|
Name |
Accession |
Description |
Interval |
E-value |
| ATPS |
cd00517 |
ATP-sulfurylase; ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, ... |
261-644 |
6.66e-177 |
|
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: 506.40 E-value: 6.66e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 261 LPTVELTKVDLQWLQVLAEGWATPLSGFMRERQYLQSMHFGQLLDlkhkvafvgeksddkedswpmmdDINQSIPIVLPI 340
Cdd:cd00517 1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLD-----------------------GTLWPIPIVLDV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 341 SDDVKKGLEGVTRIALKYNGQVYAILSDPEIFEHRKDERVCRQFGTNDPRHPAVAQVLESGNWLLGGDVAVVQKIQFNDg 420
Cdd:cd00517 58 SEEDAKRLKEGERVALRYPGQPLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 421 LDKYRKTPNELRAIFAEKNADAVFAFQLRNPIHNGHALLMRDTREKLLaehkNPILLLHPLGGWTKDDDVPLDIRIKQHE 500
Cdd:cd00517 137 FDQYRLTPAELRALFKERGWRRVVAFQTRNPMHRAHEELMKRAAEKLL----NDGLLLHPLVGWTKPGDVPDEVRMRAYE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 501 AVIAERVLdPEWTVLSIFPSPMMYAGPTEVQWHARSRIAAGIQHYIVGRDPAGIQKPGSPDALYETTHGAKVLSMAPGls 580
Cdd:cd00517 213 ALLEEYYL-PERTVLAILPLPMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEIFKKLAPELG-- 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17542422 581 aLHILPFRVAAYDKTAKKMSFFDTSR-KEDFENISGTKMRGLARNGDTPPEGFMAPTAWEVLAGY 644
Cdd:cd00517 290 -IEPVPFREAAYCPKCDGMASEDTCPhGEDFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
|
|
| sopT |
TIGR00339 |
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free ... |
235-642 |
5.92e-137 |
|
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: 405.61 E-value: 5.92e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 235 PDVPAVRELFVSDDLTVAELLKESQNLPTVELTKVDLQWLQVLAEGWATPLSGFMRERQYLQSMHfgqlldlkhkvafvg 314
Cdd:TIGR00339 1 PHGGKLVELVVRDPDEEHKLLAEAESLPSITLSDRQLCDLELLGNGAFSPLEGFMNEADYDSVVE--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 315 eksddkedSWPMMDDINQSIPIVLPISDDVKKGLEGVTRIALKY-NGQVYAILSDPEIFEHRKDERVCRQFGTNDPRHPA 393
Cdd:TIGR00339 66 --------SMRLSDGVLFSVPITLDIDDEDADDIKLGDRIALTDpKGQPLAILTIEEVYKPNKEKEAKKVFGTTDPEHPG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 394 VAQVLESGNWLLGGDVAVVQKIQFnDGLDKYRKTPNELRAIFAEKNADAVFAFQLRNPIHNGHALLMRDTREKLlaehKN 473
Cdd:TIGR00339 138 VVYLNTAGNYYIGGPIEVINLPKF-YDFPRFRFTPAELREEFKERGWDTVVAFQTRNPMHRAHEELTKRAAERL----PN 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 474 PILLLHPLGGWTKDDDVPLDIRIKQHEaVIAERVLDPEWTVLSIFPSPMMYAGPTEVQWHARSRIAAGIQHYIVGRDPAG 553
Cdd:TIGR00339 213 AGVLVHPLVGLTKPGDIPAEVRMRAYE-VLKEGYPNPERTVVSFLPLAMRYAGPREAIWHAIIRKNYGATHFIVGRDHAG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 554 IQKPGSPDALYETTHGAKVLSMAPGLSALHILPFRVAAYDKTAKKMSFFDTSR--KEDFENISGTKMRGLARNGDTPPEG 631
Cdd:TIGR00339 292 PGSNSKGQDFYGPYDAQELFEKYKAELGIKIVPFRHVAYCPDEDEYAPADQAGhtNLRTLNISGTKLRGMLRNGVFPPEW 371
|
410
....*....|.
