|
Name |
Accession |
Description |
Interval |
E-value |
| ATPS |
cd00517 |
ATP-sulfurylase; ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, ... |
244-607 |
0e+00 |
|
ATP-sulfurylase; ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, catalyzes the transfer of an adenylyl group from ATP to sulfate, forming adenosine 5'-phosphosulfate (APS). This reaction is generally accompanied by a further reaction, catalyzed by APS kinase, in which APS is phosphorylated to yield 3'-phospho-APS (PAPS). In some organisms the APS kinase is a separate protein, while in others it is incorporated with ATP sulfurylase in a bifunctional enzyme that catalyzes both reactions. In bifunctional proteins, the domain that performs the kinase activity can be attached at the N-terminal end of the sulfurylase unit or at the C-terminal end, depending on the organism. While the reaction is ubiquitous among organisms, the physiological role of the reaction varies. In some organisms it is used to generate APS from sulfate and ATP, while in others it proceeds in the opposite direction to generate ATP from APS and pyrophosphate. ATP sulfurylase can be a monomer, a homodimer, or a homo-oligomer, depending on the organism. ATPS belongs to a large superfamily of nucleotidyltransferases that includes pantothenate synthetase (PanC), phosphopantetheine adenylyltransferase (PPAT), and the amino-acyl tRNA synthetases. The enzymes of this family are structurally similar and share a dinucleotide-binding domain.
Pssm-ID: 173895 [Multi-domain] Cd Length: 353 Bit Score: 522.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 244 LPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDDgvINMSIPIVLPVSAEDKTRLEGCSKFVLAHGGR 323
Cdd:cd00517 1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDG--TLWPIPIVLDVSEEDAKRLKEGERVALRYPGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 324 RVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRWNDgLDQYRLTPLELKQKCKEMNAD 403
Cdd:cd00517 79 PLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD-FDQYRLTPAELRALFKERGWR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 404 AVFAFQLRNPVHNGHALLMQDTRRRLLErgykhPVLLLHPLGGWTKDDDVPLDWRMKQHAAVLEEGVLdPKSTIVAIFPS 483
Cdd:cd00517 158 RVVAFQTRNPMHRAHEELMKRAAEKLLN-----DGLLLHPLVGWTKPGDVPDEVRMRAYEALLEEYYL-PERTVLAILPL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 484 PMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMApglTSVEIIPFRVAAYNKAKKAMD 563
Cdd:cd00517 232 PMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEIFKKLAPE---LGIEPVPFREAAYCPKCDGMA 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 34447231 564 FYDPARHNE-FDFISGTRMRKLAREGENPPDGFMAPKAWKVLTDY 607
Cdd:cd00517 309 SEDTCPHGEdFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
|
|
| sopT |
TIGR00339 |
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free ... |
226-606 |
7.84e-139 |
|
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free sulfate, the first step in the formation of the activated sulfate donor 3'-phosphoadenylylsulfate (PAPS). In some cases, it is found in a bifunctional protein in which the other domain, APS kinase, catalyzes the second and final step, the phosphorylation of APS to PAPS; the combined ATP sulfurylase/APS kinase may be called PAPS synthase. Members of this family also include the dissimilatory sulfate adenylyltransferase (sat) of the sulfate reducer Archaeoglobus fulgidus. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 273023 Cd Length: 383 Bit Score: 409.08 E-value: 7.84e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 226 ELFVPENKLDH-VRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHfDTLLDDGViNMSIPIVLPVSA 304
Cdd:TIGR00339 8 ELVVRDPDEEHkLLAEAESLPSITLSDRQLCDLELLGNGAFSPLEGFMNEADYDSVVE-SMRLSDGV-LFSVPITLDIDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 305 EDKTRLEGCSKFVLAH-GGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRWnDGL 383
Cdd:TIGR00339 86 EDADDIKLGDRIALTDpKGQPLAILTIEEVYKPNKEKEAKKVFGTTDPEHPGVVYLNTAGNYYIGGPIEVINLPKF-YDF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 384 DQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMQDTRRRLlergyKHPVLLLHPLGGWTKDDDVPLDWRMKQHA 463
Cdd:TIGR00339 165 PRFRFTPAELREEFKERGWDTVVAFQTRNPMHRAHEELTKRAAERL-----PNAGVLVHPLVGLTKPGDIPAEVRMRAYE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 464 aVLEEGVLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMAPGLT 543
Cdd:TIGR00339 240 -VLKEGYPNPERTVVSFLPLAMRYAGPREAIWHAIIRKNYGATHFIVGRDHAGPGSNSKGQDFYGPYDAQELFEKYKAEL 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34447231 544 SVEIIPFRVAAYNKAKKAMDFYDPARHNEFDF--ISGTRMRKLAREGENPPDGFMAPKAWKVLTD 606
Cdd:TIGR00339 319 GIKIVPFRHVAYCPDEDEYAPADQAGHTNLRTlnISGTKLRGMLRNGVFPPEWFSRPEVVKILRE 383
|
|
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
23-217 |
1.43e-103 |
|
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 440295 [Multi-domain] Cd Length: 189 Bit Score: 311.25 E-value: 1.43e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 23 HHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRR 102
Cdd:COG0529 1 SAVTREERAA----LKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 103 IAEVAKLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDY 182
Cdd:COG0529 77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEG--EFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154
|
170 180 190
....*....|....*....|....*....|....*
gi 34447231 183 EKPETPERVLKTNLSTVSDCVHQVVELLQEQNIVP 217
Cdd:COG0529 155 EAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
44-194 |
1.33e-99 |
|
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.
