|
Name |
Accession |
Description |
Interval |
E-value |
| CobQ |
COG1492 |
Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of ... |
1-491 |
0e+00 |
|
Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441101 [Multi-domain] Cd Length: 493 Bit Score: 838.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 1 MKSIMVVGTTSHAGKSLITTAICRILSRRGWRVAPFKGQNMALNAYVTATGGEIGYAQAVQAWAAGVVPLVEMNPILLKP 80
Cdd:COG1492 2 AKALMVQGTTSDAGKSLLVAALCRILARRGYRVAPFKAQNMSLNSAVTADGGEIGRAQALQAEAAGVEPSVDMNPVLLKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 81 QGDMTSQVILKGRAVGTVSATDYYEqYFELGWRTIEECLQHLKTEFDLLVCEGAGSPAEINLKHRDLTNMRVAKYLNAPT 160
Cdd:COG1492 82 EGDTGSQVIVQGKPVGNMSARDYYE-YKPRLLEAVLESLDRLAAEYDLVVIEGAGSPAEINLRDRDIANMGFAEAADAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 161 LLVVDIDRGGAFAHVVGTLELLEPDERALIKGVIINKFRGQRSILQPGIKWLEERTGIPVVAVIPYLEQV-FPAEDSLDL 239
Cdd:COG1492 161 ILVGDIDRGGVFASLVGTLALLPEEERARVKGFIINKFRGDPSLLEPGLDWLEERTGVPVLGVLPYLEDLrLPAEDSLAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 240 LERKPYKVQSELNITVIRLPKIANFTDFDALESEPTVSVKYVSPKQDLGHPDAVIIPGTKTTIADLIVLQKSGMAEAIQN 319
Cdd:COG1492 241 ESRRGSKGGGRLRIAVIRLPRISNFTDFDPLAAEPGVRLRYVRPPEELGDADLVILPGSKNTIADLAWLRESGLDDAIRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 320 YAASGGTVLGICGGFQMLGQIIADPEGSEGQAGRFQGLNLLPIRTVITGQKIARQRQVSSNYPQMGLPVNGFEIHQGRSR 399
Cdd:COG1492 321 HARRGGPVLGICGGYQMLGRRIADPDGVEGGAGEVPGLGLLPVETVFAPEKTLRQVTGTLLGPLSGAPVSGYEIHMGRTT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 400 LEtqddkQSCQPLFDD---ANLGLVDSCQSIWGTYLHGLFDNGPWRRAWINRLRQQRGLKSLPTGVANYREHREQMLDSL 476
Cdd:COG1492 401 GP-----DGARPLLRRdgrEPDGAVSADGRVWGTYLHGLFDNDAFRRALLNALREKKGLSPLAAGAVDYAARREAALDRL 475
|
490
....*....|....*
gi 515518310 477 ATQIENHLNLNPFLS 491
Cdd:COG1492 476 ADHVEEHLDLDALLA 490
|
|
| PRK00784 |
PRK00784 |
cobyric acid synthase; |
1-491 |
0e+00 |
|
cobyric acid synthase;
Pssm-ID: 234838 [Multi-domain] Cd Length: 488 Bit Score: 806.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 1 MKSIMVVGTTSHAGKSLITTAICRILSRRGWRVAPFKGQNMALNAYVTATGGEIGYAQAVQAWAAGVVPLVEMNPILLKP 80
Cdd:PRK00784 2 AKALMVQGTASDAGKSTLVAGLCRILARRGYRVAPFKAQNMSLNSAVTADGGEIGRAQALQAEAAGVEPSVDMNPVLLKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 81 QGDMTSQVILKGRAVGTVSATDYYEqYFELGWRTIEECLQHLKTEFDLLVCEGAGSPAEINLKHRDLTNMRVAKYLNAPT 160
Cdd:PRK00784 82 QSDRGSQVIVQGKPVGNMDARDYHD-YKPRLLEAVLESLDRLAAEYDVVVVEGAGSPAEINLRDRDIANMGFAEAADAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 161 LLVVDIDRGGAFAHVVGTLELLEPDERALIKGVIINKFRGQRSILQPGIKWLEERTGIPVVAVIPYLEQV-FPAEDSLDL 239
Cdd:PRK00784 161 ILVADIDRGGVFASLVGTLALLPPEERARVKGFIINKFRGDISLLEPGLDWLEELTGVPVLGVLPYLDDLrLPAEDSLAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 240 LERKPYKVQSELNITVIRLPKIANFTDFDALESEPTVSVKYVSPKQDLGHPDAVIIPGTKTTIADLIVLQKSGMAEAIQN 319
Cdd:PRK00784 241 LERAARAGGGALRIAVIRLPRISNFTDFDPLRAEPGVDVRYVRPGEPLPDADLVILPGSKNTIADLAWLRESGWDEAIRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 320 YAASGGTVLGICGGFQMLGQIIADPEGSEGQAGRFQGLNLLPIRTVITGQKiaRQRQVSSNYPQMGLPVNGFEIHQGRSR 399
Cdd:PRK00784 321 HARRGGPVLGICGGYQMLGRRIADPDGVEGAPGSVEGLGLLDVETVFEPEK--TLRQVTGLLLGSGAPVSGYEIHMGRTT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 400 LETqddkqSCQPLF---DDANLGLVDSCQSIWGTYLHGLFDNGPWRRAWINRLRQQRGLksLPTGVANYREHREQMLDSL 476
Cdd:PRK00784 399 GPA-----LARPFLrldDGRPDGAVSADGRVFGTYLHGLFDNDAFRRALLNWLGARKGL--APASALDYAALREAQLDRL 471
|
490
....*....|....*
gi 515518310 477 ATQIENHLNLNPFLS 491
Cdd:PRK00784 472 ADLVEEHLDLDALLA 486
|
|
| cobQ |
TIGR00313 |
cobyric acid synthase CobQ; [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, ... |
