|
Name |
Accession |
Description |
Interval |
E-value |
| ATPS |
cd00517 |
ATP-sulfurylase; ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, ... |
251-622 |
3.05e-176 |
|
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: 504.09 E-value: 3.05e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 251 LQAIEISTVELQWVQVLAEGWAYPLRGFMREDEYLQTLHFNTLQSGmdgsyrENHSVPIVLSATQADKDRLDGCSSLTLK 330
Cdd:cd00517 1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDG------TLWPIPIVLDVSEEDAKRLKEGERVALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 331 YQGKAVAILRRPEFYFQRKEERLARQFGTSNPNHPYSKQVYESGDYLVGGDLAVIERIRWEDgLDQYRLTPNELRRRFKE 410
Cdd:cd00517 75 YPGQPLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD-FDQYRLTPAELRALFKE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 411 LNADAIFAFQLRNPIHNGHALLMQDTRRQLLergfkQPVLLLHPLGGWTKDDDVPLDVRMKQHQAVLDAGVLrREDTVLA 490
Cdd:cd00517 154 RGWRRVVAFQTRNPMHRAHEELMKRAAEKLL-----NDGLLLHPLVGWTKPGDVPDEVRMRAYEALLEEYYL-PERTVLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 491 IFPSPMMYAGPTEVQWHAKARMNAGANFYIVGRDPAGMPHPaketYPDGNLYDATHGARVLKMAQGldsMEILPFRVAAY 570
Cdd:cd00517 228 ILPLPMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHP----GDYYGPYDAQEIFKKLAPELG---IEPVPFREAAY 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 24667028 571 DKSASRMAFFEPKR-KDEFEFISGTKMRTLAKTGASPPDGFMEPEAWRILATY 622
Cdd:cd00517 301 CPKCDGMASEDTCPhGEDFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
|
|
| sopT |
TIGR00339 |
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free ... |
242-620 |
5.91e-132 |
|
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: 392.13 E-value: 5.91e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 242 EALRHEAESLQAIEISTVELQWVQVLAEGWAYPLRGFMREDEYLQTLHFNTLQSGMdgsyreNHSVPIVLSATQADKDRL 321
Cdd:TIGR00339 18 HKLLAEAESLPSITLSDRQLCDLELLGNGAFSPLEGFMNEADYDSVVESMRLSDGV------LFSVPITLDIDDEDADDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 322 DGCSSLTLKYQ-GKAVAILRRPEFYFQRKEERLARQFGTSNPNHPYSKQVYESGDYLVGGDLAVIERIRWEDgLDQYRLT 400
Cdd:TIGR00339 92 KLGDRIALTDPkGQPLAILTIEEVYKPNKEKEAKKVFGTTDPEHPGVVYLNTAGNYYIGGPIEVINLPKFYD-FPRFRFT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 401 PNELRRRFKELNADAIFAFQLRNPIHNGHALLMQDTRRQLlergfKQPVLLLHPLGGWTKDDDVPLDVRMKQHQAVLDaG 480
Cdd:TIGR00339 171 PAELREEFKERGWDTVVAFQTRNPMHRAHEELTKRAAERL-----PNAGVLVHPLVGLTKPGDIPAEVRMRAYEVLKE-G 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 481 VLRREDTVLAIFPSPMMYAGPTEVQWHAKARMNAGANFYIVGRDPAGMPHPAKETypdgNLYDATHGARVLKMAQGLDSM 560
Cdd:TIGR00339 245 YPNPERTVVSFLPLAMRYAGPREAIWHAIIRKNYGATHFIVGRDHAGPGSNSKGQ----DFYGPYDAQELFEKYKAELGI 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24667028 561 EILPFRVAAYDKSASRMAFFE--PKRKDEFEFISGTKMRTLAKTGASPPDGFMEPEAWRILA 620
Cdd:TIGR00339 321 KIVPFRHVAYCPDEDEYAPADqaGHTNLRTLNISGTKLRGMLRNGVFPPEWFSRPEVVKILR 382
|
|
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
27-221 |
2.12e-102 |
|
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: 308.94 E-value: 2.12e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 27 HHVTRETRGKNlglcRGFRGCTVWLTGLSGAGKTSIAFELEAYLVSRGIPAYGLDGDNIRTGLNKNLGFTPADREENIRR 106
Cdd:COG0529 1 SAVTREERAAL----KGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 107 VGEVAKLFADSGVVAICSFVSPFADDREMARKIHKDAGlkFYEIFVDTPLDVCETRDVKGLYKKAREGVIKGFTGITQEY 186
Cdd:COG0529 77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEGE--FIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154
|
170 180 190
....*....|....*....|....*....|....*
gi 24667028 187 ERPQMPELVVNTHGYTVRESTQKLVTLLEQEGIIP 221