Pssm-ID: 238985 [Multi-domain] Cd Length: 149 Bit Score: 299.78 E-value: 1.33e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 44 TVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITSFIS 123
Cdd:cd02027 1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34447231 124 PFAKDRENARKIHEsaGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKT 194
Cdd:cd02027 81 PYREDREAARKIIG--GGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
41-194 |
2.02e-96 |
|
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.
Pssm-ID: 396247 [Multi-domain] Cd Length: 154 Bit Score: 291.53 E-value: 2.02e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 41 RGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITS 120
Cdd:pfam01583 1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34447231 121 FISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKT 194
Cdd:pfam01583 81 FISPYREDREQARELHEEG--KFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDT 152
|
|
| ATP-sulfurylase |
pfam01747 |
ATP-sulfurylase; This domain is the catalytic domain of ATP-sulfurylase or sulfate ... |
384-607 |
5.62e-92 |
|
ATP-sulfurylase; This domain is the catalytic domain of ATP-sulfurylase or sulfate adenylyltransferase EC:2.7.7.4 some of which are part of a bifunctional polypeptide chain associated with adenosyl phosphosulphate (APS) kinase pfam01583. Both enzymes are required for PAPS (phosphoadenosine-phosphosulfate) synthesis from inorganic sulphate. ATP sulfurylase catalyzes the synthesis of adenosine-phosphosulfate APS from ATP and inorganic sulphate.
Pssm-ID: 460310 Cd Length: 213 Bit Score: 282.51 E-value: 5.62e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 384 DQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMQDTRRRLlERGYkhpvLLLHPLGGWTKDDDVPLDWRMKQHA 463
Cdd:pfam01747 1 DEYRLTPAETRALFKEKGWRTVVAFQTRNPLHRAHEELMKRALEEL-EADG----LLLHPLVGPTKPGDVPAEVRVRCYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 464 AVLEEgVLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHpetkkdLYEPTHGGKVLSMAPGLT 543
Cdd:pfam01747 76 ALLEN-YLPPDRVVLALLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGVGD------FYGPYDAQEIFDEYPGEL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34447231 544 SVEIIPFRVAAYNKAKKAM-DFYDPARHNEFDFISGTRMRKLAREGENPPDGFMAPKAWKVLTDY 607
Cdd:pfam01747 149 GIEPVPFREAVYCKKCGEMaSTKCPHGGEDRLFISGTKVRELLREGEEPPEWFSRPEVAKVLREY 213
|
|
| PRK03846 |
PRK03846 |
adenylylsulfate kinase; Provisional |
15-216 |
7.92e-90 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179661 Cd Length: 198 Bit Score: 276.44 E-value: 7.92e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 15 STNVVYQAHHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPG 94
Cdd:PRK03846 1 DENIVWHQHPVTKAQREQ----LHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 95 DREENIRRIAEVAKLFADAGLVCITSFISPFAKDRENARKIhesagLP---FFEIFVDAPLNICESRDVKGLYKRARAGE 171
Cdd:PRK03846 77 DRKENIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRER-----LGegeFIEVFVDTPLAICEARDPKGLYKKARAGE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 34447231 172 IKGFTGIDSDYEKPETPERVLKTNLSTVSDCVHQVVELLQEQNIV 216
Cdd:PRK03846 152 IRNFTGIDSVYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDII 196
|
|
| apsK |
TIGR00455 |
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ... |
24-210 |
5.41e-81 |
|
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion protein with sulfate adenylyltransferase. Important residue (active site in E.coli) is residue 100 of the seed alignment. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 129547 Cd Length: 184 Bit Score: 253.16 E-value: 5.41e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 24 HVSRNKRGQVVGTRGgfrgCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRI 103
Cdd:TIGR00455 4 AITKDERQALNGHRG----VVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 104 AEVAKLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYE 183
Cdd:TIGR00455 80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKG--EFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYE 157
|
170 180
....*....|....*....|....*..
