|
Name |
Accession |
Description |
Interval |
E-value |
| TrpB |
COG0133 |
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta ... |
19-453 |
0e+00 |
|
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta chain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439903 Cd Length: 400 Bit Score: 674.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 19 DGRFGEYGGQYVPEALVPALSELADAYQRYVIDNEdgFRDELREHLQTFAGRPTPLQRADRLSERYDR-EIYLKREDLVH 97
Cdd:COG0133 11 KGYFGEFGGRFVPETLMPALDELEEAYEKAKNDPE--FQAELDYLLKDYVGRPTPLYFAERLSEKLGGaKIYLKREDLNH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 98 GGAHKLNNALGQVLLAKYMGKERVIAETGAGQHGTATAMAAAHLDMPCEIYMGRTDVNRQRPNVYRMRMSGAEVTPVDAG 177
Cdd:COG0133 89 TGAHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVVYMGEEDIERQALNVFRMKLLGAEVVPVTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 178 SATLKEAINETMRDWAGSVETTHYAVGSVVGPHPFPAMVRDFQAVIGEEIRAQIRDEIGRLPDSVVACAGGGSNTMGTFD 257
Cdd:COG0133 169 SRTLKDAVNEALRDWVTNVDDTHYLIGSVVGPHPYPMMVRDFQSVIGREAREQILEKEGRLPDAVVACVGGGSNAIGIFY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 258 AFVDHterraeddsrgrspqedtEGVALHAVEAGGSDLGVDEetgvapNSASLSTGTDGVLHGALTKLLQTADGQVVESH 337
Cdd:COG0133 249 PFLDD------------------ESVRLIGVEAGGKGLETGE------HAATLTKGRPGVLHGARTYLLQDEDGQILETH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 338 SVSAGLDYAGVGPELANLVDRGRVTPATVDDKAALEAFHRLSRLEGIIPALESSHALGYIEERLgavggtssaddddsET 417
Cdd:COG0133 305 SISAGLDYPGVGPEHAYLKDTGRAEYVSVTDDEALEAFQLLSRTEGIIPALESAHALAYALKLA--------------PE 370
|
410 420 430
....*....|....*....|....*....|....*.
gi 433291063 418 PRPDddddlgEVIVVTVSGRGDKDLETVLEETERRD 453
Cdd:COG0133 371 LSKD------QIIVVNLSGRGDKDVDTVAKYLGLED 400
|
|
| PRK04346 |
PRK04346 |
tryptophan synthase subunit beta; Validated |
19-450 |
0e+00 |
|
tryptophan synthase subunit beta; Validated
Pssm-ID: 235288 Cd Length: 397 Bit Score: 666.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 19 DGRFGEYGGQYVPEALVPALSELADAYQRYviDNEDGFRDELREHLQTFAGRPTPLQRADRLSERY-DREIYLKREDLVH 97
Cdd:PRK04346 8 NGYFGEFGGRFVPETLMPALEELEEAYEKA--KNDPEFQAELDYLLKNYVGRPTPLYFAERLSEHLgGAKIYLKREDLNH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 98 GGAHKLNNALGQVLLAKYMGKERVIAETGAGQHGTATAMAAAHLDMPCEIYMGRTDVNRQRPNVYRMRMSGAEVTPVDAG 177
Cdd:PRK04346 86 TGAHKINNVLGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVIYMGAEDVERQALNVFRMKLLGAEVVPVTSG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 178 SATLKEAINETMRDWAGSVETTHYAVGSVVGPHPFPAMVRDFQAVIGEEIRAQIRDEIGRLPDSVVACAGGGSNTMGTFD 257
Cdd:PRK04346 166 SRTLKDAVNEALRDWVTNVEDTHYLIGSVAGPHPYPTMVRDFQSVIGEEAKAQILEKEGRLPDAVVACVGGGSNAIGIFH 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 258 AFVDHterraeddsrgrspqedtEGVALHAVEAGGsdLGVDeeTGvaPNSASLSTGTDGVLHGALTKLLQTADGQVVESH 337
Cdd:PRK04346 246 PFIDD------------------ESVRLIGVEAAG--KGLE--TG--KHAATLTKGRPGVLHGAKTYLLQDEDGQILETH 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 338 SVSAGLDYAGVGPELANLVDRGRVTPATVDDKAALEAFHRLSRLEGIIPALESSHALGYIEERlgavggtssaddddSET 417
Cdd:PRK04346 302 SISAGLDYPGVGPEHAYLKDIGRAEYVSITDDEALEAFQLLSRLEGIIPALESSHALAYALKL--------------APT 367
|
410 420 430
....*....|....*....|....*....|...
gi 433291063 418 PRPDDdddlgeVIVVTVSGRGDKDLETVLEETE 450
Cdd:PRK04346 368 LGKDQ------IIVVNLSGRGDKDVFTVAKLLG 394
|
|
| trpB |
TIGR00263 |
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the ... |
20-447 |
0e+00 |
|
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the biosynthesis of tryptophan. the beta chain contains the functional domain for or the synthesis of tryptophan from indole and serine. The enzyme requires pyridoxal-phosphate as a cofactor. The pyridoxal-P attachment site is contained within the conserved region [LIVM]-x-H-x-G-[STA]-H-K-x-N] [K is the pyridoxal-P attachment site] which is present between residues 90-100 of the model. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 272987 Cd Length: 385 Bit Score: 582.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 20 GRFGEYGGQYVPEALVPALSELADAYQRYVIDneDGFRDELREHLQTFAGRPTPLQRADRLSERYD-REIYLKREDLVHG 98
Cdd:TIGR00263 1 GYFGDFGGQYVPETLMPALEELEAAFEDAKAD--PAFWAELNELLRNYAGRPTPLTFAPNLTEALGgAKIYLKREDLNHT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 99 GAHKLNNALGQVLLAKYMGKERVIAETGAGQHGTATAMAAAHLDMPCEIYMGRTDVNRQRPNVYRMRMSGAEVTPVDAGS 178
Cdd:TIGR00263 79 GAHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLDCEVYMGAEDVERQKPNVFRMELLGAKVIPVTSGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 179 ATLKEAINETMRDWAGSVETTHYAVGSVVGPHPFPAMVRDFQAVIGEEIRAQIRDEIGRLPDSVVACAGGGSNTMGTFDA 258
Cdd:TIGR00263 159 GTLKDAVNEALRDWVTSVDDTHYVLGSAVGPHPFPTMVRDFQSVIGEEAKEQILEQEGRLPDAVIACVGGGSNAIGIFYA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 259 FVdhterraeddsrgrspqeDTEGVALHAVEAGGsdLGVDEetgvAPNSASLSTGTDGVLHGALTKLLQTADGQVVESHS 338
Cdd:TIGR00263 239 FI------------------DDPSVQLIGVEAGG--LGIDT----HKHAATLSKGSPGVLHGMKTYLLQDEDGQILEAHS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 339 VSAGLDYAGVGPELANLVDRGRVTPATVDDKAALEAFHRLSRLEGIIPALESSHALGYIEerlgavggtssaddddSETP 418
Cdd:TIGR00263 295 VSAGLDYPGVGPEHAYLHETGRATYEAITDDEALEAFKLLSRNEGIIPALESSHALAHLE----------------KIAP 358
|
410 420
....*....|....*....|....*....