4-488 |
0e+00 |
|
cobyric acid synthase CobQ; [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 129413 [Multi-domain] Cd Length: 475 Bit Score: 657.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 4 IMVVGTTSHAGKSLITTAICRILSRRGWRVAPFKGQNMALNAYVTATGGEIGYAQAVQAWAAGVVPLVEMNPILLKPQGD 83
Cdd:TIGR00313 1 IMVVGTTSSAGKSTLTAGLCRILARRGYRVAPFKSQNMSLNSFVTKEGGEIAIAQATQALAAGIEPSVHMNPILLKPKGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 84 MTSQVILKGRAVGTVSATDYYEQYFELGWRTIEECLQHLKTEFDLLVCEGAGSPAEINLKHRDLTNMRVAKYLNAPTLLV 163
Cdd:TIGR00313 81 FTSQVIVHGRAVGDMNYQEYYKNKVDFFLKAIKESLEILAREYDYVVIEGAGSPAEINLLKRDLANMRIAELANADAILV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 164 VDIDRGGAFAHVVGTLELLEPDERALIKGVIINKFRGQRSILQPGIKWLEERTGIPVVAVIPYLEQVFPAEDSLDLLERK 243
Cdd:TIGR00313 161 ADIDRGGVFASIYGTLKLLPENWRKLIKGIVINKFRGNVDVLKSGIEKLEELTGIPVLGVLPYDENLFPEEDSLVIQERR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 244 PYKVQSELNITVIRLPKIANFTDFDALESEPtvSVKYVSPKQDLGHPDAVIIPGTKTTIADLIVLQKSGMAEAIQNYAAS 323
Cdd:TIGR00313 241 SRGNAKSIRIGVVRLPRISNFTDFEPLRYEA--FVKFLDLDDSLTGCDAVIIPGSKSTIADLYALKQSGFAEEILDFAKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 324 GGTVLGICGGFQMLGQIIADPEGSEGQAGRFQGLNLLPIRTVITGQKIARQRQVSSNYPQMGLPVNGFEIHQGRSRLetq 403
Cdd:TIGR00313 319 GGIVIGICGGYQMLGKELIDKEKKESDVGDIEGLGLLDAKTYFGEDKITKQSQGRVEGNNRGETVKGYEIHEGFTRS--- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 404 ddkqSCQPLFDDANLGLVDSCQSIWGTYLHGLFDNGPWRRAWINRLRQQRGLksLPTGVANYREHREQMLDSLATQIENH 483
Cdd:TIGR00313 396 ----KEKPLFKIERFGNCGNDGNAWGTYLHGLFENYEFRRYIINLLRKRKGP--LEIYGGNYKDQREKSLDYLADVVERS 469
|
....*
gi 515518310 484 LNLNP 488
Cdd:TIGR00313 470 VNLKP 474
|
|
| CobQ_N |
cd05389 |
N-terminal domain of cobyric acid synthase; Cobyric acid synthase (CobQ, CbiP) N-terminal ... |
2-225 |
9.72e-142 |
|
N-terminal domain of cobyric acid synthase; Cobyric acid synthase (CobQ, CbiP) N-terminal domain. CobQ plays a role in the cobalamin (vitamin B12) biosynthesis pathway. CobQ catalyzes the ATP-dependent amidation of adenosyl-cobyrinic acid a,c-diamide at carboxylates positions b, d, e, and g to produce cobyric acid using glutamine or ammonia as the nitrogen source. The C-terminal glutaminase domain catalyzes the hydrolysis of glutamine to glutamate and ammonia. Ammonia is translocated via an intramolecular tunnel to the N-terminal domain for the synthesis of cobyric acid.
Pssm-ID: 349774 Cd Length: 223 Bit Score: 405.82 E-value: 9.72e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 2 KSIMVVGTTSHAGKSLITTAICRILSRRGWRVAPFKGQNMALNAYVTATGGEIGYAQAVQAWAAGVVPLVEMNPILLKPQ 81
Cdd:cd05389 1 KSIMVQGTASDVGKSTLVAALCRILKRRGYRVAPFKAQNMSLNSFVTKDGGEIGRAQAVQAEAAGVEPSVDMNPVLLKPK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 82 GDMTSQVILKGRAVGTVSATDYYEQYFELGWrTIEECLQHLKTEFDLLVCEGAGSPAEINLKHRDLTNMRVAKYLNAPTL 161
Cdd:cd05389 81 GDFKSQVIVMGKPIGDMDAREYYEYKGRLAP-AVLESLDRLAAEYDLVVIEGAGSPAEINLRDRDIVNMGMARAADAPVI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515518310 162 LVVDIDRGGAFAHVVGTLELLEPDERALIKGVIINKFRGQRSILQPGIKWLEERTGIPVVAVIP 225
Cdd:cd05389 160 LVADIDRGGVFASLYGTLALLPEEERKLVKGVVINKFRGDRSLLEPGIEMLEERTGVPVLGVLP 223
|
|
| GATase1_CobQ |
cd01750 |
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ... |
253-446 |
1.54e-76 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ). CobQ plays a role in cobalamin biosythesis. CobQ catalyses amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide in the biosynthesis of cobalamin. CobQ belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobQ.