gi 34447231 184 KPETPERVLKTNLSTVSDCVHQVVELL 210
Cdd:TIGR00455 158 APENPEVVLDTDQNDREECVGQIIEKL 184
|
|
| MET3 |
COG2046 |
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP ... |
226-613 |
5.85e-72 |
|
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP sulfurylase (sulfate adenylyltransferase) is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 441649 Cd Length: 388 Bit Score: 236.58 E-value: 5.85e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 226 ELFVPENKLDHVRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQV---MHfdtlLDDGVInMSIPIVLPV 302
Cdd:COG2046 14 NRVVPGEEREALLEEAKGLPSIELSSRALSDLEMIAIGGFSPLTGFMNKADYESVvenMR----LADGLL-WPIPITLDV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 303 SAEDKTRLEGCSKFVL-AHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRWND 381
Cdd:COG2046 89 SEEDAAGLKEGDEVALrDEEGEPLAVLEVEEIYEYDKEEEAEKVYGTTDPAHPGVAKLYERGDVYLGGPITLLNRPKHPD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 382 gLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMqdtrRRLLERGYkhpVLLLHPLGGWTKDDDVPLDWRMKQ 461
Cdd:COG2046 169 -FPDYRLTPAETRALFEEKGWKTVVAFQTRNPMHRAHEYLQ----KRALETVD---GLLIHPLVGETKPGDIPAEVRVRC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 462 HAAVLEEGVlDPKSTIVAIFPSPMLYAGPTEVQWH--CRSRMiaGANFYIVGRDPAGMPhpetkkDLYEP--------TH 531
Cdd:COG2046 241 YEALLENYY-PKDRVLLSGLPLAMRYAGPREALLHaiIRKNY--GCTHFIVGRDHAGVG------DYYGPydaqeifdEF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 532 GGKVLSMapgltsvEIIPFRVAAYNKAKKAMDFYDPARHNEFDF--ISGTRMRKLAREGENPPDGFMAPKAWKVLTDYYR 609
Cdd:COG2046 312 PPGELGI-------EPLKFEEAFYCKKCGGMATSKTCPHDKEDRvsLSGTKVREMLREGEEPPPEFSRPEVAEILRKYYQ 384
|
....
gi 34447231 610 SLEK 613
Cdd:COG2046 385 PFGE 388
|
|
| sat |
PRK04149 |
sulfate adenylyltransferase; Reviewed |
226-612 |
5.78e-62 |
|
sulfate adenylyltransferase; Reviewed
Pssm-ID: 235227 Cd Length: 391 Bit Score: 210.10 E-value: 5.78e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 226 ELFVPENKLDHVRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDDGVinMSIPIVLPVSAE 305
Cdd:PRK04149 13 NRVVEGRDREEILEEAESLPRIELDERAASDLEMIAIGGFSPLTGFMGREDYDSVVEEMRLANGLV--WSIPITLDVSEE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 306 DKTRLEGCSKFVLAHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRwNDGLDQ 385
Cdd:PRK04149 91 DAASLKEGDEVALVYKGEPYGVLEVEEIYTYDKKKEAEKVYKTTDEKHPGVKKLYEQGDVYLAGPVTLLNRKF-HEPFPR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 386 YRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMqdtrrrllergyKHPV-----LLLHPLGGWTKDDDVPLDWRMK 460
Cdd:PRK04149 170 FWLTPAETRELFEEKGWKTVVAFQTRNPPHRAHEYLQ------------KCALeivdgLLLNPLVGETKSGDIPAEVRME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 461 QHAAVLeEGVLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMphpetkKDLYEPTHGGKVLSM-- 538
Cdd:PRK04149 238 AYEALL-KNYYPKDRVLLSVTPAAMRYAGPREAIFHAIVRKNYGCTHFIVGRDHAGV------GDYYGPYDAQEIFDEft 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34447231 539 APGLtSVEIIPFRVAAYNKAKKAMDFYDPARHNEFD--FISGTRMRKLAREGENPPDGFMAPKAWKVLTDYYRSLE 612
Cdd:PRK04149 311 EEEL-GITPLKFEEAFYCPKCGGMASEKTCPHGKEDrvHLSGTKVREMLREGEKPPPEFSRPEVAEVLIKGLKKYG 385
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ATPS |
cd00517 |
ATP-sulfurylase; ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, ... |
244-607 |
0e+00 |
|
ATP-sulfurylase; ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, catalyzes the transfer of an adenylyl group from ATP to sulfate, forming adenosine 5'-phosphosulfate (APS). This reaction is generally accompanied by a further reaction, catalyzed by APS kinase, in which APS is phosphorylated to yield 3'-phospho-APS (PAPS). In some organisms the APS kinase is a separate protein, while in others it is incorporated with ATP sulfurylase in a bifunctional enzyme that catalyzes both reactions. In bifunctional proteins, the domain that performs the kinase activity can be attached at the N-terminal end of the sulfurylase unit or at the C-terminal end, depending on the organism. While the reaction is ubiquitous among organisms, the physiological role of the reaction varies. In some organisms it is used to generate APS from sulfate and ATP, while in others it proceeds in the opposite direction to generate ATP from APS and pyrophosphate. ATP sulfurylase can be a monomer, a homodimer, or a homo-oligomer, depending on the organism. ATPS belongs to a large superfamily of nucleotidyltransferases that includes pantothenate synthetase (PanC), phosphopantetheine adenylyltransferase (PPAT), and the amino-acyl tRNA synthetases. The enzymes of this family are structurally similar and share a dinucleotide-binding domain.