gi 433291063 419 RPDDDDdlgeVIVVTVSGRGDKDLETVLE 447
Cdd:TIGR00263 359 TLPKDQ----IVVVNLSGRGDKDIFTIAK 383
|
|
| PRK13028 |
PRK13028 |
tryptophan synthase subunit beta; Provisional |
18-447 |
0e+00 |
|
tryptophan synthase subunit beta; Provisional
Pssm-ID: 183851 Cd Length: 402 Bit Score: 569.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 18 TDGRFGEYGGQYVPEALVPALSELADAYQRYVidNEDGFRDELREHLQTFAGRPTPLQRADRLSERYD-REIYLKREDLV 96
Cdd:PRK13028 11 ADGFFGEYGGQFVPPELKPALDELEAAYEEIK--KDPDFIAELRYLLKHYVGRPTPLYHAKRLSEELGgAQIYLKREDLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 97 HGGAHKLNNALGQVLLAKYMGKERVIAETGAGQHGTATAMAAAHLDMPCEIYMGRTDVNRQRPNVYRMRMSGAEVTPVDA 176
Cdd:PRK13028 89 HTGAHKINNCLGQALLAKRMGKKRLIAETGAGQHGVATATAAALFGLECEIYMGEVDIERQHPNVFRMKLLGAEVVPVTR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 177 GSATLKEAINETMRDWAGSVETTHYAVGSVVGPHPFPAMVRDFQAVIGEEIRAQIRDEIGRLPDSVVACAGGGSNTMGTF 256
Cdd:PRK13028 169 GGRTLKEAVDSAFEDYLKDPDNTHYAIGSVVGPHPFPMMVRDFQSVIGEEAREQFLEMTGRLPDAVVACVGGGSNAIGLF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 257 DAFVdhterraeddsrgrspqeDTEGVALHAVEAGGSDLGVDEetgvapNSASLSTGTDGVLHGALTKLLQTADGQVVES 336
Cdd:PRK13028 249 SAFL------------------DDESVRLVGVEPAGRGLDLGE------HAATLTLGKPGVIHGFKSYVLQDEDGEPAPV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 337 HSVSAGLDYAGVGPELANLVDRGRVTPATVDDKAALEAFHRLSRLEGIIPALESSHALGYieerlgAVGGTSSADDDDSe 416
Cdd:PRK13028 305 HSIAAGLDYPGVGPEHAYLKDIGRVEYVTATDEEALDAFFLLSRTEGIIPALESSHAVAY------AIKLAPELSKDET- 377
|
410 420 430
....*....|....*....|....*....|.
gi 433291063 417 tprpdddddlgevIVVTVSGRGDKDLETVLE 447
Cdd:PRK13028 378 -------------ILVNLSGRGDKDIDYVAE 395
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
36-445 |
0e+00 |
|
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions.
Pssm-ID: 107207 Cd Length: 365 Bit Score: 545.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 36 PALSELADAYQRYVIDNEdgFRDELREHLQTFAGRPTPLQRADRLSERYDR-EIYLKREDLVHGGAHKLNNALGQVLLAK 114
Cdd:cd06446 1 PALEELEQEFSKERYDPD--FPEELRELYKDYVGRPTPLYRAKRLSEYLGGaKIYLKREDLNHTGAHKINNALGQALLAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 115 YMGKERVIAETGAGQHGTATAMAAAHLDMPCEIYMGRTDVNRQRPNVYRMRMSGAEVTPVDAGSATLKEAINETMRDWAG 194
Cdd:cd06446 79 RMGKKRVIAETGAGQHGVATATACALFGLECEIYMGAVDVERQPLNVFRMELLGAEVVPVPSGSGTLKDAISEAIRDWVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 195 SVETTHYAVGSVVGPHPFPAMVRDFQAVIGEEIRAQIRDEIGRLPDSVVACAGGGSNTMGTFDAFVDHterraeddsrgr 274
Cdd:cd06446 159 NVEDTHYLLGSVVGPHPYPNMVRDFQSVIGEEAKKQILEKEGELPDVVIACVGGGSNAAGLFYPFIND------------ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 275 spqedtEGVALHAVEAGGSDLGVDEEtgvapnSASLSTGTDGVLHGALTKLLQTADGQVVESHSVSAGLDYAGVGPELAN 354
Cdd:cd06446 227 ------KDVKLIGVEAGGCGLETGGH------AAYLFGGTAGVLHGLKMYTLQDEDGQIVPPHSISAGLDYPGVGPEHAY 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 355 LVDRGRVTPATVDDKAALEAFHRLSRLEGIIPALESSHALGYIEErlgavggtssaddddsETPRPDDDddlgEVIVVTV 434
Cdd:cd06446 295 LKDSGRVEYVAVTDEEALEAFKLLARTEGIIPALESSHAIAYAIK----------------LAKKLGKE----KVIVVNL 354
|
410
....*....|.