Cdd:COG0529 155 EAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
45-200 |
3.76e-98 |
|
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: 296.54 E-value: 3.76e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 45 RGCTVWLTGLSGAGKTSIAFELEAYLVSRGIPAYGLDGDNIRTGLNKNLGFTPADREENIRRVGEVAKLFADSGVVAICS 124
Cdd:pfam01583 1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24667028 125 FVSPFADDREMARKIHKDAglKFYEIFVDTPLDVCETRDVKGLYKKAREGVIKGFTGITQEYERPQMPELVVNTHG 200
Cdd:pfam01583 81 FISPYREDREQARELHEEG--KFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDTDK 154
|
|
| ATP-sulfurylase |
pfam01747 |
ATP-sulfurylase; This domain is the catalytic domain of ATP-sulfurylase or sulfate ... |
395-622 |
1.49e-95 |
|
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: 292.14 E-value: 1.49e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 395 DQYRLTPNELRRRFKELNADAIFAFQLRNPIHNGHALLMQDTRRQLLERGfkqpvLLLHPLGGWTKDDDVPLDVRMKQHQ 474
Cdd:pfam01747 1 DEYRLTPAETRALFKEKGWRTVVAFQTRNPLHRAHEELMKRALEELEADG-----LLLHPLVGPTKPGDVPAEVRVRCYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 475 AVLDAgVLRREDTVLAIFPSPMMYAGPTEVQWHAKARMNAGANFYIVGRDPAGMphpaketypdGNLYDATHGARVLKMA 554
Cdd:pfam01747 76 ALLEN-YLPPDRVVLALLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGV----------GDFYGPYDAQEIFDEY 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24667028 555 QGLDSMEILPFRVAAYDKSASRMAFFE-PKRKDEFEFISGTKMRTLAKTGASPPDGFMEPEAWRILATY 622
Cdd:pfam01747 145 PGELGIEPVPFREAVYCKKCGEMASTKcPHGGEDRLFISGTKVRELLREGEEPPEWFSRPEVAKVLREY 213
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
48-198 |
3.44e-92 |
|
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: 280.90 E-value: 3.44e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 48 TVWLTGLSGAGKTSIAFELEAYLVSRGIPAYGLDGDNIRTGLNKNLGFTPADREENIRRVGEVAKLFADSGVVAICSFVS 127
Cdd:cd02027 1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24667028 128 PFADDREMARKIHkdAGLKFYEIFVDTPLDVCETRDVKGLYKKAREGVIKGFTGITQEYERPQMPELVVNT 198
Cdd:cd02027 81 PYREDREAARKII--GGGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
16-220 |
1.11e-82 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 272.57 E-value: 1.11e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 16 LQVATNVTEQKHHVTRETRGKNlglcRGFRGCTVWLTGLSGAGKTSIAFELEAYLVSRGIPAYGLDGDNIRTGLNKNLGF 95
Cdd:PRK05506 434 LRRATNVHWQASDVSREARAAR----KGQKPATVWFTGLSGSGKSTIANLVERRLHALGRHTYLLDGDNVRHGLNRDLGF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 96 TPADREENIRRVGEVAKLFADSGVVAICSFVSPFADDREMARKIHKDAglKFYEIFVDTPLDVCETRDVKGLYKKAREGV 175
Cdd:PRK05506 510 SDADRVENIRRVAEVARLMADAGLIVLVSFISPFREERELARALHGEG--EFVEVFVDTPLEVCEARDPKGLYAKARAGE 587
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24667028 176 IKGFTGITQEYERPQMPELVVNTHGYTVRESTQKLVTLLEQEGII 220
Cdd:PRK05506 588 IKNFTGIDSPYEAPENPELRLDTTGRSPEELAEQVLELLRRRGAI 632
|
|
| apsK |
TIGR00455 |
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ... |
28-214 |
5.77e-77 |
|
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: 242.76 E-value: 5.77e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 28 HVTRETRGknlgLCRGFRGCTVWLTGLSGAGKTSIAFELEAYLVSRGIPAYGLDGDNIRTGLNKNLGFTPADREENIRRV 107
Cdd:TIGR00455 4 AITKDERQ----ALNGHRGVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 108 GEVAKLFADSGVVAICSFVSPFADDREMARKIHKDAglKFYEIFVDTPLDVCETRDVKGLYKKAREGVIKGFTGITQEYE 187
Cdd:TIGR00455 80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKG--EFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYE 157
|
170 180
....*....|....*....|....*..