Pssm-ID: 173895 [Multi-domain] Cd Length: 353 Bit Score: 522.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 244 LPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDDgvINMSIPIVLPVSAEDKTRLEGCSKFVLAHGGR 323
Cdd:cd00517 1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDG--TLWPIPIVLDVSEEDAKRLKEGERVALRYPGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 324 RVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRWNDgLDQYRLTPLELKQKCKEMNAD 403
Cdd:cd00517 79 PLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD-FDQYRLTPAELRALFKERGWR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 404 AVFAFQLRNPVHNGHALLMQDTRRRLLErgykhPVLLLHPLGGWTKDDDVPLDWRMKQHAAVLEEGVLdPKSTIVAIFPS 483
Cdd:cd00517 158 RVVAFQTRNPMHRAHEELMKRAAEKLLN-----DGLLLHPLVGWTKPGDVPDEVRMRAYEALLEEYYL-PERTVLAILPL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 484 PMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMApglTSVEIIPFRVAAYNKAKKAMD 563
Cdd:cd00517 232 PMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEIFKKLAPE---LGIEPVPFREAAYCPKCDGMA 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 34447231 564 FYDPARHNE-FDFISGTRMRKLAREGENPPDGFMAPKAWKVLTDY 607
Cdd:cd00517 309 SEDTCPHGEdFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
|
|
| sopT |
TIGR00339 |
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free ... |
226-606 |
7.84e-139 |
|
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free sulfate, the first step in the formation of the activated sulfate donor 3'-phosphoadenylylsulfate (PAPS). In some cases, it is found in a bifunctional protein in which the other domain, APS kinase, catalyzes the second and final step, the phosphorylation of APS to PAPS; the combined ATP sulfurylase/APS kinase may be called PAPS synthase. Members of this family also include the dissimilatory sulfate adenylyltransferase (sat) of the sulfate reducer Archaeoglobus fulgidus. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 273023 Cd Length: 383 Bit Score: 409.08 E-value: 7.84e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 226 ELFVPENKLDH-VRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHfDTLLDDGViNMSIPIVLPVSA 304
Cdd:TIGR00339 8 ELVVRDPDEEHkLLAEAESLPSITLSDRQLCDLELLGNGAFSPLEGFMNEADYDSVVE-SMRLSDGV-LFSVPITLDIDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 305 EDKTRLEGCSKFVLAH-GGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRWnDGL 383
Cdd:TIGR00339 86 EDADDIKLGDRIALTDpKGQPLAILTIEEVYKPNKEKEAKKVFGTTDPEHPGVVYLNTAGNYYIGGPIEVINLPKF-YDF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 384 DQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMQDTRRRLlergyKHPVLLLHPLGGWTKDDDVPLDWRMKQHA 463
Cdd:TIGR00339 165 PRFRFTPAELREEFKERGWDTVVAFQTRNPMHRAHEELTKRAAERL-----PNAGVLVHPLVGLTKPGDIPAEVRMRAYE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 464 aVLEEGVLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMAPGLT 543
Cdd:TIGR00339 240 -VLKEGYPNPERTVVSFLPLAMRYAGPREAIWHAIIRKNYGATHFIVGRDHAGPGSNSKGQDFYGPYDAQELFEKYKAEL 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34447231 544 SVEIIPFRVAAYNKAKKAMDFYDPARHNEFDF--ISGTRMRKLAREGENPPDGFMAPKAWKVLTD 606
Cdd:TIGR00339 319 GIKIVPFRHVAYCPDEDEYAPADQAGHTNLRTlnISGTKLRGMLRNGVFPPEWFSRPEVVKILRE 383
|
|
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
23-217 |
1.43e-103 |
|
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 440295 [Multi-domain] Cd Length: 189 Bit Score: 311.25 E-value: 1.43e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 23 HHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRR 102
Cdd:COG0529 1 SAVTREERAA----LKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 103 IAEVAKLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDY 182
Cdd:COG0529 77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEG--EFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154
|
170 180 190
....*....|....*....|....*....|....*
gi 34447231 183 EKPETPERVLKTNLSTVSDCVHQVVELLQEQNIVP 217
Cdd:COG0529 155 EAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
44-194 |
1.33e-99 |
|
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.