gi 17542422 632 FMAPTAWEVLA 642
Cdd:TIGR00339 372 FSRPEVVKILR 382
|
|
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
37-231 |
2.52e-110 |
|
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: 329.74 E-value: 2.52e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 37 HTISREERAAAVGRhegfRGCTIWFTGLSGAGKTTISFALERTLNKLGIPCYGLDGDNIRHGLCKNLGFSKEDRQENIRR 116
Cdd:COG0529 1 SAVTREERAALKGQ----KGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 117 VAEVAKLFADSGMICLAAFISPFQEDRLDARKIHESENvkFIEVHVSTTLEVCEQRDPKQLYKKARAGQILGFTGIDSAY 196
Cdd:COG0529 77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEGE--FIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154
|
170 180 190
....*....|....*....|....*....|....*
gi 17542422 197 EPPENAEIILDAGKDGVQQCVQKVLDHLESKGLLP 231
Cdd:COG0529 155 EAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
55-210 |
2.63e-100 |
|
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: 302.70 E-value: 2.63e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 55 RGCTIWFTGLSGAGKTTISFALERTLNKLGIPCYGLDGDNIRHGLCKNLGFSKEDRQENIRRVAEVAKLFADSGMICLAA 134
Cdd:pfam01583 1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17542422 135 FISPFQEDRLDARKIHESEnvKFIEVHVSTTLEVCEQRDPKQLYKKARAGQILGFTGIDSAYEPPENAEIILDAGK 210
Cdd:pfam01583 81 FISPYREDREQARELHEEG--KFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDTDK 154
|
|
| PRK03846 |
PRK03846 |
adenylylsulfate kinase; Provisional |
29-230 |
3.46e-98 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179661 Cd Length: 198 Bit Score: 299.16 E-value: 3.46e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 29 STNITYQEHTISREERAAavgrHEGFRGCTIWFTGLSGAGKTTISFALERTLNKLGIPCYGLDGDNIRHGLCKNLGFSKE 108
Cdd:PRK03846 1 DENIVWHQHPVTKAQREQ----LHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 109 DRQENIRRVAEVAKLFADSGMICLAAFISPFQEDRLDARKIHESEnvKFIEVHVSTTLEVCEQRDPKQLYKKARAGQILG 188
Cdd:PRK03846 77 DRKENIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEG--EFIEVFVDTPLAICEARDPKGLYKKARAGEIRN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17542422 189 FTGIDSAYEPPENAEIILDAGKDGVQQCVQKVLDHLESKGLL 230
Cdd:PRK03846 155 FTGIDSVYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDII 196
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
58-207 |
6.39e-97 |
|
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: 294.00 E-value: 6.39e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 58 TIWFTGLSGAGKTTISFALERTLNKLGIPCYGLDGDNIRHGLCKNLGFSKEDRQENIRRVAEVAKLFADSGMICLAAFIS 137
Cdd:cd02027 1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 138 PFQEDRLDARKIHESENvkFIEVHVSTTLEVCEQRDPKQLYKKARAGQILGFTGIDSAYEPPENAEIILD 207
Cdd:cd02027 81 PYREDREAARKIIGGGD--FLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLD 148
|
|
| ATP-sulfurylase |
pfam01747 |
ATP-sulfurylase; This domain is the catalytic domain of ATP-sulfurylase or sulfate ... |
422-644 |
7.71e-93 |
|
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: 285.59 E-value: 7.71e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 422 DKYRKTPNELRAIFAEKNADAVFAFQLRNPIHNGHALLMRDTREKLLAEHknpiLLLHPLGGWTKDDDVPLDIRIKQHEA 501
Cdd:pfam01747 1 DEYRLTPAETRALFKEKGWRTVVAFQTRNPLHRAHEELMKRALEELEADG----LLLHPLVGPTKPGDVPAEVRVRCYEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 502 VIaERVLDPEWTVLSIFPSPMMYAGPTEVQWHARSRIAAGIQHYIVGRDPAGiqkPGSpdaLYETTHGAKVLSMAPGLSA 581
Cdd:pfam01747 77 LL-ENYLPPDRVVLALLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAG---VGD---FYGPYDAQEIFDEYPGELG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17542422 582 LHILPFRVAAYDKTAKKM-SFFDTSRKEDFENISGTKMRGLARNGDTPPEGFMAPTAWEVLAGY 644
Cdd:pfam01747 150 IEPVPFREAVYCKKCGEMaSTKCPHGGEDRLFISGTKVRELLREGEEPPEWFSRPEVAKVLREY 213
|
|
| apsK |
TIGR00455 |
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ... |
39-224 |
6.03e-82 |
|
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: 256.63 E-value: 6.03e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 39 ISREERAAavgrHEGFRGCTIWFTGLSGAGKTTISFALERTLNKLGIPCYGLDGDNIRHGLCKNLGFSKEDRQENIRRVA 118
Cdd:TIGR00455 5 ITKDERQA----LNGHRGVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 119 EVAKLFADSGMICLAAFISPFQEDRLDARKIHESenVKFIEVHVSTTLEVCEQRDPKQLYKKARAGQILGFTGIDSAYEP 198
Cdd:TIGR00455 81 EVAKLFVRNGIIVITSFISPYRADRQMVRELIEK--GEFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYEA 158
|
170 180
....*....|....*....|....*.