gi 24667028 188 RPQMPELVVNTHGYTVRESTQKLVTLL 214
Cdd:TIGR00455 158 APENPEVVLDTDQNDREECVGQIIEKL 184
|
|
| MET3 |
COG2046 |
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP ... |
242-626 |
9.43e-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: 9.43e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 242 EALRHEAESLQAIEISTVELQWVQVLAEGwAY-PLRGFMREDEYLQTLHFNTLQSGMdgsyreNHSVPIVLSATQADKDR 320
Cdd:COG2046 23 EALLEEAKGLPSIELSSRALSDLEMIAIG-GFsPLTGFMNKADYESVVENMRLADGL------LWPIPITLDVSEEDAAG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 321 LDGCSSLTLK-YQGKAVAILRRPEFY-FQRKEErlARQ-FGTSNPNHPYSKQVYESGDYLVGGDLAVIERIRWEDgLDQY 397
Cdd:COG2046 96 LKEGDEVALRdEEGEPLAVLEVEEIYeYDKEEE--AEKvYGTTDPAHPGVAKLYERGDVYLGGPITLLNRPKHPD-FPDY 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 398 RLTPNELRRRFKELNADAIFAFQLRNPIHNGHALLMqdtrRQLLER--GfkqpvLLLHPLGGWTKDDDVPLDVRMKQHQA 475
Cdd:COG2046 173 RLTPAETRALFEEKGWKTVVAFQTRNPMHRAHEYLQ----KRALETvdG-----LLIHPLVGETKPGDIPAEVRVRCYEA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 476 VLDAGVlrREDTV-LAIFPSPMMYAGPTEVQWHAKARMNAGANFYIVGRDPAGM-----PHPAKE---TYPDGNLydath 546
Cdd:COG2046 244 LLENYY--PKDRVlLSGLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGVgdyygPYDAQEifdEFPPGEL----- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 547 garvlkmaqgldSMEILPFRVAAYDKSASRMAFFE--PKRKDEFEFISGTKMRTLAKTGASPPDGFMEPEAWRILATYYQ 624
Cdd:COG2046 317 ------------GIEPLKFEEAFYCKKCGGMATSKtcPHDKEDRVSLSGTKVREMLREGEEPPPEFSRPEVAEILRKYYQ 384
|
..
gi 24667028 625 NL 626
Cdd:COG2046 385 PF 386
|
|
| sat |
PRK04149 |
sulfate adenylyltransferase; Reviewed |
237-626 |
1.08e-64 |
|
sulfate adenylyltransferase; Reviewed
Pssm-ID: 235227 Cd Length: 391 Bit Score: 217.81 E-value: 1.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 237 ESIATEALRHEAESLQAIEISTVELQWVQVLAEGWAYPLRGFMREDEYLQTLHFNTLQSGMDGSYrenhsvPIVLSATQA 316
Cdd:PRK04149 17 EGRDREEILEEAESLPRIELDERAASDLEMIAIGGFSPLTGFMGREDYDSVVEEMRLANGLVWSI------PITLDVSEE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 317 DKDRLDGCSSLTLKYQGKAVAILRRPEFYFQRKEERLARQFGTSNPNHPYSKQVYESGDYLVGGDLAVIERIRWEDgLDQ 396
Cdd:PRK04149 91 DAASLKEGDEVALVYKGEPYGVLEVEEIYTYDKKKEAEKVYKTTDEKHPGVKKLYEQGDVYLAGPVTLLNRKFHEP-FPR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 397 YRLTPNELRRRFKELNADAIFAFQLRNPIHNGHALLMqdtrRQLLE--RGfkqpvLLLHPLGGWTKDDDVPLDVRMKQHQ 474
Cdd:PRK04149 170 FWLTPAETRELFEEKGWKTVVAFQTRNPPHRAHEYLQ----KCALEivDG-----LLLNPLVGETKSGDIPAEVRMEAYE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 475 AVLDAgVLRREDTVLAIFPSPMMYAGPTEVQWHAKARMNAGANFYIVGRDPAGMphpaketypdGNLYDaTHGARVLKMA 554
Cdd:PRK04149 241 ALLKN-YYPKDRVLLSVTPAAMRYAGPREAIFHAIVRKNYGCTHFIVGRDHAGV----------GDYYG-PYDAQEIFDE 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24667028 555 QGLDSMEILP--FRVAAYDKSASRMAFFE--PKRKDEFEFISGTKMRTLAKTGASPPDGFMEPEAWRILATYYQNL 626
Cdd:PRK04149 309 FTEEELGITPlkFEEAFYCPKCGGMASEKtcPHGKEDRVHLSGTKVREMLREGEKPPPEFSRPEVAEVLIKGLKKY 384
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ATPS |
cd00517 |
ATP-sulfurylase; ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, ... |
251-622 |
3.05e-176 |
|
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: 504.09 E-value: 3.05e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 251 LQAIEISTVELQWVQVLAEGWAYPLRGFMREDEYLQTLHFNTLQSGmdgsyrENHSVPIVLSATQADKDRLDGCSSLTLK 330
Cdd:cd00517 1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDG------TLWPIPIVLDVSEEDAKRLKEGERVALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 331 YQGKAVAILRRPEFYFQRKEERLARQFGTSNPNHPYSKQVYESGDYLVGGDLAVIERIRWEDgLDQYRLTPNELRRRFKE 410