Pssm-ID: 238985 [Multi-domain] Cd Length: 149 Bit Score: 299.78 E-value: 1.33e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 44 TVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITSFIS 123
Cdd:cd02027 1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34447231 124 PFAKDRENARKIHEsaGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKT 194
Cdd:cd02027 81 PYREDREAARKIIG--GGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
41-194 |
2.02e-96 |
|
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.
Pssm-ID: 396247 [Multi-domain] Cd Length: 154 Bit Score: 291.53 E-value: 2.02e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 41 RGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITS 120
Cdd:pfam01583 1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34447231 121 FISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKT 194
Cdd:pfam01583 81 FISPYREDREQARELHEEG--KFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDT 152
|
|
| ATP-sulfurylase |
pfam01747 |
ATP-sulfurylase; This domain is the catalytic domain of ATP-sulfurylase or sulfate ... |
384-607 |
5.62e-92 |
|
ATP-sulfurylase; This domain is the catalytic domain of ATP-sulfurylase or sulfate adenylyltransferase EC:2.7.7.4 some of which are part of a bifunctional polypeptide chain associated with adenosyl phosphosulphate (APS) kinase pfam01583. Both enzymes are required for PAPS (phosphoadenosine-phosphosulfate) synthesis from inorganic sulphate. ATP sulfurylase catalyzes the synthesis of adenosine-phosphosulfate APS from ATP and inorganic sulphate.
Pssm-ID: 460310 Cd Length: 213 Bit Score: 282.51 E-value: 5.62e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 384 DQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMQDTRRRLlERGYkhpvLLLHPLGGWTKDDDVPLDWRMKQHA 463
Cdd:pfam01747 1 DEYRLTPAETRALFKEKGWRTVVAFQTRNPLHRAHEELMKRALEEL-EADG----LLLHPLVGPTKPGDVPAEVRVRCYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 464 AVLEEgVLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHpetkkdLYEPTHGGKVLSMAPGLT 543
Cdd:pfam01747 76 ALLEN-YLPPDRVVLALLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGVGD------FYGPYDAQEIFDEYPGEL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34447231 544 SVEIIPFRVAAYNKAKKAM-DFYDPARHNEFDFISGTRMRKLAREGENPPDGFMAPKAWKVLTDY 607
Cdd:pfam01747 149 GIEPVPFREAVYCKKCGEMaSTKCPHGGEDRLFISGTKVRELLREGEEPPEWFSRPEVAKVLREY 213
|
|
| PRK03846 |
PRK03846 |
adenylylsulfate kinase; Provisional |
15-216 |
7.92e-90 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179661 Cd Length: 198 Bit Score: 276.44 E-value: 7.92e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 15 STNVVYQAHHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPG 94
Cdd:PRK03846 1 DENIVWHQHPVTKAQREQ----LHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 95 DREENIRRIAEVAKLFADAGLVCITSFISPFAKDRENARKIhesagLP---FFEIFVDAPLNICESRDVKGLYKRARAGE 171
Cdd:PRK03846 77 DRKENIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRER-----LGegeFIEVFVDTPLAICEARDPKGLYKKARAGE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 34447231 172 IKGFTGIDSDYEKPETPERVLKTNLSTVSDCVHQVVELLQEQNIV 216
Cdd:PRK03846 152 IRNFTGIDSVYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDII 196
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
13-213 |
3.82e-86 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 281.05 E-value: 3.82e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 13 QKSTNVVYQAHHVSRNKRGqvvgTRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFS 92
Cdd:PRK05506 435 RRATNVHWQASDVSREARA----ARKGQKPATVWFTGLSGSGKSTIANLVERRLHALGRHTYLLDGDNVRHGLNRDLGFS 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 93 PGDREENIRRIAEVAKLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEI 172
Cdd:PRK05506 511 DADRVENIRRVAEVARLMADAGLIVLVSFISPFREERELARALHGEG--EFVEVFVDTPLEVCEARDPKGLYAKARAGEI 588
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 34447231 173 KGFTGIDSDYEKPETPERVLKTNLSTVSDCVHQVVELLQEQ 213
Cdd:PRK05506 589 KNFTGIDSPYEAPENPELRLDTTGRSPEELAEQVLELLRRR 629
|
|
| apsK |
TIGR00455 |
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ... |
24-210 |
5.41e-81 |
|
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion protein with sulfate adenylyltransferase. Important residue (active site in E.coli) is residue 100 of the seed alignment. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 129547 Cd Length: 184 Bit Score: 253.16 E-value: 5.41e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 24 HVSRNKRGQVVGTRGgfrgCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRI 103
Cdd:TIGR00455 4 AITKDERQALNGHRG----VVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 104 AEVAKLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYE 183
Cdd:TIGR00455 80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKG--EFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYE 157
|
170 180
....*....|....*....|....*..