Pssm-ID: 153221 [Multi-domain] Cd Length: 194 Bit Score: 238.30 E-value: 1.54e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 253 ITVIRLPKIANFTDFDALESEPTVSVKYVSPKQDLGHPDAVIIPGTKTTIADLIVLQKSGMAEAIQNYAASGGTVLGICG 332
Cdd:cd01750 1 IAVIRYPDISNFTDLDPLAREPGVDVRYVEVPEGLGDADLIILPGSKDTIQDLAWLRKRGLAEAIKNYARAGGPVLGICG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 333 GFQMLGQIIADPEGSEGQaGRFQGLNLLPIRTVITGQKIARQRQVSSNYPQMGLPVNGFEIHQGRSRLE--TQDDKQSCQ 410
Cdd:cd01750 81 GYQMLGKYIVDPEGVEGP-GEIEGLGLLDVETEFGPEKTTRRVTGRLDEEGEGGEVTGYEIHSGRTTLGdgARPLGKGYG 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 515518310 411 PLFDDANLGLVDSCqSIWGTYLHGLFDNGPWRRAWI 446
Cdd:cd01750 160 NNGEDGTDGAVSGD-NVIGTYLHGIFLNDAFRDALL 194
|
|
| GATase_3 |
pfam07685 |
CobB/CobQ-like glutamine amidotransferase domain; |
252-440 |
7.02e-59 |
|
CobB/CobQ-like glutamine amidotransferase domain;
Pssm-ID: 429595 [Multi-domain] Cd Length: 189 Bit Score: 192.46 E-value: 7.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 252 NITVIRLPKIANFT--DFDALESEPTVSVKYVS-PKQDLG-HPDAVIIPGTKTTIADLIVLQKSGMAEAIQNYAASGGTV 327
Cdd:pfam07685 1 RIAVIRLPRISNYTddNLDPLRYEPAVRVRFVPlPDESLGpDADLIILPGGKPTIQDLALLRNSGMDEAIKEAAEDGGPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 328 LGICGGFQMLGQIIADPEGSegqagRFQGLNLLPIRTVITGQKIARQRQVssnYPQM-GLPVNGFEIHQGRSRLEtqddk 406
Cdd:pfam07685 81 LGICGGYQMLGETIEDPEGV-----RIEGLGLLDIETVFQKEKLTGQVVG---YLLLeGETVRGYEIHYGRTILG----- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515518310 407 QSCQPLF----------DDANLGLVDscQSIWGTYLHGLFDNGP 440
Cdd:pfam07685 148 DGAKPLGrvkvgggnngEDGKDGAVS--GNVFGTYLHGHFLNRN 189
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
4-240 |
4.83e-49 |
|
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.
Pssm-ID: 426369 [Multi-domain] Cd Length: 228 Bit Score: 167.91 E-value: 4.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 4 IMVVGTTSHAGKSLITTAICRILSRRGWRVAPFKGQNMALNAyvTATGGEIGYAQAVQAWAAGVVPLVEMNPILLKPQGD 83
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNS--SVEGLEGDIAPALQALAEGLKGRVNLDPILLKEKSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 84 MTSQVILKGRAVGTVSATDYYEQYFELgwrTIEECLQHLKTEFDLLVCEGAGSPAEiNLKHRDLTNMRVAKYLNAPTLLV 163
Cdd:pfam01656 79 EGGLDLIPGNIDLEKFEKELLGPRKEE---RLREALEALKEDYDYVIIDGAPGLGE-LLRNALIAADYVIIPLEPEVILV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 164 VDIDR-GGAFAHVVGTLELLepdeRALIKGVIINKFRGQRSI--LQPGIKWLEErtGIPVVAVIPYLEQVFPAEDSLDLL 240
Cdd:pfam01656 155 EDAKRlGGVIAALVGGYALL----GLKIIGVVLNKVDGDNHGklLKEALEELLR--GLPVLGVIPRDEAVAEAPARGLPV 228
|
|
| BioD |
COG0132 |
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ... |
1-239 |
1.41e-23 |
|
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 439902 [Multi-domain] Cd Length: 222 Bit Score: 98.69 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 1 MKSIMVVGTTSHAGKSLITTAICRILSRRGWRVAPFKgqnMAlnayvtATGGEIGY-------AQAVQAWAAGVVPLVEM 73
Cdd:COG0132 1 MKGLFVTGTDTDVGKTVVTAALAAALRAAGLRVGYYK---PV------QTGCEETDgglrngdAELLRRLSGLPLSYELV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 74 NPILLK----PqgDMTSQviLKGRAVgtvsatdyyeqyfELGwrTIEECLQHLKTEFDLLVCEGAG---SPaeINlkhRD 146
Cdd:COG0132 72 NPYRFEeplsP--HLAAR--LEGVPI-------------DLD--KILAALRALAARYDLVLVEGAGgllVP--LT---ED 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 147 LTNMRVAKYLNAPTLLVVDIdRGGAFAHVVGTLELLEpdERAL-IKGVIINKFRGQRSILQPGIKWLEERTGIPVVAVIP 225
Cdd:COG0132 128 LTLADLAKALGLPVILVVRA-RLGTINHTLLTVEALR--ARGLpLAGIVLNGVPPPDLAERDNLETLERLTGAPVLGVLP 204
|
250
....*....|....*.
gi 515518310 226 YLEQVFPAE--DSLDL 239
Cdd:COG0132 205 YLADLDPEAlaAYLDL 220
|
|
| AAA_26 |
pfam13500 |
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ... |
2-230 |
7.85e-21 |
|
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis such as dethiobiotin synthase and cobyric acid synthase. This domain contains a P-loop motif.