gi 17542422 199 PENAEIILDAGKDGVQQCVQKVLDHL 224
Cdd:TIGR00455 159 PENPEVVLDTDQNDREECVGQIIEKL 184
|
|
| MET3 |
COG2046 |
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP ... |
242-648 |
2.14e-78 |
|
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: 254.30 E-value: 2.14e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 242 ELFVSDDlTVAELLKESQNLPTVELTKVDLQWLQVLAEGWATPLSGFMRERQYLQSMHFGQLLDlkhkvafvGEksddke 321
Cdd:COG2046 14 NRVVPGE-EREALLEEAKGLPSIELSSRALSDLEMIAIGGFSPLTGFMNKADYESVVENMRLAD--------GL------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 322 dSWPmmddinqsIPIVLPISDDVKKGLEGVTRIALK-YNGQVYAILSDPEIFEHRKdERVCRQ-FGTNDPRHPAVAQVLE 399
Cdd:COG2046 79 -LWP--------IPITLDVSEEDAAGLKEGDEVALRdEEGEPLAVLEVEEIYEYDK-EEEAEKvYGTTDPAHPGVAKLYE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 400 SGNWLLGGDVAVVQKIQFNDgLDKYRKTPNELRAIFAEKNADAVFAFQLRNPIHNGHALLMrdtreKLLAEHKNPiLLLH 479
Cdd:COG2046 149 RGDVYLGGPITLLNRPKHPD-FPDYRLTPAETRALFEEKGWKTVVAFQTRNPMHRAHEYLQ-----KRALETVDG-LLIH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 480 PLGGWTKDDDVPLDIRIKQHEAVIaERVLDPEWTVLSIFPSPMMYAGPTEVQWHARSRIAAGIQHYIVGRDPAGiqkPGS 559
Cdd:COG2046 222 PLVGETKPGDIPAEVRVRCYEALL-ENYYPKDRVLLSGLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAG---VGD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 560 pdaLYET--------THGAKVLSMAPglsalhiLPFRVAAYDKTAKKMSFFDT--SRKEDFENISGTKMRGLARNGDTPP 629
Cdd:COG2046 298 ---YYGPydaqeifdEFPPGELGIEP-------LKFEEAFYCKKCGGMATSKTcpHDKEDRVSLSGTKVREMLREGEEPP 367
|
410
....*....|....*....
gi 17542422 630 EGFMAPTAWEVLAGYYKSL 648
Cdd:COG2046 368 PEFSRPEVAEILRKYYQPF 386
|
|
| sat |
PRK04149 |
sulfate adenylyltransferase; Reviewed |
245-646 |
3.34e-71 |
|
sulfate adenylyltransferase; Reviewed
Pssm-ID: 235227 Cd Length: 391 Bit Score: 235.53 E-value: 3.34e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 245 VSDDLTVAELLKESQNLPTVELTKVDLQWLQVLAEGWATPLSGFMRERQYLQSMHFGQLLDlkhkvafvgeksddkedSW 324
Cdd:PRK04149 15 VVEGRDREEILEEAESLPRIELDERAASDLEMIAIGGFSPLTGFMGREDYDSVVEEMRLAN-----------------GL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 325 PMmddinqSIPIVLPISDDVKKGLEGVTRIALKYNGQVYAILSDPEIFEHRKdERVCRQ-FGTNDPRHPAVAQVLESGNW 403
Cdd:PRK04149 78 VW------SIPITLDVSEEDAASLKEGDEVALVYKGEPYGVLEVEEIYTYDK-KKEAEKvYKTTDEKHPGVKKLYEQGDV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 404 LLGGDVAVVQKIQfNDGLDKYRKTPNELRAIFAEKNADAVFAFQLRNPIHNGHALLMrdtreKLLAEHKNPiLLLHPLGG 483
Cdd:PRK04149 151 YLAGPVTLLNRKF-HEPFPRFWLTPAETRELFEEKGWKTVVAFQTRNPPHRAHEYLQ-----KCALEIVDG-LLLNPLVG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 484 WTKDDDVPLDIRIKQHEAVIaERVLDPEWTVLSIFPSPMMYAGPTEVQWHARSRIAAGIQHYIVGRDPAGIqkpGSPDAL 563
Cdd:PRK04149 224 ETKSGDIPAEVRMEAYEALL-KNYYPKDRVLLSVTPAAMRYAGPREAIFHAIVRKNYGCTHFIVGRDHAGV---GDYYGP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 564 YET----THGAKvlsmaPGLSaLHILPFRVAAYDKTAKKMSFFDT--SRKEDFENISGTKMRGLARNGDTPPEGFMAPTA 637
Cdd:PRK04149 300 YDAqeifDEFTE-----EELG-ITPLKFEEAFYCPKCGGMASEKTcpHGKEDRVHLSGTKVREMLREGEKPPPEFSRPEV 373
|
....*....