gi 34447231 184 KPETPERVLKTNLSTVSDCVHQVVELL 210
Cdd:TIGR00455 158 APENPEVVLDTDQNDREECVGQIIEKL 184
|
|
| MET3 |
COG2046 |
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP ... |
226-613 |
5.85e-72 |
|
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP sulfurylase (sulfate adenylyltransferase) is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 441649 Cd Length: 388 Bit Score: 236.58 E-value: 5.85e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 226 ELFVPENKLDHVRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQV---MHfdtlLDDGVInMSIPIVLPV 302
Cdd:COG2046 14 NRVVPGEEREALLEEAKGLPSIELSSRALSDLEMIAIGGFSPLTGFMNKADYESVvenMR----LADGLL-WPIPITLDV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 303 SAEDKTRLEGCSKFVL-AHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRWND 381
Cdd:COG2046 89 SEEDAAGLKEGDEVALrDEEGEPLAVLEVEEIYEYDKEEEAEKVYGTTDPAHPGVAKLYERGDVYLGGPITLLNRPKHPD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 382 gLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMqdtrRRLLERGYkhpVLLLHPLGGWTKDDDVPLDWRMKQ 461
Cdd:COG2046 169 -FPDYRLTPAETRALFEEKGWKTVVAFQTRNPMHRAHEYLQ----KRALETVD---GLLIHPLVGETKPGDIPAEVRVRC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 462 HAAVLEEGVlDPKSTIVAIFPSPMLYAGPTEVQWH--CRSRMiaGANFYIVGRDPAGMPhpetkkDLYEP--------TH 531
Cdd:COG2046 241 YEALLENYY-PKDRVLLSGLPLAMRYAGPREALLHaiIRKNY--GCTHFIVGRDHAGVG------DYYGPydaqeifdEF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 532 GGKVLSMapgltsvEIIPFRVAAYNKAKKAMDFYDPARHNEFDF--ISGTRMRKLAREGENPPDGFMAPKAWKVLTDYYR 609
Cdd:COG2046 312 PPGELGI-------EPLKFEEAFYCKKCGGMATSKTCPHDKEDRvsLSGTKVREMLREGEEPPPEFSRPEVAEILRKYYQ 384
|
....
gi 34447231 610 SLEK 613
Cdd:COG2046 385 PFGE 388
|
|
| PRK00889 |
PRK00889 |
adenylylsulfate kinase; Provisional |
41-217 |
1.21e-69 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179157 Cd Length: 175 Bit Score: 222.97 E-value: 1.21e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 41 RGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITS 120
Cdd:PRK00889 3 RGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 121 FISPFAKDRENARkihesAGLP-FFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKTNLSTV 199
Cdd:PRK00889 83 AISPYRETREEVR-----ANIGnFLEVFVDAPLEVCEQRDVKGLYAKARAGEIKHFTGIDDPYEPPLNPEVECRTDLESL 157
|
170
....*....|....*...
gi 34447231 200 SDCVHQVVELLQEQNIVP 217
Cdd:PRK00889 158 EESVDKVLQKLEELGYLV 175
|
|
| PUA_2 |
pfam14306 |
PUA-like domain; This PUA like domain is found at the N-terminus of ATP-sulfurylase enzymes. |
226-376 |
2.24e-66 |
|
PUA-like domain; This PUA like domain is found at the N-terminus of ATP-sulfurylase enzymes.