Pssm-ID: 433259 [Multi-domain] Cd Length: 198 Bit Score: 90.40 E-value: 7.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 2 KSIMVVGTTSHAGKSLITTAICRILSRRGWRVAPFKgqnmALNAYVTATGGeigyAQAVQAWAAGVVPLVEMNPILLKPQ 81
Cdd:pfam13500 1 RTLFVTGTDTGVGKTVVSLGLARALKRRGVKVGYWK----PVQTGLVEDGD----SELVKRLLGLDQSYEDPEPFRLSAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 82 gdmTSQVILKGRAVGTVSATDYyeqyfelgWRTIEEclqhlktEFDLLVCEGAGSPAE-INlkhRDLTNMRVAKYLNAPT 160
Cdd:pfam13500 73 ---LSPHLAARQEGVTIDLEKI--------IYELPA-------DADPVVVEGAGGLLVpIN---EDLLNADIAANLGLPV 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 161 LLVVDIDRGgAFAHVVGTLELLEpDERALIKGVIINKFRGQRSILQpgikwLEERTGIPVVAVIPYLEQV 230
Cdd:pfam13500 132 ILVARGGLG-TINHTLLTLEALR-QRGIPVLGVILNGVPNPENVRT-----IFAFGGVPVLGAVPYLPDL 194
|
|
| PRK01077 |
PRK01077 |
cobyrinate a,c-diamide synthase; |
1-433 |
1.92e-19 |
|
cobyrinate a,c-diamide synthase;
Pssm-ID: 234896 [Multi-domain] Cd Length: 451 Bit Score: 90.58 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 1 MKSIMVVGTTSHAGKSLITTAICRILSRRGWRVAPFKgqnmalnayvtatggeIG-------YAQAvqawAAGvVPLVEM 73
Cdd:PRK01077 3 MPALVIAAPASGSGKTTVTLGLMRALRRRGLRVQPFK----------------VGpdyidpaYHTA----ATG-RPSRNL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 74 NPILLKPQGdmtsqvilkgravgtvsatdyyeqyfelgwrtIEECLQHLKTEFDLLVCEGA-------------GSPAEI 140
Cdd:PRK01077 62 DSWMMGEEL--------------------------------VRALFARAAQGADIAVIEGVmglfdgagsdpdeGSTADI 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 141 nlkhrdltnmrvAKYLNAPTLLVVDIdRGGA--FAHVVGTLELLEPDERalIKGVIINKFRGQR--SILQPGIkwleERT 216
Cdd:PRK01077 110 ------------AKLLGAPVVLVVDA-SGMAqsAAALVLGFATFDPDVR--IAGVILNRVGSERhyQLLREAL----ERC 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 217 GIPVVAVIPY---------------------LEQVFPA-----EDSLDL-----LERKPYKVQSELNITVIRLP--KIA- 262
Cdd:PRK01077 171 GIPVLGALPRdaalalperhlglvqasehgdLEARLDAladlvEEHVDLdallaLARAAPPPPPAAAPPPPAPPgvRIAv 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 263 ------NFT---DFDALEsEPTVSVKYVSPKQD--LGHPDAVIIPGT-----KTTIAdlivlQKSGMAEAIQNYAASGGT 326
Cdd:PRK01077 251 ardaafNFYypeNLELLR-AAGAELVFFSPLADeaLPDCDGLYLGGGypelfAAELA-----ANTSMRASIRAAAAAGKP 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 327 VLGICGGFQMLGQIIADPEGSegqagRFQGLNLLPIRTVITGQK------IARQRQVSSNYPQmGLPVNGFEIHqgRSRL 400
Cdd:PRK01077 325 IYAECGGLMYLGESLEDADGE-----RHPMVGLLPGEASMTKRLqalgyrEAEALEDTLLGKA-GERLRGHEFH--YSTL 396
|
490 500 510
....*....|....*....|....*....|....*....