gi 433291063 435 SGRGDKDLETV 445
Cdd:cd06446 355 SGRGDKDLQTV 365
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
20-447 |
1.93e-178 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 513.20 E-value: 1.93e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 20 GRFGEYGGQYVPEALVPALSELADAYQRYVIDNEdgFRDELREHLQTFAGRPTPLQRADRLSERYDREIYLKREDLVHGG 99
Cdd:PRK13803 222 GRYGTFGGAYVPETLMANLQELQESYTKIIKSNE--FQKTFKRLLQNYAGRPTPLTEAKRLSDIYGARIYLKREDLNHTG 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 100 AHKLNNALGQVLLAKYMGKERVIAETGAGQHGTATAMAAAHLDMPCEIYMGRTDVNRQRPNVYRMRMSGAEVTPVDAGSA 179
Cdd:PRK13803 300 SHKINNALGQALLAKRMGKTRIIAETGAGQHGVATATACALFGLKCTIFMGEEDIKRQALNVERMKLLGANVIPVLSGSK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 180 TLKEAINETMRDWAGSVETTHYAVGSVVGPHPFPAMVRDFQAVIGEEIRAQIRDEIGRLPDSVVACAGGGSNTMGTFDAF 259
Cdd:PRK13803 380 TLKDAVNEAIRDWVASVPDTHYLIGSAVGPHPYPEMVAYFQSVIGEEAKEQLKEQTGKLPDAIIACVGGGSNAIGIFYHF 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 260 VDhterraeDDSrgrspqedtegVALHAVEAGGSDLGVDEetgvapNSASLSTGTDGVLHGALTKLLQTADGQVVESHSV 339
Cdd:PRK13803 460 LD-------DPS-----------VKLIGVEAGGKGVNTGE------HAATIKKGRKGVLHGSMTYLMQDENGQILEPHSI 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 340 SAGLDYAGVGPELANLVDRGRVTPATVDDKAALEAFHRLSRLEGIIPALESSHALGYIEErlgaVGGTSSADDddsetpr 419
Cdd:PRK13803 516 SAGLDYPGIGPMHANLFETGRAIYTSVTDEEALDAFKLLAKLEGIIPALESSHALAYLKE----GRKKFKKKD------- 584
|
410 420
....*....|....*....|....*...
gi 433291063 420 pdddddlgeVIVVTVSGRGDKDLETVLE 447
Cdd:PRK13803 585 ---------IVIVNLSGRGDKDIPTLKE 603
|
|
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
20-446 |
5.90e-161 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 461.15 E-value: 5.90e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 20 GRFGEYGGQYVPEALVPALSELADAYQRYVIDNEdgFRDELREHLQTFAGRPTPLQRADRLSERYDR------EIYLKRE 93
Cdd:PLN02618 17 GRFGKFGGKYVPETLMTALSELEAAFNALATDPE--FQEELAGILKDYVGRETPLYFAERLTEHYKRadgegpEIYLKRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 94 DLVHGGAHKLNNALGQVLLAKYMGKERVIAETGAGQHGTATAMAAAHLDMPCEIYMGRTDVNRQRPNVYRMRMSGAEVTP 173
Cdd:PLN02618 95 DLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIVYMGAQDMERQALNVFRMRLLGAEVRP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 174 VDAGSATLKEAINETMRDWAGSVETTHYAVGSVVGPHPFPAMVRDFQAVIGEEIRAQIRDEIGRLPDSVVACAGGGSNTM 253
Cdd:PLN02618 175 VHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHSVIGKETRRQAMEKWGGKPDVLVACVGGGSNAM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 254 GTFDAFVDHTERRaeddsrgrspqedtegvaLHAVEAGGSDLGVDEetgvapNSASLSTGTDGVLHGALTKLLQTADGQV 333
Cdd:PLN02618 255 GLFHEFIDDEDVR------------------LIGVEAAGFGLDSGK------HAATLTKGEVGVLHGAMSYLLQDEDGQI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 334 VESHSVSAGLDYAGVGPELANLVDRGRVTPATVDDKAALEAFHRLSRLEGIIPALESSHALGYIEERLGAVggtssaddd 413
Cdd:PLN02618 311 IEPHSISAGLDYPGVGPEHSFLKDTGRAEYYSVTDEEALEAFQRLSRLEGIIPALETSHALAYLEKLCPTL--------- 381
|
410 420 430
....*....|....*....|....*....|...
gi 433291063 414 dsetprPDddddlGEVIVVTVSGRGDKDLETVL 446
Cdd:PLN02618 382 ------PD-----GTKVVVNCSGRGDKDVNTAI 403
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
22-444 |
5.57e-127 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 384.38 E-value: 5.57e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 22 FGEYGGQYVPEALVPALSELADAYQRYVIDNEdgFRDELREHLQTFAGRPTPLQRADRLSER------YDREIYLKREDL 95
Cdd:PRK13802 279 WGQFGGRYVPEALITALDELERVYTQAKADPE--FHKELATLNQRYVGRPSPLTEAPRFAERvkektgLDARVFLKREDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 96 VHGGAHKLNNALGQVLLAKYMGKERVIAETGAGQHGTATAMAAAHLDMPCEIYMGRTDVNRQRPNVYRMRMSGAEVTPVD 175
Cdd:PRK13802 357 NHTGAHKINNALGQALLVKRMGKTRVIAETGAGQHGVATATVCAMLGLKCRIYMGQIDARRQALNVARMRMLGAEVVEVT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 176 AGSATLKEAINETMRDWAGSVETTHYAVGSVVGPHPFPAMVRDFQAVIGEEIRAQIRDEIG-RLPDSVVACAGGGSNTMG 254
Cdd:PRK13802 437 LGDRILKDAINEALRDWVTNVKDTHYLLGTVAGPHPFPAMVRDFQKIIGEEAKQQLQDWYGiDHPDAICACVGGGSNAIG 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 255 TFDAFVdhterraeDDSRgrspqedtegVALHAVEAGGSdlgvDEETGVAPNSASLSTGTDGVLHGALTKLLQTADGQVV 334
Cdd:PRK13802 517 VMNAFL--------DDER----------VNLYGYEAGGN----GPESGKHAIRFAPGTGELGMFQGAKSYLLENDEGQTL 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 335 ESHSVSAGLDYAGVGPELANLVDRGRVTPATVDDKAALEAFHRLSRLEGIIPALESSHALGyieerlGAVGGTSSADDDD 414
Cdd:PRK13802 575 DTYSISAGLDYASVGPEHAWLKDIGRVNYSWATDEEAMNAFKDLCETEGIIPAIESSHAVA------GAYKAAADLKAKG 648
|
410 420 430
....*....|....*....|....*....|
gi 433291063 415 SETPrpdddddlgeVIVVTVSGRGDKDLET 444
Cdd:PRK13802 649 YEHP----------VMIVNISGRGDKDMNT 668
|
|
| PRK12391 |
PRK12391 |