Pssm-ID: 464131 [Multi-domain] Cd Length: 159 Bit Score: 213.92 E-value: 2.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 226 ELFVPENKLDHVRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTlLDDGVInMSIPIVLPVSAE 305
Cdd:pfam14306 10 DLVVRDAEREELLAEAAELPSIELSKRELCDLELIAIGGFSPLTGFMGEADYLSVLEFMR-LADGLL-WSIPITLDVSEE 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34447231 306 DKTRLEGCSKFVLAHG-GRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEK 376
Cdd:pfam14306 88 DAASLKEGDRVALRDPeGEPLAILTVEEIYEPDKEEEAEKVFGTTDPAHPGVKKLYEQGDFYVGGDIEVLNR 159
|
|
| sat |
PRK04149 |
sulfate adenylyltransferase; Reviewed |
226-612 |
5.78e-62 |
|
sulfate adenylyltransferase; Reviewed
Pssm-ID: 235227 Cd Length: 391 Bit Score: 210.10 E-value: 5.78e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 226 ELFVPENKLDHVRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDDGVinMSIPIVLPVSAE 305
Cdd:PRK04149 13 NRVVEGRDREEILEEAESLPRIELDERAASDLEMIAIGGFSPLTGFMGREDYDSVVEEMRLANGLV--WSIPITLDVSEE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 306 DKTRLEGCSKFVLAHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRwNDGLDQ 385
Cdd:PRK04149 91 DAASLKEGDEVALVYKGEPYGVLEVEEIYTYDKKKEAEKVYKTTDEKHPGVKKLYEQGDVYLAGPVTLLNRKF-HEPFPR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 386 YRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMqdtrrrllergyKHPV-----LLLHPLGGWTKDDDVPLDWRMK 460
Cdd:PRK04149 170 FWLTPAETRELFEEKGWKTVVAFQTRNPPHRAHEYLQ------------KCALeivdgLLLNPLVGETKSGDIPAEVRME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 461 QHAAVLeEGVLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMphpetkKDLYEPTHGGKVLSM-- 538
Cdd:PRK04149 238 AYEALL-KNYYPKDRVLLSVTPAAMRYAGPREAIFHAIVRKNYGCTHFIVGRDHAGV------GDYYGPYDAQEIFDEft 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34447231 539 APGLtSVEIIPFRVAAYNKAKKAMDFYDPARHNEFD--FISGTRMRKLAREGENPPDGFMAPKAWKVLTDYYRSLE 612
Cdd:PRK04149 311 EEEL-GITPLKFEEAFYCPKCGGMASEKTCPHGKEDrvHLSGTKVREMLREGEKPPPEFSRPEVAEVLIKGLKKYG 385
|
|
| PRK05537 |
PRK05537 |
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase; |
42-213 |
1.04e-53 |
|
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
Pssm-ID: 180124 [Multi-domain] Cd Length: 568 Bit Score: 192.58 E-value: 1.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 42 GCTVWLTGLSGAGKTTISFALEEYLVSH-AIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITS 120
Cdd:PRK05537 392 GFTVFFTGLSGAGKSTIAKALMVKLMEMrGRPVTLLDGDVVRKHLSSELGFSKEDRDLNILRIGFVASEITKNGGIAICA 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 121 FISPFAKDRENARKIHESAGlPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKTNLSTVS 200
Cdd:PRK05537 472 PIAPYRATRREVREMIEAYG-GFIEVHVATPLEVCEQRDRKGLYAKAREGKIKGFTGISDPYEPPANPELVIDTTNVTPD 550
|
170
....*....|...
gi 34447231 201 DCVHQVVELLQEQ 213
Cdd:PRK05537 551 ECAHKILLYLEEK 563
|
|
| PRK05537 |
PRK05537 |
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase; |
215-604 |
6.59e-51 |
|
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
Pssm-ID: 180124 [Multi-domain] Cd Length: 568 Bit Score: 184.87 E-value: 6.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 215 IVPYTiiKDIHELFVPENKLDHVRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHfDTLLDDGVInM 294
Cdd:PRK05537 2 ILPNG--GPLPNLYVSPESREKLKAEALSLPSLDLSPRQICDLELLMNGGFSPLKGFMGRADYECVLE-NMRLADGTL-W 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 295 SIPIVLPVSAEDKTRLEGCSKFVLAHG-GRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHI-KMVMESGDWLVGGDLQ 372
Cdd:PRK05537 78 PIPITLDVSEKFAAGLEIGERIALRDQeGVLLAILTVSDIWEPDKEREAEAVFGTTDPAHPGVnYLHRWAGKFYLGGPLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 373 VLEKIRWNDgLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLmqdTRRRLLERGYKhpvLLLHPLGGWTKDDD 452
Cdd:PRK05537 158 GIQLPVHYD-FVQLRLTPAELRARFRKLGWRRVVAFQTRNPLHRAHEEL---TKRAAREVGAN---LLIHPVVGMTKPGD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 453 VPLDWRMKQHAAVLEEgvLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHG 532