gi 17542422 638 WEVLAGYYK 646
Cdd:PRK04149 374 AEVLIKGLK 382
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ATPS |
cd00517 |
ATP-sulfurylase; ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, ... |
261-644 |
6.66e-177 |
|
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: 506.40 E-value: 6.66e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 261 LPTVELTKVDLQWLQVLAEGWATPLSGFMRERQYLQSMHFGQLLDlkhkvafvgeksddkedswpmmdDINQSIPIVLPI 340
Cdd:cd00517 1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLD-----------------------GTLWPIPIVLDV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 341 SDDVKKGLEGVTRIALKYNGQVYAILSDPEIFEHRKDERVCRQFGTNDPRHPAVAQVLESGNWLLGGDVAVVQKIQFNDg 420
Cdd:cd00517 58 SEEDAKRLKEGERVALRYPGQPLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 421 LDKYRKTPNELRAIFAEKNADAVFAFQLRNPIHNGHALLMRDTREKLLaehkNPILLLHPLGGWTKDDDVPLDIRIKQHE 500
Cdd:cd00517 137 FDQYRLTPAELRALFKERGWRRVVAFQTRNPMHRAHEELMKRAAEKLL----NDGLLLHPLVGWTKPGDVPDEVRMRAYE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 501 AVIAERVLdPEWTVLSIFPSPMMYAGPTEVQWHARSRIAAGIQHYIVGRDPAGIQKPGSPDALYETTHGAKVLSMAPGls 580
Cdd:cd00517 213 ALLEEYYL-PERTVLAILPLPMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEIFKKLAPELG-- 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17542422 581 aLHILPFRVAAYDKTAKKMSFFDTSR-KEDFENISGTKMRGLARNGDTPPEGFMAPTAWEVLAGY 644
Cdd:cd00517 290 -IEPVPFREAAYCPKCDGMASEDTCPhGEDFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
|
|
| sopT |
TIGR00339 |
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free ... |
235-642 |
5.92e-137 |
|
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: 405.61 E-value: 5.92e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 235 PDVPAVRELFVSDDLTVAELLKESQNLPTVELTKVDLQWLQVLAEGWATPLSGFMRERQYLQSMHfgqlldlkhkvafvg 314
Cdd:TIGR00339 1 PHGGKLVELVVRDPDEEHKLLAEAESLPSITLSDRQLCDLELLGNGAFSPLEGFMNEADYDSVVE--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 315 eksddkedSWPMMDDINQSIPIVLPISDDVKKGLEGVTRIALKY-NGQVYAILSDPEIFEHRKDERVCRQFGTNDPRHPA 393
Cdd:TIGR00339 66 --------SMRLSDGVLFSVPITLDIDDEDADDIKLGDRIALTDpKGQPLAILTIEEVYKPNKEKEAKKVFGTTDPEHPG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 394 VAQVLESGNWLLGGDVAVVQKIQFnDGLDKYRKTPNELRAIFAEKNADAVFAFQLRNPIHNGHALLMRDTREKLlaehKN 473
Cdd:TIGR00339 138 VVYLNTAGNYYIGGPIEVINLPKF-YDFPRFRFTPAELREEFKERGWDTVVAFQTRNPMHRAHEELTKRAAERL----PN 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 474 PILLLHPLGGWTKDDDVPLDIRIKQHEaVIAERVLDPEWTVLSIFPSPMMYAGPTEVQWHARSRIAAGIQHYIVGRDPAG 553
Cdd:TIGR00339 213 AGVLVHPLVGLTKPGDIPAEVRMRAYE-VLKEGYPNPERTVVSFLPLAMRYAGPREAIWHAIIRKNYGATHFIVGRDHAG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 554 IQKPGSPDALYETTHGAKVLSMAPGLSALHILPFRVAAYDKTAKKMSFFDTSR--KEDFENISGTKMRGLARNGDTPPEG 631
Cdd:TIGR00339 292 PGSNSKGQDFYGPYDAQELFEKYKAELGIKIVPFRHVAYCPDEDEYAPADQAGhtNLRTLNISGTKLRGMLRNGVFPPEW 371
|
410
....*....|.
gi 17542422 632 FMAPTAWEVLA 642
Cdd:TIGR00339 372 FSRPEVVKILR 382
|
|
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
37-231 |
2.52e-110 |
|
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: 329.74 E-value: 2.52e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 37 HTISREERAAAVGRhegfRGCTIWFTGLSGAGKTTISFALERTLNKLGIPCYGLDGDNIRHGLCKNLGFSKEDRQENIRR 116
Cdd:COG0529 1 SAVTREERAALKGQ----KGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 117 VAEVAKLFADSGMICLAAFISPFQEDRLDARKIHESENvkFIEVHVSTTLEVCEQRDPKQLYKKARAGQILGFTGIDSAY 196
Cdd:COG0529 77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEGE--FIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154
|
170 180 190
....*....|....*....|....*....|....*
gi 17542422 197 EPPENAEIILDAGKDGVQQCVQKVLDHLESKGLLP 231
Cdd:COG0529 155 EAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
55-210 |
2.63e-100 |
|
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: 302.70 E-value: 2.63e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 55 RGCTIWFTGLSGAGKTTISFALERTLNKLGIPCYGLDGDNIRHGLCKNLGFSKEDRQENIRRVAEVAKLFADSGMICLAA 134
