Cdd:smart00996 159 YQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 237 NPVRALEAHMDGFDVMPMSQAAKIGEIFITTTGMTSIIRKEHILTMKDGAVLGNVGHFDVEVDSKFLLKQSKSVR-RVRP 315
Cdd:smart00996 239 DPICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLRNNPGLKWeNIKP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 316 YLDECVLKNGKKVYLIGEGRIANLTAAEGHPPEVMAQSFSNQLLSILYILKNHNKMPKKVIGVPKEIDKQIAIDALKAMN 395
Cdd:smart00996 319 QVDHITFPDGKRIILLAEGRLVNLGCATGHPSFVMSNSFTNQVLAQIELFTKPGKYKNGVYVLPKKLDEKVARLHLEKLG 398
|
410
....*....|....*
gi 663532394 396 VKIDKLTKEQIKYMG 410
Cdd:smart00996 399 AKLTKLTKEQADYIG 413
|
|
| AdoHcyase |
pfam05221 |
S-adenosyl-L-homocysteine hydrolase; |
3-410 |
1.02e-114 |
|
S-adenosyl-L-homocysteine hydrolase;
Pssm-ID: 461594 Cd Length: 429 Bit Score: 341.73 E-value: 1.02e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 3 KVKNPKLAkqgkisyEWARSHMQI-------LDNTINRLKKSKPLKG--ITlGfCLHITKETSVLLIGAKELGANV--AC 71
Cdd:pfam05221 3 KVADISLA-------DFGRKEIEIaehempgLMALREEYGASKPLKGarIA-G-SLHMTIQTAVLIETLVALGAEVrwAS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 72 CggNPLTTQDDIAAFLALQGIHTYCWAGQSPKEYDWCIQQVLNH-----KPQILTDDGSDMNIKAHfdKKYNSL--KIFG 144
Cdd:pfam05221 74 C--NIFSTQDHAAAAIAAAGVPVFAWKGETLEEYWWCTEQALTWppdggGPNMILDDGGDATLLVH--KKYPRIakGIKG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 145 ATEETTAGVNRIRAVEKDGKLRYPVISVNDAYTKHMFDNKYGTGQSTIDGYLRAMNLLLASKRIVVAGYGWVGKGVAANF 224
Cdd:pfam05221 150 VSEETTTGVHRLYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 225 RGMNAKVIVTEVNPVRALEAHMDGFDVMPMSQAAKIGEIFITTTGMTSIIRKEHILTMKDGAVLGNVGHFDVEVDSKFLL 304
Cdd:pfam05221 230 RGQGARVIVTEIDPICALQAAMEGYEVVTMEDVVGEADIFITTTTNTNVITVEHMDHMKMMAIVCNIGHFDNEIDEIVLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 305 KQSKSVRR-VRPYLDECVLKNGKKVYLIGEGRIANLTAAEGHPPEVMAQSFSNQLLSILYILKNHNKMPKKVIGVPKEID 383
Cdd:pfam05221 310 LLKGVKWVnIKPQVDDITFPDGKSIIVLAEGRLVNLGCATGHPSFVMSNSFTNQVLAQIELWTNDKEYENGVYVLPKKLD 389
|
410 420
....*....|....*....|....*..
gi 663532394 384 KQIAIDALKAMNVKIDKLTKEQIKYMG 410
Cdd:pfam05221 390 EKVARLHLEKLGAKLTELTKEQADYIG 416
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SAHH |
cd00401 |
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ... |
11-412 |
0e+00 |
|
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine hydrolase (SAHH, AdoHycase) catalyzes the hydrolysis of S-adenosyl-L-homocysteine (AdoHyc) to form adenosine (Ado) and homocysteine (Hcy). The equilibrium lies far on the side of AdoHyc synthesis, but in nature the removal of Ado and Hyc is sufficiently fast, so that the net reaction is in the direction of hydrolysis. Since AdoHyc is a potent inhibitor of S-adenosyl-L-methionine dependent methyltransferases, AdoHycase plays a critical role in the modulation of the activity of various methyltransferases. The enzyme forms homotetramers, with each monomer binding one molecule of NAD+.