TrpB-like pyridoxal phosphate-dependent enzyme; |
58-442 |
1.12e-54 |
|
TrpB-like pyridoxal phosphate-dependent enzyme;
Pssm-ID: 237087 Cd Length: 427 Bit Score: 188.08 E-value: 1.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 58 DELREHLQtfAGRPTPLQRADRLsERYDR---EIYLKREDLVHGGAHKLNNALGQVLLAKYMGKERVIAETGAGQHGTAT 134
Cdd:PRK12391 66 EEVREIYR--LWRPTPLIRARRL-EKALGtpaKIYYKYEGVSPTGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWGSAL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 135 AMAAAHLDMPCEIYMGRTDVNrQRPnvYR---MRMSGAEVTP-----VDAGSATLKE----------AINETMRDWAGSv 196
Cdd:PRK12391 143 ALACALFGLECTVFMVRVSYE-QKP--YRrslMETYGAEVIPspsdlTEAGRKILAEdpdhpgslgiAISEAVEDAAKR- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 197 ETTHYAVGSVVgPHpfpamVRDFQAVIGEEIRAQIrDEIGRLPDSVVACAGGGSNTMGTFDAFVdhterraEDDSRGRsp 276
Cdd:PRK12391 219 PDTKYALGSVL-NH-----VLLHQTVIGLEAKKQL-ELAGEYPDVVIGCVGGGSNFAGLAFPFL-------GDKLEGK-- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 277 qEDTEGValhAVEaggsdlgvdeetgvapnSASLSTGTDGVL---HG---ALTKLLQ--TADGQVVESHSVSAGLDYAGV 348
Cdd:PRK12391 283 -KDTRFI---AVE-----------------PAACPTLTKGEYaydFGdtaGLTPLLKmyTLGHDFVPPPIHAGGLRYHGM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 349 GPELANLVDRGRVTPATVDDKAALEAFHRLSRLEGIIPALESSHAL-GYIEERLGAvggtssaddddSETPRPdddddlg 427
Cdd:PRK12391 342 APLVSLLVHEGLIEARAYPQTEVFEAAVLFARTEGIVPAPESSHAIaAAIDEALKA-----------KEEGEE------- 403
|
410
....*....|....*
gi 433291063 428 EVIVVTVSGRGDKDL 442
Cdd:PRK12391 404 KVILFNLSGHGLLDL 418
|
|
| COG1350 |
COG1350 |
Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) [Amino acid transport ... |
58-442 |
3.87e-50 |
|
Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) [Amino acid transport and metabolism]; Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440961 Cd Length: 433 Bit Score: 176.47 E-value: 3.87e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 58 DELREHLQTFagRPTPLQRADRLSERYDR--EIYLKREDLVHGGAHKLNNALGQVLLAKYMGKERVIAETGAGQHGTATA 135
Cdd:COG1350 67 EEVREIYRLW--RPSPLYRARRLEKALGTpaKIYYKYEGVSPAGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWGSALS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 136 MAAAHLDMPCEIYMGRTDVNrQRPnvYR---MRMSGAEVTP-----VDAGSATLKE----------AINETMRDWAGSvE 197
Cdd:COG1350 145 FACALFGLECTVYMVKVSYE-QKP--YRrsmMETYGAEVIPspsdlTEAGRKILAEdpdtpgslgiAISEAVEDAATR-D 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 198 TTHYAVGSV---VGPHpfpamvrdfQAVIGEEIRAQIrDEIGRLPDSVVACAGGGSNTMGTFDAFVdhterraEDDSRGR 274
Cdd:COG1350 221 DTKYALGSVlnhVLLH---------QTVIGLEAKKQL-EKAGEYPDVVIGCAGGGSNFAGLAFPFL-------RDKLRGK 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 275 SpqeDTEGVAlhaveaggsdlgvdeetgVAPnsASLSTGTDGVL---HG---ALTKLLQ--TADGQVVESHSVSAGLDYA 346
Cdd:COG1350 284 K---DVRFIA------------------VEP--AACPTLTRGVYaydFGdtaGLTPLLKmyTLGHDFIPPPIHAGGLRYH 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 347 GVGPELANLVDRGRVTPATVDDKAALEAFHRLSRLEGIIPALESSHAL-GYIEERLGAvggtssaddddSETprpddddd 425
Cdd:COG1350 341 GMAPLVSQLYHDGLIEAVAYPQLEVFEAGVLFARTEGIVPAPESAHAIkAAIDEALKC-----------KEE-------- 401
|
410
....*....|....*....
gi 433291063 426 lGE--VIVVTVSGRGDKDL 442
Cdd:COG1350 402 -GEekTILFNLSGHGHFDL 419
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
72-437 |
7.15e-49 |
|
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.
Pssm-ID: 107202 [Multi-domain] Cd Length: 244 Bit Score: 167.31 E-value: 7.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 72 TPLQRADRLSERYDREIYLKREDLVHGGAHKLNNALGQVLLAKYMGKER--VIAETGAGQHGTATAMAAAHLDMPCEIYM 149
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPkgVIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 150 GRTDvnrQRPNVYRMRMSGAEVTPVDAGsatLKEAINETMRDWAgSVETTHYAVGSVvgpHPfpaMVRDFQAVIGEEIRA 229
Cdd:cd00640 81 PEGA---SPEKVAQMRALGAEVVLVPGD---FDDAIALAKELAE-EDPGAYYVNQFD---NP---ANIAGQGTIGLEILE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 230 QIRdeiGRLPDSVVACAGGGSNTMGTFDAFvdhterraeddsrgrspQEDTEGVALHAVEAGgsdlgvdeetgvapnsas 309
Cdd:cd00640 148 QLG---GQKPDAVVVPVGGGGNIAGIARAL-----------------KELLPNVKVIGVEPE------------------ 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 310 lstgtdgvlhgaltkllqtadgqVVeshsvsagldyagvgpelanlvdrgrvtpaTVDDKAALEAFHRLSRLEGIIPALE 389
Cdd:cd00640 190 -----------------------VV------------------------------TVSDEEALEAIRLLAREEGILVEPS 216
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 433291063 390 SSHALGYIEERLgavggtssaddddsetprpdDDDDLGEVIVVTVSGR 437
Cdd:cd00640 217 SAAALAAALKLA--------------------KKLGKGKTVVVILTGG 244
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
66-406 |
7.91e-36 |
|
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.