Cdd:pfam01583 1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17542422 135 FISPFQEDRLDARKIHESEnvKFIEVHVSTTLEVCEQRDPKQLYKKARAGQILGFTGIDSAYEPPENAEIILDAGK 210
Cdd:pfam01583 81 FISPYREDREQARELHEEG--KFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDTDK 154
|
|
| PRK03846 |
PRK03846 |
adenylylsulfate kinase; Provisional |
29-230 |
3.46e-98 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179661 Cd Length: 198 Bit Score: 299.16 E-value: 3.46e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 29 STNITYQEHTISREERAAavgrHEGFRGCTIWFTGLSGAGKTTISFALERTLNKLGIPCYGLDGDNIRHGLCKNLGFSKE 108
Cdd:PRK03846 1 DENIVWHQHPVTKAQREQ----LHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 109 DRQENIRRVAEVAKLFADSGMICLAAFISPFQEDRLDARKIHESEnvKFIEVHVSTTLEVCEQRDPKQLYKKARAGQILG 188
Cdd:PRK03846 77 DRKENIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEG--EFIEVFVDTPLAICEARDPKGLYKKARAGEIRN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17542422 189 FTGIDSAYEPPENAEIILDAGKDGVQQCVQKVLDHLESKGLL 230
Cdd:PRK03846 155 FTGIDSVYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDII 196
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
58-207 |
6.39e-97 |
|
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: 294.00 E-value: 6.39e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 58 TIWFTGLSGAGKTTISFALERTLNKLGIPCYGLDGDNIRHGLCKNLGFSKEDRQENIRRVAEVAKLFADSGMICLAAFIS 137
Cdd:cd02027 1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 138 PFQEDRLDARKIHESENvkFIEVHVSTTLEVCEQRDPKQLYKKARAGQILGFTGIDSAYEPPENAEIILD 207
Cdd:cd02027 81 PYREDREAARKIIGGGD--FLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLD 148
|
|
| ATP-sulfurylase |
pfam01747 |
ATP-sulfurylase; This domain is the catalytic domain of ATP-sulfurylase or sulfate ... |
422-644 |
7.71e-93 |
|
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: 285.59 E-value: 7.71e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 422 DKYRKTPNELRAIFAEKNADAVFAFQLRNPIHNGHALLMRDTREKLLAEHknpiLLLHPLGGWTKDDDVPLDIRIKQHEA 501
Cdd:pfam01747 1 DEYRLTPAETRALFKEKGWRTVVAFQTRNPLHRAHEELMKRALEELEADG----LLLHPLVGPTKPGDVPAEVRVRCYEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 502 VIaERVLDPEWTVLSIFPSPMMYAGPTEVQWHARSRIAAGIQHYIVGRDPAGiqkPGSpdaLYETTHGAKVLSMAPGLSA 581
Cdd:pfam01747 77 LL-ENYLPPDRVVLALLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAG---VGD---FYGPYDAQEIFDEYPGELG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17542422 582 LHILPFRVAAYDKTAKKM-SFFDTSRKEDFENISGTKMRGLARNGDTPPEGFMAPTAWEVLAGY 644
Cdd:pfam01747 150 IEPVPFREAVYCKKCGEMaSTKCPHGGEDRLFISGTKVRELLREGEEPPEWFSRPEVAKVLREY 213
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
28-230 |
3.83e-86 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 282.20 E-value: 3.83e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 28 QSTNITYQEHTISREERAAAVGRhegfRGCTIWFTGLSGAGKTTISFALERTLNKLGIPCYGLDGDNIRHGLCKNLGFSK 107
Cdd:PRK05506 436 RATNVHWQASDVSREARAARKGQ----KPATVWFTGLSGSGKSTIANLVERRLHALGRHTYLLDGDNVRHGLNRDLGFSD 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 108 EDRQENIRRVAEVAKLFADSGMICLAAFISPFQEDRLDARKIHESEnvKFIEVHVSTTLEVCEQRDPKQLYKKARAGQIL 187
Cdd:PRK05506 512 ADRVENIRRVAEVARLMADAGLIVLVSFISPFREERELARALHGEG--EFVEVFVDTPLEVCEARDPKGLYAKARAGEIK 589
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17542422 188 GFTGIDSAYEPPENAEIILDAGKDGVQQCVQKVLDHLESKGLL 230
Cdd:PRK05506 590 NFTGIDSPYEAPENPELRLDTTGRSPEELAEQVLELLRRRGAI 632
|
|
| apsK |
TIGR00455 |
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ... |
39-224 |
6.03e-82 |
|
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: 256.63 E-value: 6.03e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 39 ISREERAAavgrHEGFRGCTIWFTGLSGAGKTTISFALERTLNKLGIPCYGLDGDNIRHGLCKNLGFSKEDRQENIRRVA 118
Cdd:TIGR00455 5 ITKDERQA----LNGHRGVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 119 EVAKLFADSGMICLAAFISPFQEDRLDARKIHESenVKFIEVHVSTTLEVCEQRDPKQLYKKARAGQILGFTGIDSAYEP 198
Cdd:TIGR00455 81 EVAKLFVRNGIIVITSFISPYRADRQMVRELIEK--GEFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYEA 158
|
170 180
....*....|....*....|....*.