gi 515518310 401 ETQDDKqscqPLFD--DANLGLVDSC----QSIWGTYLH 433
Cdd:PRK01077 397 ETPEEA----PLYRvrDADGRPLGEEgyrrGNVLASYLH 431
|
|
| CobB |
COG1797 |
Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a, ... |
2-453 |
1.37e-15 |
|
Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a,c-diamide synthase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441402 [Multi-domain] Cd Length: 459 Bit Score: 79.00 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 2 KSIMVVGTTSHAGKSLITTAICRILSRRGWRVAPFKgqnmalnayvtatggeIG-------YaqavQAWAAGVVPLvemN 74
Cdd:COG1797 4 PRLVIAAPHSGSGKTTVTLGLLAALRRRGLKVQPFK----------------VGpdyidpgY----HTLATGRPSR---N 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 75 --PILLKPQgdmtsqvilkgravgtvsatdyyeqyfelgwrTIEECLQHLKTEFDLLVCEG-------------AGSPAE 139
Cdd:COG1797 61 ldPFLMGEE--------------------------------GVRELFARGSAGADIAVIEGvmglydgldgdsgSGSTAH 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 140 InlkhrdltnmrvAKYLNAPTLLVVDIDR--GGAFAHVVGTLELlepDERALIKGVIINKFRGQR--SILQPGIkwlEER 215
Cdd:COG1797 109 L------------AKLLGAPVVLVVDASGmsRSAAALVLGFRAF---DPDVRIAGVILNRVGSERheELLREAI---EHY 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 216 TGIPVVAVIPYLEQV-FP-------------------------AEDSLDL---LE------RKPYKVQSELNITVIRLPK 260
Cdd:COG1797 171 TGIPVLGALPRDEELeLPsrhlglvpaaereeleealdrlaelVEEHVDLdalLElarsapPLPAPPSPLFAPPPGPRVR 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 261 IA-------NFT---DFDALES---EptvsVKYVSPKQDLGHP---DAVIIPGtkttiadlivlqksG------------ 312
Cdd:COG1797 251 IAvardeafNFYypeNLELLEAagaE----LVFFSPLRDEALPedvDGLYLGG--------------Gfpelfaeelsan 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 313 --MAEAIQNYAASGGTVLGICGGFQMLGQIIADPEGSegqagRFQGLNLLPIRTVITGQKIA---RQRQVSSNYP--QMG 385
Cdd:COG1797 313 rsMRESIREAAEAGMPIYAECGGLMYLCRSITDFEGK-----GYPMVGVLPGDAVMTKRLQGlgyREATALGDSPlgPAG 387
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515518310 386 LPVNGFEIHqgRSRLETQDDkqsCQPLF--------DDANLGLVDscQSIWGTYLHGLFDNGP-WRRAWINRLRQQR 453
Cdd:COG1797 388 ERIRGHEFH--YSTLTPEGD---LRPAYrlrrgrgiDGGRDGFVY--GNVLASYLHLHFASNPeWAERFVAACRAYR 457
|
|
| COG3442 |
COG3442 |
Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction ... |
275-434 |
5.03e-14 |
|
Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction only];
Pssm-ID: 442666 [Multi-domain] Cd Length: 241 Bit Score: 71.75 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 275 TVSVKYVSPKQDL--GHPDAVIIpGTKTTIADLIVLQK-SGMAEAIQNYAASGGTVLGICGGFQMLGQIIADPEGSegqa 351
Cdd:COG3442 34 DVEVVEVNPGDDLpfDDVDIVFI-GGGQDREQEIVADDlLRIKDALRAAIEDGVPVLAICGGYQLLGHYYETADGE---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 352 gRFQGLNLLPIRTVitGQKiarQR-----QVSSNYPQMGLPVNGFEIHQGRSRLETQddkqsCQPL----------FDDA 416
Cdd:COG3442 109 -RIPGLGILDVYTV--AGK---KRlignvVVETELNGEFGTLVGFENHSGRTYLGPG-----VKPLgrvlygygnnGEDG 177
|
170
....*....|....*...
gi 515518310 417 NLGLVDscQSIWGTYLHG 434
Cdd:COG3442 178 TEGARY--KNVIGTYLHG 193
|
|
| DTBS |
cd03109 |
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ... |
2-214 |
1.39e-13 |
|
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the biotin biosynthesis pathway in Escherichia coli and other microorganisms. The enzyme catalyzes formation of the ureido ring of dethiobiotin from (7R,8S)-7,8-diaminononanoic acid (DAPA) and carbon dioxide. The enzyme utilizes carbon dioxide instead of hydrogen carbonate as substrate and is dependent on ATP and divalent metal ions as cofactors.
Pssm-ID: 349763 [Multi-domain] Cd Length: 189 Bit Score: 69.14 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 2 KSIMVVGTTSHAGKSLITTAICRILSRRGWRVAPFKgqnmalnayVTATGGEIGY---AQAVQAWAAGVVPLVEMNPILL 78
Cdd:cd03109 1 KTLFVTGTDTDVGKTVVSAGLARALRKKGIKVGYLK---------PVQTGCPGLEdsdAELLRKLAGLLLDLELINPYRF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 79 KPQgdmTSQVILKGRAVGTVSatdyyeqyfelgWRTIEECLQHLKTEFDLLVCEGAG---SPaeINlkhRDLTNMRVAKY 155
Cdd:cd03109 72 EAP---LSPHLAAELEGRDID------------LEEIVRALEELAKSYDVVLVEGAGgllVP--LT---EGYLNADLARA 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 156 LNAPTLLVVDIdRGGAFAHVVGTLELLEpdERAL-IKGVIINKFRGQRSILQPGIKWLEE 214
Cdd:cd03109 132 LGLPVILVARG-GLGTINHTLLTLEALK--SRGLdVAGVVLNGIPPEPEAEADNAETLKE 188
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
276-385 |
5.77e-08 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153219 [Multi-domain] Cd Length: 198 Bit Score: 52.89 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 276 VSVKYVSPKQDLGHPDAVIIPGTKTTIADLIVLQKSGMAEAIQNYAASGGTVLGICGGFQMLGqiiadpEGSEgQAGRFQ 355
Cdd:cd01748 23 AEVIITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAIASGKPFLGICLGMQLLF------ESSE-EGGGTK 95
|
90 100 110
....*....|....*....|....*....|....
gi 515518310 356 GLNLLPIRTV----ITGQKIarqrqvssnyPQMG 385
Cdd:cd01748 96 GLGLIPGKVVrfpaSEGLKV----------PHMG 119
|
|
| hisH |
PRK13181 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
267-385 |
6.47e-08 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 52.95 E-value: 6.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 267 FDALESEPTVSvkyvSPKQDLGHPDAVIIPGT---KTTIADLivlQKSGMAEAIQNYAASGGTVLGICGGFQMLGqiiad 343
Cdd:PRK13181 19 LKRLGVEAVVS----SDPEEIAGADKVILPGVgafGQAMRSL---RESGLDEALKEHVEKKQPVLGICLGMQLLF----- 86
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 515518310 344 pEGSEgqAGRFQGLNLLPIRTVitgqkiaRQRQVSSNYPQMG 385
Cdd:PRK13181 87 -ESSE--EGNVKGLGLIPGDVK-------RFRSEPLKVPQMG 118
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
264-337 |
8.10e-08 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 50.67 E-value: 8.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 264 FTDFDALESEPtVSVKYVSPK-------QDLGHPDAVIIPGTKTTIADLIVLQksGMAEAIQNYAASGGTVLGICGGFQM 336
Cdd:cd01653 15 ASPLDALREAG-AEVDVVSPDggpvesdVDLDDYDGLILPGGPGTPDDLARDE--ALLALLREAAAAGKPILGICLGAQL 91
|
.