Pssm-ID: 459749 [Multi-domain] Cd Length: 295 Bit Score: 134.36 E-value: 7.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 66 TFAGRPTPLQRADRLSERYDREIYLKREDLVHGGAHKLNNALGQVLLAKYMGKERVIAETGAGQHGTATAMAAAHLDMPC 145
Cdd:pfam00291 2 SLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 146 EIYMGRTDVNRqrpNVYRMRMSGAEVTPVDAGSATLKEAINETMRDWAGSVETTHYAvgsvvgpHPFpamVRDFQAVIGE 225
Cdd:pfam00291 82 TIVVPEDAPPG---KLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGAYYINQYD-------NPL---NIEGYGTIGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 226 EIRAQirdeIGRLPDSVVACAGGGSNTMGTFDAFvdhterraeddsrgrspQEDTEGVALHAVEAGGSDLGVDeetgvap 305
Cdd:pfam00291 149 EILEQ----LGGDPDAVVVPVGGGGLIAGIARGL-----------------KELGPDVRVIGVEPEGAPALAR------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 306 nsaSLSTGTDGVLHGALTkllqTADGqvveshsVSAGLDyagVGPELANLVDRGRVTPATVDDKAALEAFHRLSRLEGII 385
Cdd:pfam00291 201 ---SLAAGRPVPVPVADT----IADG-------LGVGDE---PGALALDLLDEYVGEVVTVSDEEALEAMRLLARREGIV 263
|
330 340
....*....|....*....|..
gi 433291063 386 PALESSHAL-GYIEERLGAVGG 406
Cdd:pfam00291 264 VEPSSAAALaALKLALAGELKG 285
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
67-256 |
6.32e-19 |
|
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family [Amino acid transport and metabolism];
Pssm-ID: 442005 [Multi-domain] Cd Length: 317 Bit Score: 87.16 E-value: 6.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 67 FAGRPTPLQRADRLSERYDREIYLKREDLVH---GG--AHKLNNALGQvllAKYMGKERVIAeTGAGQ--HGTATAMAAA 139
Cdd:COG2515 7 LAFLPTPLQPLPRLSAALGVELWIKRDDLTGpaiGGnkTRKLEYLLAD---ALAQGADTLVT-FGGAQsnHARATAAAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 140 HLDMPCEIYMGRTDVNRQRPNVYRMRMSGAEVTPVDAGSATLKeaiNETMRDWAGSVET---THYAV---GSvvGPHPFP 213
Cdd:COG2515 83 KLGLKCVLVLRGEEPTPLNGNLLLDRLLGAELHFVSRGEYRDR---DEAMEAVAAELRArggKPYVIpegGS--NPLGAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 433291063 214 AMVRdfqavIGEEIRAQIRdEIGRLPDSVVACAGggsnTMGTF 256
Cdd:COG2515 158 GYVE-----AAAELAAQLA-ELGVDFDYIVVASG----SGGTL 190
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
59-250 |
4.11e-16 |
|
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 440784 [Multi-domain] Cd Length: 327 Bit Score: 78.92 E-value: 4.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 59 ELREHLQTFAgRPTPLQRADRLSERYDREIYLKREDLVHGGAHKLNNALgqVLLAKYMGKER---VIAETgAGQHGTATA 135
Cdd:COG1171 13 AAAARIAGVV-RRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAY--NALASLSEEERargVVAAS-AGNHAQGVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 136 MAAAHLDMPCEIYMGRTdVNRQRpnVYRMRMSGAEVTPVDagsATLKEAINETMRDwagsVETTHYAVgsVvgpHPF-PA 214
Cdd:COG1171 89 YAARLLGIPATIVMPET-APAVK--VAATRAYGAEVVLHG---DTYDDAEAAAAEL----AEEEGATF--V---HPFdDP 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 433291063 215 MVRDFQAVIGEEIRAQIRDeigrlPDSVVACAGGGS 250
Cdd:COG1171 154 DVIAGQGTIALEILEQLPD-----LDAVFVPVGGGG 184
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
70-249 |
5.02e-16 |
|
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. Although the nitrogen atoms of most amino acids are transferred to alpha-ketoglutarate before removal, the alpha-amino group of threonine can be directly converted into NH4+. The direct deamination is catalyzed by threonine dehydratase, in which pyridoxal phosphate (PLP) is the prosthetic group. Threonine dehydratase is widely distributed in all three major phylogenetic divisions.
Pssm-ID: 107205 [Multi-domain] Cd Length: 304 Bit Score: 78.30 E-value: 5.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 70 RPTPLQRADRLSERYDREIYLKREDLVHGGAHKLNNALGQVLLAKYMGKER-VIAETgAGQHGTATAMAAAHLDMPCEIY 148
Cdd:cd01562 16 RRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKgVVAAS-AGNHAQGVAYAAKLLGIPATIV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 149 MGRTDVnrqRPNVYRMRMSGAEVTPVDagsATLKEAINETMRDwagSVETTHYAVgsvvgpHPF--PAMVRDfQAVIGEE 226
Cdd:cd01562 95 MPETAP---AAKVDATRAYGAEVVLYG---EDFDEAEAKAREL---AEEEGLTFI------HPFddPDVIAG-QGTIGLE 158
|
170 180
....*....|....*....|...