gi 17542422 199 PENAEIILDAGKDGVQQCVQKVLDHL 224
Cdd:TIGR00455 159 PENPEVVLDTDQNDREECVGQIIEKL 184
|
|
| MET3 |
COG2046 |
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP ... |
242-648 |
2.14e-78 |
|
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: 254.30 E-value: 2.14e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 242 ELFVSDDlTVAELLKESQNLPTVELTKVDLQWLQVLAEGWATPLSGFMRERQYLQSMHFGQLLDlkhkvafvGEksddke 321
Cdd:COG2046 14 NRVVPGE-EREALLEEAKGLPSIELSSRALSDLEMIAIGGFSPLTGFMNKADYESVVENMRLAD--------GL------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 322 dSWPmmddinqsIPIVLPISDDVKKGLEGVTRIALK-YNGQVYAILSDPEIFEHRKdERVCRQ-FGTNDPRHPAVAQVLE 399
Cdd:COG2046 79 -LWP--------IPITLDVSEEDAAGLKEGDEVALRdEEGEPLAVLEVEEIYEYDK-EEEAEKvYGTTDPAHPGVAKLYE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 400 SGNWLLGGDVAVVQKIQFNDgLDKYRKTPNELRAIFAEKNADAVFAFQLRNPIHNGHALLMrdtreKLLAEHKNPiLLLH 479
Cdd:COG2046 149 RGDVYLGGPITLLNRPKHPD-FPDYRLTPAETRALFEEKGWKTVVAFQTRNPMHRAHEYLQ-----KRALETVDG-LLIH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 480 PLGGWTKDDDVPLDIRIKQHEAVIaERVLDPEWTVLSIFPSPMMYAGPTEVQWHARSRIAAGIQHYIVGRDPAGiqkPGS 559
Cdd:COG2046 222 PLVGETKPGDIPAEVRVRCYEALL-ENYYPKDRVLLSGLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAG---VGD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 560 pdaLYET--------THGAKVLSMAPglsalhiLPFRVAAYDKTAKKMSFFDT--SRKEDFENISGTKMRGLARNGDTPP 629
Cdd:COG2046 298 ---YYGPydaqeifdEFPPGELGIEP-------LKFEEAFYCKKCGGMATSKTcpHDKEDRVSLSGTKVREMLREGEEPP 367
|
410
....*....|....*....
gi 17542422 630 EGFMAPTAWEVLAGYYKSL 648
Cdd:COG2046 368 PEFSRPEVAEILRKYYQPF 386
|
|
| sat |
PRK04149 |
sulfate adenylyltransferase; Reviewed |
245-646 |
3.34e-71 |
|
sulfate adenylyltransferase; Reviewed
Pssm-ID: 235227 Cd Length: 391 Bit Score: 235.53 E-value: 3.34e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 245 VSDDLTVAELLKESQNLPTVELTKVDLQWLQVLAEGWATPLSGFMRERQYLQSMHFGQLLDlkhkvafvgeksddkedSW 324
Cdd:PRK04149 15 VVEGRDREEILEEAESLPRIELDERAASDLEMIAIGGFSPLTGFMGREDYDSVVEEMRLAN-----------------GL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 325 PMmddinqSIPIVLPISDDVKKGLEGVTRIALKYNGQVYAILSDPEIFEHRKdERVCRQ-FGTNDPRHPAVAQVLESGNW 403
Cdd:PRK04149 78 VW------SIPITLDVSEEDAASLKEGDEVALVYKGEPYGVLEVEEIYTYDK-KKEAEKvYKTTDEKHPGVKKLYEQGDV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 404 LLGGDVAVVQKIQfNDGLDKYRKTPNELRAIFAEKNADAVFAFQLRNPIHNGHALLMrdtreKLLAEHKNPiLLLHPLGG 483
Cdd:PRK04149 151 YLAGPVTLLNRKF-HEPFPRFWLTPAETRELFEEKGWKTVVAFQTRNPPHRAHEYLQ-----KCALEIVDG-LLLNPLVG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 484 WTKDDDVPLDIRIKQHEAVIaERVLDPEWTVLSIFPSPMMYAGPTEVQWHARSRIAAGIQHYIVGRDPAGIqkpGSPDAL 563
Cdd:PRK04149 224 ETKSGDIPAEVRMEAYEALL-KNYYPKDRVLLSVTPAAMRYAGPREAIFHAIVRKNYGCTHFIVGRDHAGV---GDYYGP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 564 YET----THGAKvlsmaPGLSaLHILPFRVAAYDKTAKKMSFFDT--SRKEDFENISGTKMRGLARNGDTPPEGFMAPTA 637
Cdd:PRK04149 300 YDAqeifDEFTE-----EELG-ITPLKFEEAFYCPKCGGMASEKTcpHGKEDRVHLSGTKVREMLREGEKPPPEFSRPEV 373
|
....*....
gi 17542422 638 WEVLAGYYK 646
Cdd:PRK04149 374 AEVLIKGLK 382
|
|
| PRK00889 |
PRK00889 |
adenylylsulfate kinase; Provisional |
55-231 |
3.29e-66 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179157 Cd Length: 175 Bit Score: 214.89 E-value: 3.29e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 55 RGCTIWFTGLSGAGKTTISFALERTLNKLGIPCYGLDGDNIRHGLCKNLGFSKEDRQENIRRVAEVAKLFADSGMICLAA 134
Cdd:PRK00889 3 RGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 135 FISPFQEDRLDARkiheSENVKFIEVHVSTTLEVCEQRDPKQLYKKARAGQILGFTGIDSAYEPPENAEIILDAGKDGVQ 214
Cdd:PRK00889 83 AISPYRETREEVR----ANIGNFLEVFVDAPLEVCEQRDVKGLYAKARAGEIKHFTGIDDPYEPPLNPEVECRTDLESLE 158
|
170
....*....|....*..