gi 515518310 337 L 337
Cdd:cd01653 92 L 92
|
|
| hisH |
PRK13141 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
291-385 |
9.20e-08 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 52.44 E-value: 9.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 291 DAVIIPG---TKTTIAdliVLQKSGMAEAIQNYAASGGTVLGICGGFQMLGqiiadpEGSEgQAGRFQGLNLLPIRTV-- 365
Cdd:PRK13141 39 DGVILPGvgaFPDAMA---NLRERGLDEVIKEAVASGKPLLGICLGMQLLF------ESSE-EFGETEGLGLLPGRVRrf 108
|
90 100
....*....|....*....|..
gi 515518310 366 --ITGQKIarqrqvssnyPQMG 385
Cdd:PRK13141 109 ppEEGLKV----------PHMG 120
|
|
| CobB_N |
cd05388 |
N-terminal domain of cobyrinic acid a,c-diamide synthase; Cobyrinic acid a,c-diamide synthase ... |
2-225 |
1.68e-07 |
|
N-terminal domain of cobyrinic acid a,c-diamide synthase; Cobyrinic acid a,c-diamide synthase (CobB, CbiA). Biosynthesis of cobalamin (vitamin B12) requires more than two dozen different enzymes. CobB catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinic acid, via the formation of a phosphorylated intermediate, using glutamine or ammonia as the nitrogen source. CobB is comprised of two protein domains: the C-terminal glutaminase domain and the N-terminal ATP-binding domain. The glutaminase domain catalyzes the hydrolysis of glutamine to glutamate and ammonia. It belongs to the triad class of glutamine amidotransferases. This classification is based on the N-terminal domain which catalyzes the ultimate synthesis of the diamide product by using energy from the hydrolysis of ATP and ammonia transferred from the C-terminal domain.
Pssm-ID: 349773 [Multi-domain] Cd Length: 193 Bit Score: 51.45 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 2 KSIMVVGTTSHAGKSLITTAICRILSRRGWRVAPFK-GQNmalnaYVTATggeigyaqaVQAWAAGvVPLVEMNPILLKP 80
Cdd:cd05388 1 PRIVIAGTSSGSGKTTITLGLMRALARRGLRVQPFKvGPD-----YIDPG---------FHEAATG-RPSRNLDSWMMGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 81 QGdmtsqvilkgravgtvsatdyyeqyfelgwrtIEECLQHLKTEFDLLVCEGA-------------GSPAEInlkhrdl 147
Cdd:cd05388 66 DG--------------------------------VRELFARAAGGADVAIIEGVmglydgrdtdsdeGSTAEL------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 148 tnmrvAKYLNAPTLLVVDIdRGGAF--AHVVGTLELLEPDERalIKGVIINKFRGQR--SILQPGIkwlEERTGIPVVAV 223
Cdd:cd05388 107 -----ARLLGAPVLLVLDC-KGMARsaAAIVKGYKEFDPDLN--LAGVILNRVGSPRhaELLKEAI---EEYTGIPVLGY 175
|
..
gi 515518310 224 IP 225
Cdd:cd05388 176 LP 177
|
|
| GATase1_PB |
cd01749 |
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ... |
268-379 |
4.67e-07 |
|
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis. Glutamine amidotransferase (GATase) activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. This group contains proteins like Bacillus subtilus YaaE and Plasmodium falciparum Pdx2 which are members of the triad glutamine aminotransferase family and function in a pathway for the biosynthesis of vitamin B6.
Pssm-ID: 153220 [Multi-domain] Cd Length: 183 Bit Score: 49.83 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 268 DALESePTVSVKYVSPKQDLGHPDAVIIPGTK-TTIADLivLQKSGMAEAIQNYAASGGTVLGICGGFQMLGQIIADPeg 346
Cdd:cd01749 15 RALER-LGVEVIEVRTPEDLEGIDGLIIPGGEsTTIGKL--LRRTGLLDPLREFIRAGKPVFGTCAGLILLAKEVEDQ-- 89
|
90 100 110
....*....|....*....|....*....|...
gi 515518310 347 segqaGRFQGLNLLPIrTVitgQKIARQRQVSS 379
Cdd:cd01749 90 -----GGQPLLGLLDI-TV---RRNAFGRQVDS 113
|
|
| GATase1_CobB |
cd03130 |
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide ... |
278-433 |
5.14e-07 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide Synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide Synthase. CobB plays a role in cobalamin biosythesis catalyzing the conversion of cobyrinic acid to cobyrinic acid a,c-diamide. CobB belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobB.