gi 433291063 227 IRAQIRDeigrlPDSVVACAGGG 249
Cdd:cd01562 159 ILEQVPD-----LDAVFVPVGGG 176
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
71-249 |
2.60e-12 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 68.29 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 71 PTPLQRADRLSERYDREIYLKREDLVHGGAHKLN---NALGQVLLAKymgKERVIAETGAGQHGTATAMAAAHLDMPCEI 147
Cdd:PRK08639 25 ETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRgayNAISQLSDEE---LAAGVVCASAGNHAQGVAYACRHLGIPGVI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 148 YMGRTdVNRQRpnVYRMRMSGAEVTPVDAGSATLKEAINETMRDwagsVETTHyavGSVVgpHPFP-AMVRDFQAVIGEE 226
Cdd:PRK08639 102 FMPVT-TPQQK--IDQVRFFGGEFVEIVLVGDTFDDSAAAAQEY----AEETG---ATFI--PPFDdPDVIAGQGTVAVE 169
|
170 180
....*....|....*....|...
gi 433291063 227 IRAQIRDEigRLPDSVVACAGGG 249
Cdd:PRK08639 170 ILEQLEKE--GSPDYVFVPVGGG 190
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
56-463 |
1.86e-11 |
|
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis
Pssm-ID: 440264 [Multi-domain] Cd Length: 394 Bit Score: 65.61 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 56 FRDElrEHLQTFAGRPTPLQRADRLSERYDREIYLKREDLVHGGAHKlnnALG-QVL--LAKYMGKERVIAETgAGQHGT 132
Cdd:COG0498 53 FDDE--EKAVSLGEGGTPLVKAPRLADELGKNLYVKEEGHNPTGSFK---DRAmQVAvsLALERGAKTIVCAS-SGNGSA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 133 ATAMAAAHLDMPCEIYMGRTDVN----RQrpnvyrMRMSGAEVTPV-----DAGSAtLKEAINEtmRDWagsvetthYAV 203
Cdd:COG0498 127 ALAAYAARAGIEVFVFVPEGKVSpgqlAQ------MLTYGAHVIAVdgnfdDAQRL-VKELAAD--EGL--------YAV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 204 GSVvgpHPFpamVRDFQAVIGEEIRAQirdeIGRLPDSVVACAGGGSNTMGTFDAFvdhtERRAEDDSRGRSPQedtegv 283
Cdd:COG0498 190 NSI---NPA---RLEGQKTYAFEIAEQ----LGRVPDWVVVPTGNGGNILAGYKAF----KELKELGLIDRLPR------ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 284 aLHAVEAggsdlgvdeeTGVAPNSASLSTGTDGVlhgaltkllqtadgQVVESHSVSAGLD--YAGVGPELANLVDRGRV 361
Cdd:COG0498 250 -LIAVQA----------TGCNPILTAFETGRDEY--------------EPERPETIAPSMDigNPSNGERALFALRESGG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 362 TPATVDDKAALEAFHRLSRLEGII--PAlesshalgyieerlGAVgGTSSADDDDSETPRPDDdddlgEVIVVTVSGRGD 439
Cdd:COG0498 305 TAVAVSDEEILEAIRLLARREGIFvePA--------------TAV-AVAGLRKLREEGEIDPD-----EPVVVLSTGHGL 364
|
410 420
....*....|....*....|....
gi 433291063 440 KDLETVLEETERRDLEAAPDVEVF 463
Cdd:COG0498 365 KFPDAVREALGGEPLAVPPDLEAV 388
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
40-249 |
3.94e-10 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 60.86 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 40 ELADAYQRyvidnedgfrdeLREHLqtfagRPTPLQRADRLSERYDREIYLKREDLVHGGAHKLNNALGQVLLAKYMGKE 119
Cdd:PRK06815 6 AILEAHQR------------LRPQV-----RVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 120 RVIAETGAGQHGTATAMAAAHLDMPCEIYmgrTDVNRQRPNVYRMRMSGAEVT--PVDAGSATLkEAINETMRdwAGSVE 197
Cdd:PRK06815 69 QGVITASSGNHGQGVALAAKLAGIPVTVY---APEQASAIKLDAIRALGAEVRlyGGDALNAEL-AARRAAEQ--QGKVY 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 433291063 198 TTHYAVGSVVGPhpfpamvrdfQAVIGEEIRAQIRDeigrlPDSVVACAGGG 249
Cdd:PRK06815 143 ISPYNDPQVIAG----------QGTIGMELVEQQPD-----LDAVFVAVGGG 179
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
67-253 |
5.72e-09 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 57.53 E-value: 5.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 67 FAGRPTPLQRADRLSERYDREIYLKREDLVH---GG--AHKLNNALGQVLLAKYmgkeRVIAETGAGQ--HGTATAMAAA 139
Cdd:PRK03910 11 LAGLPTPLEPLPRLSAALGPDIYIKRDDLTGlalGGnkTRKLEFLLADALAQGA----DTLITAGAIQsnHARQTAAAAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 140 HLDMPCEIYM-----GRTDVNRQRPNVYRMRMSGAEVTPVDAGSatlkeAINETMRDWAGSVE---TTHYAV---GS-VV 207
Cdd:PRK03910 87 KLGLKCVLLLenpvpTEAENYLANGNVLLDDLFGAEIHVVPAGT-----DMDAQLEELAEELRaqgRRPYVIpvgGSnAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 433291063 208 GPHPFPAMvrdfqaviGEEIRAQIrDEIGRLPDSVVaCAGGGSNTM 253
Cdd:PRK03910 162 GALGYVAC--------ALEIAQQL-AEGGVDFDAVV-VASGSGGTH 197
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
72-258 |
1.60e-08 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 56.32 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 72 TPLQRADRLSERYDREIYLKREDLVHGGAHKLNNALGQVLLAKYMGK--ERVIAETgAGQHGTATAMAAAHLDMPCEIYM 149
Cdd:PRK06608 24 TPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKlpDKIVAYS-TGNHGQAVAYASKLFGIKTRIYL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 150 GRT--DVNRQRPNVYrmrmsGAEVTPVDagsaTLKEAINETMRDWAgsvETTHYAvgsvvgpHPFpamvrDFQAVIGEE- 226
Cdd:PRK06608 103 PLNtsKVKQQAALYY-----GGEVILTN----TRQEAEEKAKEDEE---QGFYYI-------HPS-----DSDSTIAGAg 158
|
170 180 190
....*....|....*....|....*....|...