Pssm-ID: 240619 [Multi-domain] Cd Length: 402 Bit Score: 638.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 11 KQGKISYEWARSHMQILDNTINRLKKSKPLKGITLGFCLHITKETSVLLIGAKELGANVACCGGNPLTTQDDIAAFLALQ 90
Cdd:cd00401 1 EFGRKEIEWAEQEMPVLMALRERYAKEKPLKGARIAGCLHMTAQTAVLIETLKALGAEVRWCSCNPLSTQDDVAAALAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 91 GIHTYCWAGQSPKEYDWCIQQVLNHKPQILTDDGSDMNIKAHFDKKYNSLKIFGATEETTAGVNRIRAVEKDGKLRYPVI 170
Cdd:cd00401 81 GIPVFAWKGETEEEYWWCIEQALDHGPNLIIDDGGDLTHLLHTKRPDLLKKIIGGSEETTTGVHRLRAMEKEGKLLFPAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 171 SVNDAYTKHMFDNKYGTGQSTIDGYLRAMNLLLASKRIVVAGYGWVGKGVAANFRGMNAKVIVTEVNPVRALEAHMDGFD 250
Cdd:cd00401 161 AVNDAVTKHKFDNRYGTGQSTIDGIKRATNVLIAGKVVVVAGYGWVGKGCAMRARGLGARVIVTEVDPICALQAAMDGFE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 251 VMPMSQAAKIGEIFITTTGMTSIIRKEHILTMKDGAVLGNVGHFDVEVDSKFLLKQSKSVRRVRPYLDECVLKNGKKVYL 330
Cdd:cd00401 241 VMPMEEAAKIGDIFVTATGNKDVIRGEHFEKMKDGAILCNAGHFDVEIDVAALEELAVEKREIRPQVDEYTLPDGRRIIL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 331 IGEGRIANLTAAEGHPPEVMAQSFSNQLLSILYILKNHNKMPKKVIGVPKEIDKQIAIDALKAMNVKIDKLTKEQIKYMG 410
Cdd:cd00401 321 LAEGRLVNLACATGHPSFVMDMSFANQALAQIELWKNRDKLEPGVYVLPKELDEEVARLKLEALGIKLDKLTEEQAEYLG 400
|
..
gi 663532394 411 SW 412
Cdd:cd00401 401 SW 402
|
|
| SAM1 |
COG0499 |
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism]; |
1-412 |
0e+00 |
|
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
Pssm-ID: 440265 [Multi-domain] Cd Length: 420 Bit Score: 628.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 1 MSKVKNPKLAKQGKISYEWARSHMQILDNTINRLKKSKPLKGITLGFCLHITKETSVLLIGAKELGANVACCGGNPLTTQ 80
Cdd:COG0499 5 DYKVKDISLAEWGRKEIEWAEREMPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGGAEVRWASCNPLSTQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 81 DDIAAFLALQGIHTYCWAGQSPKEYDWCIQQVLNHKPQILTDDGSDMNIKAHfdKKYNSL--KIFGATEETTAGVNRIRA 158
Cdd:COG0499 85 DDVAAALAAAGIPVFAWKGETLEEYYWCIEQALDHGPNIILDDGGDLTLLLH--KERPELlaGIIGGTEETTTGVHRLRA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 159 VEKDGKLRYPVISVNDAYTKHMFDNKYGTGQSTIDGYLRAMNLLLASKRIVVAGYGWVGKGVAANFRGMNAKVIVTEVNP 238
Cdd:COG0499 163 MAKEGALKFPAIAVNDAVTKSLFDNRYGTGQSLLDGIKRATNVLIAGKTVVVAGYGWCGKGVAMRARGLGARVIVTEVDP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 239 VRALEAHMDGFDVMPMSQAAKIGEIFITTTGMTSIIRKEHILTMKDGAVLGNVGHFDVEVDSKFLLKQSKSVRRVRPYLD 318
Cdd:COG0499 243 ICALEAAMDGFRVMPMEEAAKLGDIFVTATGNKDVITAEHFEAMKDGAILANAGHFDVEIDVAALEKLAVEKREIRPQVD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 319 ECVLKNGKKVYLIGEGRIANLTAAEGHPPEVMAQSFSNQLLSILYILKNHNKMPKKVIGVPKEIDKQIAIDALKAMNVKI 398
Cdd:COG0499 323 EYTLPDGRRIYLLAEGRLVNLAAATGHPSEVMDMSFANQALAQIYLVKNGDKLEPGVYVLPKELDEEVARLKLEALGVKI 402
|
410
....*....|....