Cdd:PRK05537 231 IDHFTRVRCYEALLDK--YPPATTLLSLLPLAMRMAGPREALWHAIIRRNYGCTHFIVGRDHAGPGKDSRGKPFYGPYDA 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34447231 533 GKVLSMAPGLTSVEIIPFRVAAYNKAKKAMDFYDPARHNE-FDFISGTRMRKLAREGENPPDGFMAPKAWKVL 604
Cdd:PRK05537 309 QELFAKYADEIGITMVPFKEMVYVQDKAQYVPVDEVPQGAtVLTISGTELRRRLREGLEIPEWFSFPEVVAEL 381
|
|
| PRK05541 |
PRK05541 |
adenylylsulfate kinase; Provisional |
42-215 |
1.44e-23 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 235498 Cd Length: 176 Bit Score: 97.82 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 42 GCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNlGFSPGDREENIRRIAEVAKLFADAGLVCITSF 121
Cdd:PRK05541 7 GYVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELREILGHY-GYDKQSRIEMALKRAKLAKFLADQGMIVIVTT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 122 ISPFakdRENARkiHESAGLP-FFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKTNLSTVS 200
Cdd:PRK05541 86 ISMF---DEIYA--YNRKHLPnYFEVYLKCDMEELIRRDQKGLYTKALKGEIKNVVGVDIPFDEPKADLVIDNSCRTSLD 160
|
170
....*....|....*
gi 34447231 201 DCVHQVVELLQEQNI 215
Cdd:PRK05541 161 EKVDLILNKLKLRLI 175
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
45-176 |
2.33e-08 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 53.76 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 45 VWLTGLSGAGKTTISFALEEYLvsHAIPcysLDGDNVRHGLnRNLGFSPGDREENIR-----RIAEVAKLFADAGLVCIt 119
Cdd:COG0645 2 ILVCGLPGSGKSTLARALAERL--GAVR---LRSDVVRKRL-FGAGLAPLERSPEATartyaRLLALARELLAAGRSVI- 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 34447231 120 sFISPFAK--DRENARKIHESAGLPFFEIFVDAPLNICESRdvkgLYKRARAGEIKGFT 176
Cdd:COG0645 75 -LDATFLRraQREAFRALAEEAGAPFVLIWLDAPEEVLRER----LEARNAEGGDSDAT 128
|
|
| Kti12 |
COG4088 |
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ... |
47-212 |
1.87e-07 |
|
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];
Pssm-ID: 443264 [Multi-domain] Cd Length: 179 Bit Score: 51.27 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 47 LTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPgDREENIRRIAE-VAKLFADAGLVCITSFISPF 125
Cdd:COG4088 9 LTGPPGSGKTTFAKALAQRLYAEGIAVALLHSDDFRRFLVNESFPKE-TYEEVVEDVRTtTADNALDNGYSVIVDGTFYY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 126 AKDRENARKIHESAGlPFFEIFVDAPLNICESRDvkglykRARAGEI--KGFTGIDSDYEKPET---PERVLKTNLSTVS 200
Cdd:COG4088 88 RSWQRDFRNLAKHKA-PIHIIYLKAPLETALRRN------RERGEPIpeRVIARMYRKFDKPGTkdrPDLVIDTTEDSVS 160
|
170
....*....|..
gi 34447231 201 DCVHQVVELLQE 212
Cdd:COG4088 161 ETLDAILKAIET 172
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
45-171 |
4.61e-06 |
|
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.
Pssm-ID: 463952 [Multi-domain] Cd Length: 143 Bit Score: 46.53 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 45 VWLTGLSGAGKTTISFALEEylvshAIPCYSLDGDNVRHGLNRNLGFSPGDREENI----RRIAEVAKLFADAGLVCITS 120
Cdd:pfam13671 2 ILLVGLPGSGKSTLARRLLE-----ELGAVRLSSDDERKRLFGEGRPSISYYTDATdrtyERLHELARIALRAGRPVILD 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 34447231 121 FisPFAKDRENARKIH--ESAGLPFFEIFVDAPLNICESRDVkglyKRARAGE 171
Cdd:pfam13671 77 A--TNLRRDERARLLAlaREYGVPVRIVVFEAPEEVLRERLA----ARARAGG 123
|
|
| GntK |
cd02021 |
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ... |
47-190 |
1.45e-03 |
|
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.
Pssm-ID: 238979 [Multi-domain] Cd Length: 150 Bit Score: 39.54 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34447231 47 LTGLSGAGKTTISFALeeylvSHAIPCYSLDGDNVRHGLNRNL---GFSPGDRE-----ENIRRIAEVAKLFADAGLVCI 118
Cdd:cd02021 4 VMGVSGSGKSTVGKAL-----AERLGAPFIDGDDLHPPANIAKmaaGIPLNDEDrwpwlQALTDALLAKLASAGEGVVVA 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34447231 119 TSFIspfaKD--RENARKIHESAGLPFfeIFVDAPLNICESRDvkglykRARAGEIKGFTGIDSDYEKPETPER 190
Cdd:cd02021 79 CSAL----KRiyRDILRGGAANPRVRF--VHLDGPREVLAERL------AARKGHFMPADLLDSQFETLEPPGE 140
|
|
| |