Pssm-ID: 153224 [Multi-domain] Cd Length: 198 Bit Score: 50.29 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 278 VKYVSPKQD--LGHPDAVIIPGT-----KTTIADlivlqKSGMAEAIQNYAASGGTVLGICGGFQMLGQIIADPEGSegq 350
Cdd:cd03130 27 LVPFSPLKDeeLPDADGLYLGGGypelfAEELSA-----NQSMRESIRAFAESGGPIYAECGGLMYLGESLDDEEGQ--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 351 agRFQGLNLLPIRTVIT-----GQKIARQRQVSSNYPQmGLPVNGFEIHqgRSRLETQDDKQSCQPL----FDDANLGLV 421
Cdd:cd03130 99 --SYPMAGVLPGDARMTkrlglGYREAEALGDTLLGKK-GTTLRGHEFH--YSRLEPPPEPDFAATVrrgrGIDGGEDGY 173
|
170
....*....|..
gi 515518310 422 dSCQSIWGTYLH 433
Cdd:cd03130 174 -VYGNVLASYLH 184
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
264-337 |
9.01e-07 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 46.81 E-value: 9.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 264 FTDFDALESEPtVSVKYVSPK-------QDLGHPDAVIIPGTKTTIADLivLQKSGMAEAIQNYAASGGTVLGICGGFQM 336
Cdd:cd03128 15 ASPLDALREAG-AEVDVVSPDggpvesdVDLDDYDGLILPGGPGTPDDL--AWDEALLALLREAAAAGKPVLGICLGAQL 91
|
.
gi 515518310 337 L 337
Cdd:cd03128 92 L 92
|
|
| HisH |
COG0118 |
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
291-385 |
9.17e-07 |
|
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 439888 [Multi-domain] Cd Length: 196 Bit Score: 49.27 E-value: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 291 DAVIIPGtkttiadliV---------LQKSGMAEAIQNYAASGGTVLGICGGFQMLGqiiadpEGSEgQAGRFQGLNLLP 361
Cdd:COG0118 40 DRLVLPG---------VgafgdamenLRERGLDEAIREAVAGGKPVLGICLGMQLLF------ERSE-ENGDTEGLGLIP 103
|
90 100
....*....|....*....|....*..
gi 515518310 362 IRTV---ITGQKIarqrqvssnyPQMG 385
Cdd:COG0118 104 GEVVrfpASDLKV----------PHMG 120
|
|
| PRK05632 |
PRK05632 |
phosphate acetyltransferase; Reviewed |
1-226 |
1.25e-06 |
|
phosphate acetyltransferase; Reviewed
Pssm-ID: 235537 [Multi-domain] Cd Length: 684 Bit Score: 50.92 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 1 MKSIMVVGTTSHAGKSLITTAICRILSRRGWRVAPFKGqnmalnayVTATGgeIGYAQAVQAWAAGvvplvemnpillkp 80
Cdd:PRK05632 2 SRSIYLAPTGTGVGLTSVSLGLMRALERKGVKVGFFKP--------IAQPP--LTMSEVEALLASG-------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 81 qgdmtsqvilkgravgtvsatdyyeQYFELgwrtIEECL---QHLKTEFDLLVCEG----AGSPAEINLkhrdltNMRVA 153
Cdd:PRK05632 58 -------------------------QLDEL----LEEIVaryHALAKDCDVVLVEGldptRKHPFEFSL------NAEIA 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 154 KYLNAPTLLVV--DIDRGGAFAHVV-GTLELLEPDERALIKGVIINKFRGQRSILQPGIKWLEERT-------------- 216
Cdd:PRK05632 103 KNLGAEVVLVSsgGNDTPEELAERIeLAASSFGGAKNANILGVIINKLNAPVDEQGRTRPDLSEIFddsskanvdpsklf 182
|
250
....*....|...
gi 515518310 217 ---GIPVVAVIPY 226
Cdd:PRK05632 183 assPLPLLGVVPW 195
|
|
| PLN02617 |
PLN02617 |
imidazole glycerol phosphate synthase hisHF |
277-361 |
1.64e-06 |
|
imidazole glycerol phosphate synthase hisHF
Pssm-ID: 178226 [Multi-domain] Cd Length: 538 Bit Score: 50.48 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 277 SVKYVSPKQDLGHPDAVIIPGTKTTIADLIVLQKSGMAEAIQNYAASGGTVLGICGGFQMLGqiiadpEGSEgQAGRFQG 356
Cdd:PLN02617 32 TIKDVQTPEDILNADRLIFPGVGAFGSAMDVLNNRGMAEALREYIQNDRPFLGICLGLQLLF------ESSE-ENGPVEG 104
|
....*
gi 515518310 357 LNLLP 361
Cdd:PLN02617 105 LGVIP 109
|
|
| PRK13527 |
PRK13527 |
glutamine amidotransferase subunit PdxT; Provisional |
275-379 |
1.89e-06 |
|
glutamine amidotransferase subunit PdxT; Provisional
Pssm-ID: 237412 [Multi-domain] Cd Length: 200 Bit Score: 48.34 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 275 TVSVKYVSPKQDLGHPDAVIIPGTK-TTIADLIvlQKSGMAEAIQNYAASGGTVLGICGGFQMLGQiiaDPEGSEGQAGR 353
Cdd:PRK13527 29 DGEVVEVRRPGDLPDCDALIIPGGEsTTIGRLM--KREGILDEIKEKIEEGLPILGTCAGLILLAK---EVGDDRVTKTE 103
|
90 100
....*....|....*....|....*....