gi 663532394 399 DKLTKEQIKYMGSW 412
Cdd:COG0499 403 DTLTEEQAEYLGSW 416
|
|
| PRK05476 |
PRK05476 |
S-adenosyl-L-homocysteine hydrolase; Provisional |
1-412 |
0e+00 |
|
S-adenosyl-L-homocysteine hydrolase; Provisional
Pssm-ID: 235488 [Multi-domain] Cd Length: 425 Bit Score: 587.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 1 MSKVKNPKLAKQGKISYEWARSHMQILDNTINRLKKSKPLKGITLGFCLHITKETSVLLIGAKELGANVACCGGNPLTTQ 80
Cdd:PRK05476 7 DYKVADISLADWGRKEIEWAETEMPGLMAIREEFAAEKPLKGARIAGCLHMTIQTAVLIETLKALGAEVRWASCNPFSTQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 81 DDIAAFLALQGIHTYCWAGQSPKEYDWCIQQVLN-HKPQILTDDGSDMNIKAHfdKKYNSL--KIFGATEETTAGVNRIR 157
Cdd:PRK05476 87 DDVAAALAAAGIPVFAWKGETLEEYWECIERALDgHGPNMILDDGGDLTLLVH--TERPELlaNIKGVTEETTTGVHRLY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 158 AVEKDGKLRYPVISVNDAYTKHMFDNKYGTGQSTIDGYLRAMNLLLASKRIVVAGYGWVGKGVAANFRGMNAKVIVTEVN 237
Cdd:PRK05476 165 AMAKDGALKFPAINVNDSVTKSKFDNRYGTGESLLDGIKRATNVLIAGKVVVVAGYGDVGKGCAQRLRGLGARVIVTEVD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 238 PVRALEAHMDGFDVMPMSQAAKIGEIFITTTGMTSIIRKEHILTMKDGAVLGNVGHFDVEVDSKFLLKQSKSVRRVRPYL 317
Cdd:PRK05476 245 PICALQAAMDGFRVMTMEEAAELGDIFVTATGNKDVITAEHMEAMKDGAILANIGHFDNEIDVAALEELAVKWREIKPQV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 318 DECVLKNGKKVYLIGEGRIANLTAAEGHPPEVMAQSFSNQLLSILYILKNHNKMPKKVIGVPKEIDKQIAIDALKAMNVK 397
Cdd:PRK05476 325 DEYTLPDGKRIILLAEGRLVNLGAATGHPSEVMDMSFANQALAQIELFTNRGKLEPGVYVLPKELDEEVARLKLKALGVK 404
|
410
....*....|....*
gi 663532394 398 IDKLTKEQIKYMGSW 412
Cdd:PRK05476 405 LDELTEEQAEYIGVW 419
|
|
| ahcY |
TIGR00936 |
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ... |
11-412 |
0e+00 |
|
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the regeneration of the methyl donor S-adenosylmethionine. Species that lack this enzyme are likely to have adenosylhomocysteine nucleosidase (EC 3.2.2.9), an enzyme which also acts as 5'-methyladenosine nucleosidase (see TIGR01704). [Energy metabolism, Amino acids and amines]
Pssm-ID: 213572 Cd Length: 407 Bit Score: 565.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 11 KQGKISYEWARSHMQILDNTINRLKKSKPLKGITLGFCLHITKETSVLLIGAKELGANVACCGGNPLTTQDDIAAFLA-L 89
Cdd:TIGR00936 1 AEGRKKIEWAEREMPVLMRIRERFSEEKPLKGARIAACLHVTVETAVLIETLVAGGAEVAWTSCNPLSTQDDVAAALAkG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 90 QGIHTYCWAGQSPKEYDWCIQQVLNHKPQILTDDGSDMNIKAHfdKKYNSL--KIFGATEETTAGVNRIRAVEKDGKLRY 167
Cdd:TIGR00936 81 AGIPVFAWRGETNEEYYWAIEQVLDHEPNIIIDDGADLIFLLH--TERPELleKIIGGSEETTTGVIRLRAMEAEGVLKF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 168 PVISVNDAYTKHMFDNKYGTGQSTIDGYLRAMNLLLASKRIVVAGYGWVGKGVAANFRGMNAKVIVTEVNPVRALEAHMD 247
Cdd:TIGR00936 159 PAINVNDAYTKSLFDNRYGTGQSTIDGILRATNLLIAGKTVVVAGYGWCGKGIAMRARGMGARVIVTEVDPIRALEAAMD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 248 GFDVMPMSQAAKIGEIFITTTGMTSIIRKEHILTMKDGAVLGNVGHFDVEVDSKFLLKQSKSVRRVRPYLDECVLKNGKK 327