gi 433291063 227 -IRAQIRDEIGRLPDSVVACAGGGSNTMGTFDA 258
Cdd:PRK06608 159 tLCYEALQQLGFSPDAIFASCGGGGLISGTYLA 191
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
70-152 |
2.60e-08 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 55.96 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 70 RPTPLQRADRLSERYDREIYLKREDLVHGGAHKLNNALGQVLLAKYMGKERVIAETGAGQHGTATAMAAAHLDMPCEIYM 149
Cdd:PRK12483 36 RETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGVITASAGNHAQGVALAAARLGVKAVIVM 115
|
...
gi 433291063 150 GRT 152
Cdd:PRK12483 116 PRT 118
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
70-249 |
9.24e-08 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 53.42 E-value: 9.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 70 RPTPLQRADrLSERYDREIYLKREDLVHGGAHKLNNALGQvLLAKYMGKERVIAETGaGQHGTATAMAAAHLDMPCEIYM 149
Cdd:PRK08246 22 RRTPVLEAD-GAGFGPAPVWLKLEHLQHTGSFKARGAFNR-LLAAPVPAAGVVAASG-GNAGLAVAYAAAALGVPATVFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 150 GRT--DVNRQrpnvyRMRMSGAEVTPVDAGSATLKEAinetMRDWAgsvETThyavGSVVgPHPF--PAMVRDfQAVIGE 225
Cdd:PRK08246 99 PETapPAKVA-----RLRALGAEVVVVGAEYADALEA----AQAFA---AET----GALL-CHAYdqPEVLAG-AGTLGL 160
|
170 180
....*....|....*....|....*
gi 433291063 226 EIRAQIRDeigrlPDSV-VACAGGG 249
Cdd:PRK08246 161 EIEEQAPG-----VDTVlVAVGGGG 180
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
72-176 |
9.95e-07 |
|
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.
Pssm-ID: 107204 [Multi-domain] Cd Length: 291 Bit Score: 50.20 E-value: 9.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 72 TPLQRADRLSERYDREIYLKREDLVHGGAHKLNNALGQVLLAKYMGKER---VIAETGAGQHGTATAMAAAHLDMPCEIY 148
Cdd:cd01561 3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKpgtTIIEPTSGNTGIGLAMVAAAKGYRFIIV 82
|
90 100
....*....|....*....|....*....
gi 433291063 149 M-GRTDVNRQRpnvyRMRMSGAEVTPVDA 176
Cdd:cd01561 83 MpETMSEEKRK----LLRALGAEVILTPE 107
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
72-255 |
1.08e-06 |
|
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.
Pssm-ID: 107210 Cd Length: 307 Bit Score: 50.11 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 72 TPLQRADRLSERYD--REIYLKREDLVHGGA------HKLNNALGQVLLAKYmgkeRVIAETGAGQ--HGTATAMAAAHL 141
Cdd:cd06449 1 TPIQYLPRLSEHLGgkVEIYAKRDDCNSGLAfggnkiRKLEYLLPDALAKGA----DTLVTVGGIQsnHTRQVAAVAAKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 142 DMPC----EIYMGRTDVNRQRP-NVYRMRMSGAEVTPVDAGsatLKEAINETMRDWAGSVEtthyAVGSvvGPHPFPAMV 216
Cdd:cd06449 77 GLKCvlvqENWVPYSDAVYDRVgNILLSRIMGADVRLVSAG---FDIGIRKSFEEAAEEVE----AKGG--KPYVIPAGG 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 433291063 217 RD--------FQAVigEEIRAQiRDEIGRLPDSVVACAGGGSNTMGT 255
Cdd:cd06449 148 SEhplgglgyVGFV--LEIAQQ-EEELGFKFDSIVVCSVTGSTHAGL 191
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
72-396 |
1.98e-06 |
|
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- , D-serine, or L-threonine to pyruvate/ketobutyrate and ammonia.
Pssm-ID: 107209 Cd Length: 316 Bit Score: 49.60 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 72 TPLQRADRLSERYDREIYLKREDLVHGGAHKL---NNALGQVLLAKYMGKERVIAETGaGQHGTATAMAAAHLDMPCEIY 148
Cdd:cd06448 2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIrgiGHLCQKSAKQGLNECVHVVCSSG-GNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 149 MGRTDVNRQrpnVYRMRMSGAEVtpVDAGSATLKEAInetmrdwagsvETTHYAVGSVVGP---HPF--PaMVRDFQAVI 223
Cdd:cd06448 81 VPESTKPRV---VEKLRDEGATV--VVHGKVWWEADN-----------YLREELAENDPGPvyvHPFddP-LIWEGHSSM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 224 GEEIRAQIRDeiGRLPDSVVACAGGGsntmGTFDAFVDHTERRAEDDsrgrspqedtegVALHAVEAGGSDlgvdeetgv 303
Cdd:cd06448 144 VDEIAQQLQS--QEKVDAIVCSVGGG----GLLNGIVQGLERNGWGD------------IPVVAVETEGAH--------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 304 apnsaslstgtdgVLHGALTKllqtadGQVV---ESHSVSAGLDYAGVGPELANLVDRGRVTPATVDDKAALEAFHRLSR 380
Cdd:cd06448 197 -------------SLNASLKA------GKLVtlpKITSVATSLGAKTVSSQALEYAQEHNIKSEVVSDRDAVQACLRFAD 257
|
330
....*....|....*...
gi 433291063 381 LEGII--PALESSHALGY 396
Cdd:cd06448 258 DERILvePACGAALAVVY 275
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
72-259 |
9.45e-06 |
|
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants.