gi 17542422 215 QCVQKVLDHLESKGLLP 231
Cdd:PRK00889 159 ESVDKVLQKLEELGYLV 175
|
|
| PRK05537 |
PRK05537 |
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase; |
39-230 |
7.99e-58 |
|
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
Pssm-ID: 180124 [Multi-domain] Cd Length: 568 Bit Score: 204.52 E-value: 7.99e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 39 ISREERAAAVGRH-EGFrgcTIWFTGLSGAGKTTISFALERTLNKL-GIPCYGLDGDNIRHGLCKNLGFSKEDRQENIRR 116
Cdd:PRK05537 377 VVAELRRTYPPRHkQGF---TVFFTGLSGAGKSTIAKALMVKLMEMrGRPVTLLDGDVVRKHLSSELGFSKEDRDLNILR 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 117 VAEVAKLFADSGMICLAAFISPFQEDRLDARKIHESENvKFIEVHVSTTLEVCEQRDPKQLYKKARAGQILGFTGIDSAY 196
Cdd:PRK05537 454 IGFVASEITKNGGIAICAPIAPYRATRREVREMIEAYG-GFIEVHVATPLEVCEQRDRKGLYAKAREGKIKGFTGISDPY 532
|
170 180 190
....*....|....*....|....*....|....
gi 17542422 197 EPPENAEIILDAGKDGVQQCVQKVLDHLESKGLL 230
Cdd:PRK05537 533 EPPANPELVIDTTNVTPDECAHKILLYLEEKGYL 566
|
|
| PUA_2 |
pfam14306 |
PUA-like domain; This PUA like domain is found at the N-terminus of ATP-sulfurylase enzymes. |
240-414 |
4.11e-55 |
|
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: 184.65 E-value: 4.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 240 VRELFVSDDlTVAELLKESQNLPTVELTKVDLQWLQVLAEGWATPLSGFMRERQYLQSMHFGQLLDlkhkvafvgeksdd 319
Cdd:pfam14306 8 LVDLVVRDA-EREELLAEAAELPSIELSKRELCDLELIAIGGFSPLTGFMGEADYLSVLEFMRLAD-------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 320 kedSWPMmddinqSIPIVLPISDDVKKGLEGVTRIALKYN-GQVYAILSDPEIFEHRKDERVCRQFGTNDPRHPAVAQVL 398
Cdd:pfam14306 73 ---GLLW------SIPITLDVSEEDAASLKEGDRVALRDPeGEPLAILTVEEIYEPDKEEEAEKVFGTTDPAHPGVKKLY 143
|
170
....*....|....*.
gi 17542422 399 ESGNWLLGGDVAVVQK 414
Cdd:pfam14306 144 EQGDFYVGGDIEVLNR 159
|
|
| PRK05537 |
PRK05537 |
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase; |
242-642 |
1.51e-50 |
|
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
Pssm-ID: 180124 [Multi-domain] Cd Length: 568 Bit Score: 184.49 E-value: 1.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 242 ELFVSDDlTVAELLKESQNLPTVELTKVDLQWLQVLAEGWATPLSGFMRERQYLQSMHFGQLLDlkhkvafvGEksddke 321
Cdd:PRK05537 11 NLYVSPE-SREKLKAEALSLPSLDLSPRQICDLELLMNGGFSPLKGFMGRADYECVLENMRLAD--------GT------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 322 dSWPMmddinqsiPIVLPISDDVKKGLEGVTRIALK-YNGQVYAILSDPEIFEHRKDERVCRQFGTNDPRHPAVAQVLE- 399
Cdd:PRK05537 76 -LWPI--------PITLDVSEKFAAGLEIGERIALRdQEGVLLAILTVSDIWEPDKEREAEAVFGTTDPAHPGVNYLHRw 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 400 SGNWLLGGDVAVVQKIQFNDgLDKYRKTPNELRAIFAEKNADAVFAFQLRNPIHNGH-ALLMRDTREkllaehKNPILLL 478
Cdd:PRK05537 147 AGKFYLGGPLTGIQLPVHYD-FVQLRLTPAELRARFRKLGWRRVVAFQTRNPLHRAHeELTKRAARE------VGANLLI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 479 HPLGGWTKDDDVPLDIRIKQHEAVIAErvLDPEWTVLSIFPSPMMYAGPTEVQWHARSRIAAGIQHYIVGRDPAGIQK-- 556
Cdd:PRK05537 220 HPVVGMTKPGDIDHFTRVRCYEALLDK--YPPATTLLSLLPLAMRMAGPREALWHAIIRRNYGCTHFIVGRDHAGPGKds 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 557 -------PGSPDAL---YETTHGAKvlsmapglsalhILPFRVAAYDKTAKKMSFFDTSRK-EDFENISGTKMRGLARNG 625
Cdd:PRK05537 298 rgkpfygPYDAQELfakYADEIGIT------------MVPFKEMVYVQDKAQYVPVDEVPQgATVLTISGTELRRRLREG 365
|
410
....*....|....*..