Cdd:TIGR00936 239 GFRVMTMEEAAKIGDIFITATGNKDVIRGEHFENMKDGAIVANIGHFDVEIDVKALEELAVEKVNVRPQVDEYILKDGRR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 328 VYLIGEGRIANLTAAEGHPPEVMAQSFSNQLLSILYILKNHNKMPKKVIGVPKEIDKQIAIDALKAMNVKIDKLTKEQIK 407
Cdd:TIGR00936 319 IYLLAEGRLVNLAAAEGHPSEVMDMSFANQALAAEYLWKNHDKLEPGVYRLPKELDEMVARLKLEAMGIEIDELTEEQKE 398
|
....*
gi 663532394 408 YMGSW 412
Cdd:TIGR00936 399 YLGSW 403
|
|
| AdoHcyase |
smart00996 |
S-adenosyl-L-homocysteine hydrolase; |
3-410 |
7.53e-126 |
|
S-adenosyl-L-homocysteine hydrolase;
Pssm-ID: 214963 [Multi-domain] Cd Length: 426 Bit Score: 370.34 E-value: 7.53e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 3 KVKNPKLAKQGKISYEWARSHMQILDNTINRLKKSKPLKGITLGFCLHITKETSVLLIGAKELGANVACCGGNPLTTQDD 82
Cdd:smart00996 1 KVADISLADWGRKEIEIAETEMPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 83 IAAFLALQGIHTYCWAGQSPKEYDWCIQQVLNH----KPQILTDDGSDMNIKAHfdKKYNSL--KIFGATEETTAGVNRI 156
Cdd:smart00996 81 AAAAIAAAGVPVFAWKGETLEEYWWCIEQTLTWpdgwGPNMILDDGGDATLLVH--KKYPRMlkKIRGVSEETTTGVHRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 157 RAVEKDGKLRYPVISVNDAYTKHMFDNKYGTGQSTIDGYLRAMNLLLASKRIVVAGYGWVGKGVAANFRGMNAKVIVTEV 236
Cdd:smart00996 159 YQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 237 NPVRALEAHMDGFDVMPMSQAAKIGEIFITTTGMTSIIRKEHILTMKDGAVLGNVGHFDVEVDSKFLLKQSKSVR-RVRP 315
Cdd:smart00996 239 DPICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLRNNPGLKWeNIKP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 316 YLDECVLKNGKKVYLIGEGRIANLTAAEGHPPEVMAQSFSNQLLSILYILKNHNKMPKKVIGVPKEIDKQIAIDALKAMN 395
Cdd:smart00996 319 QVDHITFPDGKRIILLAEGRLVNLGCATGHPSFVMSNSFTNQVLAQIELFTKPGKYKNGVYVLPKKLDEKVARLHLEKLG 398
|
410
....*....|....*
gi 663532394 396 VKIDKLTKEQIKYMG 410
Cdd:smart00996 399 AKLTKLTKEQADYIG 413
|
|
| PTZ00075 |
PTZ00075 |
Adenosylhomocysteinase; Provisional |
2-410 |
4.63e-123 |
|
Adenosylhomocysteinase; Provisional
Pssm-ID: 240258 Cd Length: 476 Bit Score: 364.75 E-value: 4.63e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 2 SKVKNPKLAKQGKISYEWARSHMQILDNTINRLKKSKPLKGITLGFCLHITKETSVLLIGAKELGANVACCGGNPLTTQD 81
Cdd:PTZ00075 5 YKVKDISLAEFGRKEIELAENEMPGLMALREEYGPSKPLKGARITGCLHMTVQTAVLIETLKALGAEVRWCSCNIFSTQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 82 DIAAFLALQGIHT-YCWAGQSPKEYDWCIQQVLN----HKPQILTDDGSDMNIKAHFDKKYNSL---------------- 140
Cdd:PTZ00075 85 HAAAAIAKAGSVPvFAWKGETLEEYWWCTEQALKwpngDGPNLIVDDGGDATLLVHEGVKAEKLyeekgilpdpldpsne 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 141 -------------------------KIFGATEETTAGVNRIRAVEKDGKLRYPVISVNDAYTKHMFDNKYGTGQSTIDGY 195
Cdd:PTZ00075 165 dekclltvlkklltknpdkwtnlvkKIVGVSEETTTGVHRLYKMLKKGELLFPAINVNDSVTKSKFDNIYGCRHSLIDGI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 196 LRAMNLLLASKRIVVAGYGWVGKGVAANFRGMNAKVIVTEVNPVRALEAHMDGFDVMPMSQAAKIGEIFITTTGMTSIIR 275
Cdd:PTZ00075 245 FRATDVMIAGKTVVVCGYGDVGKGCAQALRGFGARVVVTEIDPICALQAAMEGYQVVTLEDVVETADIFVTATGNKDIIT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 276 KEHILTMKDGAVLGNVGHFDVEVDSKFLLK-QSKSVRRVRPYLDECVLKNGKKVYLIGEGRIANLTAAEGHPPEVMAQSF 354