Pssm-ID: 107206 [Multi-domain] Cd Length: 324 Bit Score: 47.59 E-value: 9.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 72 TPLQRADRLSERYD-REIYLKREDLVHGGAHKlnnALGQVLL---AKYMGKERVIAETgAGQHGTATAMAAAHLDMPCEI 147
Cdd:cd01563 23 TPLVRAPRLGERLGgKNLYVKDEGLNPTGSFK---DRGMTVAvskAKELGVKAVACAS-TGNTSASLAAYAARAGIKCVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 148 YMGRtdvNRQRPNVYRMRMSGAEVTPVDAG-SATLKEAINETMRDWAgsvetthYAVGSVvgpHPFpamvrdF---QAVI 223
Cdd:cd01563 99 FLPA---GKALGKLAQALAYGATVLAVEGNfDDALRLVRELAEENWI-------YLSNSL---NPY------RlegQKTI 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 433291063 224 GEEIRAQIRdeiGRLPDSVVACAGGGSNTMGTFDAF 259
Cdd:cd01563 160 AFEIAEQLG---WEVPDYVVVPVGNGGNITAIWKGF 192
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
72-152 |
1.10e-05 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 47.83 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 72 TPLQRADRLSERYDREIYLKREDL--VHG----GAHKLNNALGQVLLAKymGkerVIAETgAGQHGTATAMAAAHLDMPC 145
Cdd:PRK09224 21 TPLEKAPKLSARLGNQVLLKREDLqpVFSfklrGAYNKMAQLTEEQLAR--G---VITAS-AGNHAQGVALSAARLGIKA 94
|
....*..
gi 433291063 146 EIYMGRT 152
Cdd:PRK09224 95 VIVMPVT 101
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
72-174 |
3.35e-05 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 45.73 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 72 TPLQRADRLSERYDREIYLKREDLVHGGAHKLNNALGQVLLAKYMGKERVIAETGAGQHGTATAMAAAHLDMPCEIYMGR 151
Cdd:PRK07476 20 TPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGRALAYAARALGIRATICMSR 99
|
90 100
....*....|....*....|....
gi 433291063 152 -TDVNRqrpnVYRMRMSGAEVTPV 174
Cdd:PRK07476 100 lVPANK----VDAIRALGAEVRIV 119
|
|
| PRK12390 |
PRK12390 |
1-aminocyclopropane-1-carboxylate deaminase; Provisional |
71-254 |
4.90e-05 |
|
1-aminocyclopropane-1-carboxylate deaminase; Provisional
Pssm-ID: 183494 Cd Length: 337 Bit Score: 45.41 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 71 PTPLQRADRLSERY--DREIYLKRED----LVHGG--AHKLN----NALGQvllakymGKERVIAETGA-GQHGTATAMA 137
Cdd:PRK12390 15 PTPIHPLKRLSAHLggKVELYAKREDcnsgLAFGGnkTRKLEylvpDALAQ-------GADTLVSIGGVqSNHTRQVAAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 138 AAHLDMPC----EIYMGRTD-VNRQRPNVYRMRMSGAEVTPVDAG-SATLKEAinetmrdWAGSVETTHYAVGSvvgPHP 211
Cdd:PRK12390 88 AAHLGMKCvlvqENWVNYEDaVYDRVGNILLSRIMGADVRLVPDGfDIGIRKS-------WEDALEDVRAAGGK---PYA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 433291063 212 FPAMVRDFQ------AVIGEEIRAQIRdEIGRLPDSVVACAGGGSNTMG 254
Cdd:PRK12390 158 IPAGASDHPlgglgfVGFAEEVRAQEA-ELGFKFDYIVVCSVTGSTQAG 205
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
72-193 |
1.85e-04 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 43.31 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 72 TPLQRADRLSERYDREIYLKREDLVHGGAHKLNNALGQVLLAKYMGKER---VIAETGAGQHGTATAMAAAHLDMPCEIY 148
Cdd:PRK10717 14 TPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKpggTIVEGTAGNTGIGLALVAAARGYKTVIV 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 149 MGRTdvnrQRPNVYRM-RMSGAEVTPVDA-----------GSATLKEAINETMRD---WA 193
Cdd:PRK10717 94 MPET----QSQEKKDLlRALGAELVLVPAapyanpnnyvkGAGRLAEELVASEPNgaiWA 149
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
72-384 |
6.33e-04 |
|
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439802 [Multi-domain] Cd Length: 301 Bit Score: 41.57 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 72 TPLQRADRLSERYDREIYLKREDLVHGGAHKlnnalgqVLLAKYM----------GKERVIAETGAGQHGTATAMAAAHL 141
Cdd:COG0031 14 TPLVRLNRLSPGPGAEIYAKLESFNPGGSVK-------DRIALSMiedaekrgllKPGGTIVEATSGNTGIGLAMVAAAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 142 DMPCEIYM-GRTDVNRQRpnvyRMRMSGAEVTPVDaGSATLKEAINETMRDwagsVETTHyavGSVVgPHPF--PAMVRD 218
Cdd:COG0031 87 GYRLILVMpETMSKERRA----LLRAYGAEVVLTP-GAEGMKGAIDKAEEL----AAETP---GAFW-PNQFenPANPEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 219 FQAVIGEEIRAQIRDEIgrlpDSVVACAG-GGSnTMGTFDAFvdhterraeddsRGRSPqedteGVALHAVEAGGsdlgv 297
Cdd:COG0031 154 HYETTGPEIWEQTDGKV----DAFVAGVGtGGT-ITGVGRYL------------KERNP-----DIKIVAVEPEG----- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 298 deetgvapnSASLSTGTDGvlhgaltkllqtadgqvveSHSVSagldyaGVGPEL------ANLVDRGRvtpaTVDDKAA 371
Cdd:COG0031 207 ---------SPLLSGGEPG-------------------PHKIE------GIGAGFvpkildPSLIDEVI----TVSDEEA 248
|
330
....*....|...
gi 433291063 372 LEAFHRLSRLEGI 384
Cdd:COG0031 249 FAMARRLAREEGI 261
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
59-149 |
8.49e-04 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 41.26 E-value: 8.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433291063 59 ELREHLQTFAgRPTPLQRADRLSERYDREIYLKREDLVHGGAHKLNNALGQVLLAKYMGKERVIAETGAGQHGTATAMAA 138
Cdd:PRK08638 16 EAKQRLAGRI-RKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGVALSC 94
|
90
....*....|.
gi 433291063 139 AHLDMPCEIYM 149
Cdd:PRK08638 95 ALLGIDGKVVM 105
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
72-149 |
2.94e-03 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 39.90 E-value: 2.94e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 433291063 72 TPLQRADRLSERYDREIYLKREDLVHGGAHKLNNALG-QVLLAKYMGKERVIAETgAGQHGTATAMAAAHLDMPCEIYM 149
Cdd:PLN02550 110 SPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNmMAKLPKEQLDKGVICSS-AGNHAQGVALSAQRLGCDAVIAM 187
|
|
| |