gi 515518310 354 FQGLNLLPIrtvitgqKIARQ---RQVSS 379
Cdd:PRK13527 104 QPLLGLMDV-------TVKRNafgRQRDS 125
|
|
| PRK03619 |
PRK03619 |
phosphoribosylformylglycinamidine synthase subunit PurQ; |
266-337 |
1.79e-05 |
|
phosphoribosylformylglycinamidine synthase subunit PurQ;
Pssm-ID: 235140 [Multi-domain] Cd Length: 219 Bit Score: 45.88 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 266 DFD---ALESEPTVSVKYVSPKQ-DLGHPDAVIIPGTKT--------TIAdlivlQKSGMAEAIQNYAASGGTVLGICGG 333
Cdd:PRK03619 14 DRDmarALRDLLGAEPEYVWHKEtDLDGVDAVVLPGGFSygdylrcgAIA-----AFSPIMKAVKEFAEKGKPVLGICNG 88
|
....
gi 515518310 334 FQML 337
Cdd:PRK03619 89 FQIL 92
|
|
| PRK13525 |
PRK13525 |
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT; |
275-379 |
3.28e-05 |
|
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
Pssm-ID: 237411 [Multi-domain] Cd Length: 189 Bit Score: 44.76 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 275 TVSVKYVSpkqDLGHPDAVIIPGTK-TTIADLivLQKSGMAEAIQNYAASGGTVLGICGGFQMLGQIIADPEgsegqAGR 353
Cdd:PRK13525 27 AVEVRRPE---DLDEIDGLILPGGEsTTMGKL--LRDFGLLEPLREFIASGLPVFGTCAGMILLAKEIEGYE-----QEH 96
|
90 100
....*....|....*....|....*.
gi 515518310 354 FQGLNllpirtvITGQKIARQRQVSS 379
Cdd:PRK13525 97 LGLLD-------ITVRRNAFGRQVDS 115
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
2-39 |
1.18e-04 |
|
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.
Pssm-ID: 349751 [Multi-domain] Cd Length: 107 Bit Score: 41.26 E-value: 1.18e-04
10 20 30
....*....|....*....|....*....|....*...
gi 515518310 2 KSIMVVGTTSHAGKSLITTAICRILSRRGWRVAPFKGQ 39
Cdd:cd01983 1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
|
|
| PurL2 |
COG0047 |
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ... |
310-337 |
2.26e-04 |
|
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439817 [Multi-domain] Cd Length: 236 Bit Score: 42.74 E-value: 2.26e-04
10 20
....*....|....*....|....*...
gi 515518310 310 KSGMAEAIQNYAASGGTVLGICGGFQML 337
Cdd:COG0047 66 FSPIMDAVREFARRGGLVLGICNGFQIL 93
|
|
| GATase1_FGAR_AT |
cd01740 |
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ... |
314-337 |
1.37e-03 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase; Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT). FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. FGAR-AT is a glutamine amidotransferase. Glutamine amidotransferase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. FGAR-AT belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site
Pssm-ID: 153211 [Multi-domain] Cd Length: 238 Bit Score: 40.29 E-value: 1.37e-03
10 20
....*....|....*....|....
gi 515518310 314 AEAIQNYAASGGTVLGICGGFQML 337
Cdd:cd01740 72 MEEVKEFAERGGLVLGICNGFQIL 95
|
|
| FGAM_synth_I |
TIGR01737 |
phosphoribosylformylglycinamidine synthase I; In some species, ... |
253-337 |
2.86e-03 |
|
phosphoribosylformylglycinamidine synthase I; In some species, phosphoribosylformylglycinamidine synthase is composed of a single polypeptide chain. This model describes the PurQ protein of Bacillus subtilis (where PurL, PurQ, and PurS are required for phosphoribosylformylglycinamidine synthase activity) and functionally equivalent proteins from other bacteria and archaea. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273782 [Multi-domain] Cd Length: 227 Bit Score: 39.28 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 253 ITVIRLPkiANFTDFD---ALES--EPTVSVKYvsPKQDLGHPDAVIIPGTKT--------TIADLIVLqksgmAEAIQN 319
Cdd:TIGR01737 3 VAVIRFP--GTNCDRDtvyALRLlgVDAEIVWY--EDGSLPDYDGVVLPGGFSygdylragAIAAASPI-----MQEVRE 73
|
90
....*....|....*...
gi 515518310 320 YAASGGTVLGICGGFQML 337
Cdd:TIGR01737 74 FAEKGVPVLGICNGFQIL 91
|
|
| hisH |
PRK13146 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
308-385 |
5.95e-03 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237290 [Multi-domain] Cd Length: 209 Bit Score: 38.22 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 308 LQKSGMAEAIQNYAASGGT-VLGICGGFQMLgqiiADpEGSEGqaGRFQGLNLLP-----IRTVITGQKIarqrqvssny 381
Cdd:PRK13146 60 LRAVGLGEAVIEAVLAAGRpFLGICVGMQLL----FE-RGLEH--GDTPGLGLIPgevvrFQPDGPALKV---------- 122
|
....
gi 515518310 382 PQMG 385
Cdd:PRK13146 123 PHMG 126
|
|
| hisH |
PRK13143 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
303-385 |
9.42e-03 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 37.54 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515518310 303 ADLIVLQ-----KSGMA------EAIQNYAASGGTVLGICGGFQMLgqiiadPEGSEgQAGRFQGLNLLPIRTVitgqKI 371
Cdd:PRK13143 39 ADGIVLPgvgafGAAMEnlsplrDVILEAARSGKPFLGICLGMQLL------FESSE-EGGGVRGLGLFPGRVV----RF 107
|
90
....*....|....
gi 515518310 372 ARQRQVssnyPQMG 385
Cdd:PRK13143 108 PAGVKV----PHMG 117
|
|
| |