Cdd:PTZ00075 325 LEHMRRMKNNAIVGNIGHFDNEIQVAELEAyPGIEIVEIKPQVDRYTFPDGKGIILLAEGRLVNLGCATGHPSFVMSNSF 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 663532394 355 SNQLLSILYILKNHN--KMPKKVIGVPKEIDKQIAIDALKAMNVKIDKLTKEQIKYMG 410
Cdd:PTZ00075 405 TNQVLAQIELWENRDtgKYPNGVYKLPKELDEKVARLHLKKLGAKLTKLTDKQAEYIG 462
|
|
| AdoHcyase |
pfam05221 |
S-adenosyl-L-homocysteine hydrolase; |
3-410 |
1.02e-114 |
|
S-adenosyl-L-homocysteine hydrolase;
Pssm-ID: 461594 Cd Length: 429 Bit Score: 341.73 E-value: 1.02e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 3 KVKNPKLAkqgkisyEWARSHMQI-------LDNTINRLKKSKPLKG--ITlGfCLHITKETSVLLIGAKELGANV--AC 71
Cdd:pfam05221 3 KVADISLA-------DFGRKEIEIaehempgLMALREEYGASKPLKGarIA-G-SLHMTIQTAVLIETLVALGAEVrwAS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 72 CggNPLTTQDDIAAFLALQGIHTYCWAGQSPKEYDWCIQQVLNH-----KPQILTDDGSDMNIKAHfdKKYNSL--KIFG 144
Cdd:pfam05221 74 C--NIFSTQDHAAAAIAAAGVPVFAWKGETLEEYWWCTEQALTWppdggGPNMILDDGGDATLLVH--KKYPRIakGIKG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 145 ATEETTAGVNRIRAVEKDGKLRYPVISVNDAYTKHMFDNKYGTGQSTIDGYLRAMNLLLASKRIVVAGYGWVGKGVAANF 224
Cdd:pfam05221 150 VSEETTTGVHRLYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 225 RGMNAKVIVTEVNPVRALEAHMDGFDVMPMSQAAKIGEIFITTTGMTSIIRKEHILTMKDGAVLGNVGHFDVEVDSKFLL 304
Cdd:pfam05221 230 RGQGARVIVTEIDPICALQAAMEGYEVVTMEDVVGEADIFITTTTNTNVITVEHMDHMKMMAIVCNIGHFDNEIDEIVLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 305 KQSKSVRR-VRPYLDECVLKNGKKVYLIGEGRIANLTAAEGHPPEVMAQSFSNQLLSILYILKNHNKMPKKVIGVPKEID 383
Cdd:pfam05221 310 LLKGVKWVnIKPQVDDITFPDGKSIIVLAEGRLVNLGCATGHPSFVMSNSFTNQVLAQIELWTNDKEYENGVYVLPKKLD 389
|
410 420
....*....|....*....|....*..
gi 663532394 384 KQIAIDALKAMNVKIDKLTKEQIKYMG 410
Cdd:pfam05221 390 EKVARLHLEKLGAKLTELTKEQADYIG 416
|
|
| PLN02494 |
PLN02494 |
adenosylhomocysteinase |
3-410 |
1.49e-95 |
|
adenosylhomocysteinase
Pssm-ID: 178111 [Multi-domain] Cd Length: 477 Bit Score: 294.46 E-value: 1.49e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 3 KVKNPKLAKQGKISYEWARSHMQILDNTINRLKKSKPLKGITLGFCLHITKETSVLLIGAKELGANVACCGGNPLTTQDD 82
Cdd:PLN02494 7 KVKDMSQADFGRLEIELAEVEMPGLMACRTEFGPSQPFKGARITGSLHMTIQTAVLIETLTALGAEVRWCSCNIFSTQDH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 83 IAAFLALQGIHTYCWAGQSPKEYDWCIQQVLN----HKPQILTDDGSDMNIKAH--------FDK--------------- 135
Cdd:PLN02494 87 AAAAIARDSAAVFAWKGETLQEYWWCTERALDwgpgGGPDLIVDDGGDATLLIHegvkaeeeFEKdgtlpdptstdnaef 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 136 ----------------KYNSLK--IFGATEETTAGVNRIRAVEKDGKLRYPVISVNDAYTKHMFDNKYGTGQSTIDGYLR 197
Cdd:PLN02494 167 kivltiikdglkvdpkKYHKMKerLVGVSEETTTGVKRLYQMQKNGTLLFPAINVNDSVTKSKFDNLYGCRHSLPDGLMR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 198 AMNLLLASKRIVVAGYGWVGKGVAANFRGMNAKVIVTEVNPVRALEAHMDGFDVMPMSQAAKIGEIFITTTGMTSIIRKE 277