gi 17542422 626 DTPPEGFMAPtawEVLA 642
Cdd:PRK05537 366 LEIPEWFSFP---EVVA 379
|
|
| PRK05541 |
PRK05541 |
adenylylsulfate kinase; Provisional |
56-228 |
1.05e-25 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 235498 Cd Length: 176 Bit Score: 103.98 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 56 GCTIWFTGLSGAGKTTISFALERTLNKLGIPCYGLDGDNIRHgLCKNLGFSKEDRQENIRRVAEVAKLFADSGMICLAAF 135
Cdd:PRK05541 7 GYVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELRE-ILGHYGYDKQSRIEMALKRAKLAKFLADQGMIVIVTT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 136 ISPFQEdrldARKIHESENVKFIEVHVSTTLEVCEQRDPKQLYKKARAGQILGFTGIDSAYEPPeNAEIILD-AGKDGVQ 214
Cdd:PRK05541 86 ISMFDE----IYAYNRKHLPNYFEVYLKCDMEELIRRDQKGLYTKALKGEIKNVVGVDIPFDEP-KADLVIDnSCRTSLD 160
|
170
....*....|....
gi 17542422 215 QCVQKVLDHLESKG 228
Cdd:PRK05541 161 EKVDLILNKLKLRL 174
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
59-172 |
5.43e-07 |
|
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: 49.23 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 59 IWFTGLSGAGKTTISFALERTLnklgiPCYGLDGDNIRHGLCKNLGFSKEDRQENIRRVAEVAKLFADSGM------ICL 132
Cdd:pfam13671 2 ILLVGLPGSGKSTLARRLLEEL-----GAVRLSSDDERKRLFGEGRPSISYYTDATDRTYERLHELARIALragrpvILD 76
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 17542422 133 AAFISPfqEDRLDARKIHESENVKFIEVHVSTTLEVCEQR 172
Cdd:pfam13671 77 ATNLRR--DERARLLALAREYGVPVRIVVFEAPEEVLRER 114
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
59-220 |
1.02e-06 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 49.14 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 59 IWFTGLSGAGKTTISFALERtlnKLGIPCygLDGDNIRHGLCKNLGFSKEDRQENIRRV----AEVAKLFADSGM--ICL 132
Cdd:COG0645 2 ILVCGLPGSGKSTLARALAE---RLGAVR--LRSDVVRKRLFGAGLAPLERSPEATARTyarlLALARELLAAGRsvILD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 133 AAFISPfqEDRLDARKIHESENVKFIEVHVSTTLEVCEQRdpkqLykKARAGQILG-------FTGIDSAYEPPENAE-- 203
Cdd:COG0645 77 ATFLRR--AQREAFRALAEEAGAPFVLIWLDAPEEVLRER----L--EARNAEGGDsdatwevLERQLAFEEPLTEDEgf 148
|
170
....*....|....*...
gi 17542422 204 -IILDAgkDGVQQCVQKV 220
Cdd:COG0645 149 lLVVDT--SGLEEALAAL 164
|
|
| GntK |
cd02021 |
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ... |
62-208 |
1.42e-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: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 62 TGLSGAGKTTISFALERtlnKLGIPcyGLDGDNIRHGLCK-----NLGFSKEDRQENIRRVAE-VAKLFADSGMICLAAF 135
Cdd:cd02021 5 MGVSGSGKSTVGKALAE---RLGAP--FIDGDDLHPPANIakmaaGIPLNDEDRWPWLQALTDaLLAKLASAGEGVVVAC 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17542422 136 ISPFQEDRLDARKIHESENVKFIevHVSTTLEVCEQRDpkqlykKARAGQILGFTGIDS---AYEPPENAE---IILDA 208
Cdd:cd02021 80 SALKRIYRDILRGGAANPRVRFV--HLDGPREVLAERL------AARKGHFMPADLLDSqfeTLEPPGEDEedvIVIDV 150
|
|
| CmkB |
COG1102 |
Cytidylate kinase [Nucleotide transport and metabolism]; |
58-228 |
9.45e-03 |
|
Cytidylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 440719 [Multi-domain] Cd Length: 188 Bit Score: 37.88 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 58 TIwfTGLSGAGKTTISFALERtlnKLGIPCYglDGDNIRHgLCKNLGFSKEDrqenIRRVAEVAKLFADSGMICLAAFIS 137
Cdd:COG1102 4 TI--SREPGSGGTTIAKRLAE---KLGLPLY--DGEILRE-AAKERGLSEEE----FEKLDEKAPSLLYRDTAEEDEIDR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542422 138 pFQEDRLdaRKIHESENVkFIE----------------VHVSTTLEVCEQR-------DPKQLYK------KARAGQILG 188
Cdd:COG1102 72 -ALDKVI--RELARKGNC-VIVgrladwilrdrpnvlkVFLTAPLEVRVKRiaeregiSEEEAEKeikkrdKSRAKYYKY 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17542422 189 FTGIDsaYEPPENAEIILDAGKDGVQQCVQKVLDHLESKG 228
Cdd:COG1102 148 YYGID--WGDPSNYDLVINTSRLGIEEAVDLILAAIEARE 185
|
|
| |