Cdd:PLN02494 247 ATDVMIAGKVAVICGYGDVGKGCAAAMKAAGARVIVTEIDPICALQALMEGYQVLTLEDVVSEADIFVTTTGNKDIIMVD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 278 HILTMKDGAVLGNVGHFDVEVDSKFLLKqSKSVRR--VRPYLDECVLKN-GKKVYLIGEGRIANLTAAEGHPPEVMAQSF 354
Cdd:PLN02494 327 HMRKMKNNAIVCNIGHFDNEIDMLGLET-YPGVKRitIKPQTDRWVFPDtGSGIIVLAEGRLMNLGCATGHPSFVMSCSF 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 663532394 355 SNQLLSILYIL--KNHNKMPKKVIGVPKEIDKQIAIDALKAMNVKIDKLTKEQIKYMG 410
Cdd:PLN02494 406 TNQVIAQLELWneKKSGKYEKKVYVLPKHLDEKVAALHLGKLGAKLTKLSKDQADYIN 463
|
|
| AdoHcyase_NAD |
smart00997 |
S-adenosyl-L-homocysteine hydrolase, NAD binding domain; |
183-344 |
2.92e-88 |
|
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
Pssm-ID: 198065 [Multi-domain] Cd Length: 162 Bit Score: 264.70 E-value: 2.92e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 183 NKYGTGQSTIDGYLRAMNLLLASKRIVVAGYGWVGKGVAANFRGMNAKVIVTEVNPVRALEAHMDGFDVMPMSQAAKIGE 262
Cdd:smart00997 1 NRYGTGESLLDGILRATNVLLAGKNVVVAGYGDVGKGVAARLRGLGARVIVTEIDPIRALEAAMDGFEVMKMEEAAKRAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 263 IFITTTGMTSIIRKEHILTMKDGAVLGNVGHFDVEVDSKFLLKQSKSVRRVRPYLDECVLKNGKKVYLIGEGRIANLTAA 342
Cdd:smart00997 81 IFVTATGNKDVITREHFRAMKDGAILANAGHFDVEIDVAALEELAVEKREVRPQVDEYTLPDGKRIYLLAEGRLVNLAAA 160
|
..
gi 663532394 343 EG 344
Cdd:smart00997 161 TG 162
|
|
| AdoHcyase_NAD |
pfam00670 |
S-adenosyl-L-homocysteine hydrolase, NAD binding domain; |
183-344 |
6.73e-55 |
|
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
Pssm-ID: 395543 [Multi-domain] Cd Length: 162 Bit Score: 179.08 E-value: 6.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 183 NKYGTGQSTIDGYLRAMNLLLASKRIVVAGYGWVGKGVAANFRGMNAKVIVTEVNPVRALEAHMDGFDVMPMSQAAKIGE 262
Cdd:pfam00670 1 NLYGCRESLIDGIKRATDVMIAGKVAVVCGYGDVGKGCAASLKGQGARVIVTEIDPICALQAAMEGFQVVTLEEVVDKAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 263 IFITTTGMTSIIRKEHILTMKDGAVLGNVGHFDVEVDSKFLLKQSKSVRRVRPYLDECVLKNGKKVYLIGEGRIANLTAA 342
Cdd:pfam00670 81 IFVTTTGNKDIITGEHMAKMKNDAIVCNIGHFDNEIDVAWLEANGKKKENIKPQVDRYTLPDGKHIILLAEGRLVNLGCA 160
|
..
gi 663532394 343 EG 344
Cdd:pfam00670 161 TG 162
|
|
| FDH_GDH_like |
cd12154 |
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ... |
60-358 |
1.32e-31 |
|
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related dehydrogenases; The formate/glycerate dehydrogenase like family contains a diverse group of enzymes such as formate dehydrogenase (FDH), glycerate dehydrogenase (GDH), D-lactate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine hydrolase, that share a common 2-domain structure. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar domains of the alpha/beta Rossmann fold NAD+ binding form. The NAD(P) binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD(P) is bound, primarily to the C-terminal portion of the 2nd (internal) domain. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of a hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases.
Pssm-ID: 240631 [Multi-domain] Cd Length: 310 Bit Score: 122.34 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 60 IGAKELGANVACCGGNPLTtqddIAAFLALQGiHTYCWAGQ---------SPKEYDWCIQQVLN-HKPQ--ILTDDGSDM 127
Cdd:cd12154 1 IAGPKEIKNEEFRVGLSPS----VVATLVEAG-HEVRVETGagigagfadQAYVQAGAIVVTLAkALWSldVVLKVKEPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 128 -NIKAHFDKKYNSLKIFgatEETTAGVNRIrAVEKDGKLRYPVISVNDAYTKHMFDNKYGTGQSTIDGYLRAMNLL---- 202
Cdd:cd12154 76 tNAEYALIQKLGDRLLF---TYTIGADHRD-LTEALARAGLTAIAVEGVELPLLTSNSIGAGELSVQFIARFLEVQqpgr 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 203 ------LASKRIVVAGYGWVGKGVAANFRGMNAKVIVTEVNPVRALEAHMDG-FDVMPMSQAAKIGEIFITTTGMTSIIR 275
Cdd:cd12154 152 lggapdVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEQLEELGgKNVEELEEALAEADVIVTTTLLPGKRA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 276 -----KEHILTMKDGAVLGNVGHFDVEVDSKfllkqsksvrrVRPYLdecvLKNGKKVYLIGEGRIANLTAAEGHPPEVM 350
Cdd:cd12154 232 gilvpEELVEQMKPGSVIVNVAVGAVGCVQA-----------LHTQL----LEEGHGVVHYGDVNMPGPGCAMGVPWDAT 296
|
....*...
gi 663532394 351 AQSFSNQL 358
Cdd:cd12154 297 LRLAANTL 304
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
207-299 |
1.21e-06 |
|
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 47.89 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 207 RIVVAGYGWVGKGVAANFRGMNAKVIVTEVNPV--RALEAHMDGFDVMPMSQAAKIGE------IFITT---TGMTS--I 273
Cdd:smart01002 22 KVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPArlRQLESLLGARFTTLYSQAELLEEavkeadLVIGAvliPGAKApkL 101
|
90 100
....*....|....*....|....*.
gi 663532394 274 IRKEHILTMKDGAVLGnvghfDVEVD 299
Cdd:smart01002 102 VTREMVKSMKPGSVIV-----DVAAD 122
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
207-299 |
7.74e-06 |
|
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.
Pssm-ID: 426165 [Multi-domain] Cd Length: 213 Bit Score: 46.72 E-value: 7.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 207 RIVVAGYGWVGKGVAANFRGMNAKVIVTEVNPVRA--LEAHMDGFDVMP-MSQAAKIGE------IFITT---TGMTS-- 272
Cdd:pfam01262 30 KVLVIGGGVAGLNAAATAKGLGAIVTILDVRPARLeqLESILGAKFVETlYSQAELIAEavkeadLVIGTaliPGAKApk 109
|
90 100
....*....|....*....|....*..
gi 663532394 273 IIRKEHILTMKDGAVLgnvghFDVEVD 299
Cdd:pfam01262 110 LVTREMVKSMKPGSVI-----VDVAID 131
|
|
| 2-Hacid_dh_C |
pfam02826 |
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ... |
203-309 |
1.23e-05 |
|
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family pfam00389.
Pssm-ID: 427007 [Multi-domain] Cd Length: 178 Bit Score: 45.56 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 203 LASKRIVVAGYGWVGKGVAANFRGMNAKVIVTEVNPVRALEAHMDGFDVMPMSQAAKIGEIFI-------TTTGMtsiIR 275
Cdd:pfam02826 34 LSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEEEELGARYVSLDELLAESDVVSlhlpltpETRHL---IN 110
|
90 100 110
....*....|....*....|....*....|....
gi 663532394 276 KEHILTMKDGAVLGNVGHFDVeVDSKFLLKQSKS 309
Cdd:pfam02826 111 AERLALMKPGAILINTARGGL-VDEDALIAALKS 143
|
|
| 2-Hacid_dh_6 |
cd12165 |
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ... |
181-292 |
1.57e-05 |
|
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.
Pssm-ID: 240642 [Multi-domain] Cd Length: 314 Bit Score: 46.47 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 181 FDNKYGTGQSTIDGYLRAMNLLLASKRIVVAGYGWVGKGVAANFRGMNAKVIVTEVNPVRALEAHMDGF-----DVMPMS 255
Cdd:cd12165 113 YDNDLRRGIWHGRAGEEPESKELRGKTVGILGYGHIGREIARLLKAFGMRVIGVSRSPKEDEGADFVGTlsdldEALEQA 192
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 663532394 256 QAakigeIFIT------TTGMtsiIRKEHILTMKDGAVLGNVG 292
Cdd:cd12165 193 DV-----VVVAlpltkqTRGL---IGAAELAAMKPGAILVNVG 227
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
207-299 |
3.17e-04 |
|
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.
Pssm-ID: 240630 [Multi-domain] Cd Length: 359 Bit Score: 42.39 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 207 RIVVAGYGWVGKGVAANFRGMNAKVIVTEVNP--VRALEAHMDG------FDVMPMSQAAK-----IGEIFITTTGMTSI 273
Cdd:cd05305 170 KVVILGAGVVGENAARVALGLGAEVTVLDINLerLRYLDDIFGGrvttlySNPANLEEALKeadlvIGAVLIPGAKAPKL 249
|
90 100
....*....|....*....|....*.
gi 663532394 274 IRKEHILTMKDGAVLgnVghfDVEVD 299
Cdd:cd05305 250 VTEEMVKTMKPGSVI--V---DVAID 270
|
|
| PRK13403 |
PRK13403 |
ketol-acid reductoisomerase; Provisional |
195-263 |
6.36e-04 |
|
ketol-acid reductoisomerase; Provisional
Pssm-ID: 106361 [Multi-domain] Cd Length: 335 Bit Score: 41.66 E-value: 6.36e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663532394 195 YLRAMNL-LLASKRIVVAGYGWVGKGVAANFRGMNAKVIVTeVNPVRALE-AHMDGFDVMPMSQAAKIGEI 263
Cdd:PRK13403 5 YEKDANVeLLQGKTVAVIGYGSQGHAQAQNLRDSGVEVVVG-VRPGKSFEvAKADGFEVMSVSEAVRTAQV 74
|
|
| PGDH_2 |
cd05303 |
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ... |
203-309 |
2.58e-03 |
|
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate dehydrogenase (PGDH) catalyzes the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDH comes in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.
Pssm-ID: 240628 [Multi-domain] Cd Length: 301 Bit Score: 39.44 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 203 LASKRIVVAGYGWVGKGVAANFRGMNAKVIVTEVNPVRALEAhMDGFDVMPMS---QAAKIGEIFITTTGMT-SIIRKEH 278
Cdd:cd05303 137 LRGKTLGIIGFGRIGREVAKIARALGMNVIAYDPYPKDEQAV-ELGVKTVSLEellKNSDFISLHVPLTPETkHMINKKE 215
|
90 100 110
....*....|....*....|....*....|.
gi 663532394 279 ILTMKDGAVLGNVGHFDVeVDSKFLLKQSKS 309
Cdd:cd05303 216 LELMKDGAIIINTSRGGV-IDEEALLEALKS 245
|
|
| formate_dh_like |
cd05198 |
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ... |
203-292 |
3.96e-03 |
|
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family; Formate dehydrogenase, D-specific 2-hydroxy acid dehydrogenase, Phosphoglycerate Dehydrogenase, Lactate dehydrogenase, Thermostable Phosphite Dehydrogenase, and Hydroxy(phenyl)pyruvate reductase, among others, share a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase, among others. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.
Pssm-ID: 240622 [Multi-domain] Cd Length: 302 Bit Score: 38.76 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 203 LASKRIVVAGYGWVGKGVAANFRGMNAKVIVTEVNPVRALEAHmDGFDVMPMSQAAKIGEIFI-------TTTGMtsiIR 275
Cdd:cd05198 138 LEGKTVGIVGLGRIGQRVAKRLQAFGMKVLYYDRTRKPEPEED-LGFRVVSLDELLAQSDVVVlhlpltpETRHL---IN 213
|
90
....*....|....*..
gi 663532394 276 KEHILTMKDGAVLGNVG 292
Cdd:cd05198 214 EEELALMKPGAVLVNTA 230
|
|
| 2-Hacid_dh_11 |
cd12175 |
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ... |
203-292 |
5.59e-03 |
|
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.
Pssm-ID: 240652 [Multi-domain] Cd Length: 311 Bit Score: 38.32 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663532394 203 LASKRIVVAGYGWVGKGVAANFRGMNAKVIVTevNPVRALEAHMDGFDVMPMS-----QAAKIGEIFITTTGMTS-IIRK 276
Cdd:cd12175 140 LSGKTVGIVGLGNIGRAVARRLRGFGVEVIYY--DRFRDPEAEEKDLGVRYVEldellAESDVVSLHVPLTPETRhLIGA 217
|
90
....*....|....*.
gi 663532394 277 EHILTMKDGAVLGNVG 292
Cdd:cd12175 218 EELAAMKPGAILINTA 233
|
|
| |