Cdd:cd00517 75 YPGQPLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD-FDQYRLTPAELRALFKE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 411 LNADAIFAFQLRNPIHNGHALLMQDTRRQLLergfkQPVLLLHPLGGWTKDDDVPLDVRMKQHQAVLDAGVLrREDTVLA 490
Cdd:cd00517 154 RGWRRVVAFQTRNPMHRAHEELMKRAAEKLL-----NDGLLLHPLVGWTKPGDVPDEVRMRAYEALLEEYYL-PERTVLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 491 IFPSPMMYAGPTEVQWHAKARMNAGANFYIVGRDPAGMPHPaketYPDGNLYDATHGARVLKMAQGldsMEILPFRVAAY 570
Cdd:cd00517 228 ILPLPMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHP----GDYYGPYDAQEIFKKLAPELG---IEPVPFREAAY 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 24667028 571 DKSASRMAFFEPKR-KDEFEFISGTKMRTLAKTGASPPDGFMEPEAWRILATY 622
Cdd:cd00517 301 CPKCDGMASEDTCPhGEDFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
|
|
| sopT |
TIGR00339 |
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free ... |
242-620 |
5.91e-132 |
|
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: 392.13 E-value: 5.91e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 242 EALRHEAESLQAIEISTVELQWVQVLAEGWAYPLRGFMREDEYLQTLHFNTLQSGMdgsyreNHSVPIVLSATQADKDRL 321
Cdd:TIGR00339 18 HKLLAEAESLPSITLSDRQLCDLELLGNGAFSPLEGFMNEADYDSVVESMRLSDGV------LFSVPITLDIDDEDADDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 322 DGCSSLTLKYQ-GKAVAILRRPEFYFQRKEERLARQFGTSNPNHPYSKQVYESGDYLVGGDLAVIERIRWEDgLDQYRLT 400
Cdd:TIGR00339 92 KLGDRIALTDPkGQPLAILTIEEVYKPNKEKEAKKVFGTTDPEHPGVVYLNTAGNYYIGGPIEVINLPKFYD-FPRFRFT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 401 PNELRRRFKELNADAIFAFQLRNPIHNGHALLMQDTRRQLlergfKQPVLLLHPLGGWTKDDDVPLDVRMKQHQAVLDaG 480
Cdd:TIGR00339 171 PAELREEFKERGWDTVVAFQTRNPMHRAHEELTKRAAERL-----PNAGVLVHPLVGLTKPGDIPAEVRMRAYEVLKE-G 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 481 VLRREDTVLAIFPSPMMYAGPTEVQWHAKARMNAGANFYIVGRDPAGMPHPAKETypdgNLYDATHGARVLKMAQGLDSM 560
Cdd:TIGR00339 245 YPNPERTVVSFLPLAMRYAGPREAIWHAIIRKNYGATHFIVGRDHAGPGSNSKGQ----DFYGPYDAQELFEKYKAELGI 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24667028 561 EILPFRVAAYDKSASRMAFFE--PKRKDEFEFISGTKMRTLAKTGASPPDGFMEPEAWRILA 620
Cdd:TIGR00339 321 KIVPFRHVAYCPDEDEYAPADqaGHTNLRTLNISGTKLRGMLRNGVFPPEWFSRPEVVKILR 382
|
|
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
27-221 |
2.12e-102 |
|
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: 308.94 E-value: 2.12e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 27 HHVTRETRGKNlglcRGFRGCTVWLTGLSGAGKTSIAFELEAYLVSRGIPAYGLDGDNIRTGLNKNLGFTPADREENIRR 106
Cdd:COG0529 1 SAVTREERAAL----KGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 107 VGEVAKLFADSGVVAICSFVSPFADDREMARKIHKDAGlkFYEIFVDTPLDVCETRDVKGLYKKAREGVIKGFTGITQEY 186
Cdd:COG0529 77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEGE--FIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154
|
170 180 190
....*....|....*....|....*....|....*
gi 24667028 187 ERPQMPELVVNTHGYTVRESTQKLVTLLEQEGIIP 221
Cdd:COG0529 155 EAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
45-200 |
3.76e-98 |
|
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: 296.54 E-value: 3.76e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 45 RGCTVWLTGLSGAGKTSIAFELEAYLVSRGIPAYGLDGDNIRTGLNKNLGFTPADREENIRRVGEVAKLFADSGVVAICS 124
Cdd:pfam01583 1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24667028 125 FVSPFADDREMARKIHKDAglKFYEIFVDTPLDVCETRDVKGLYKKAREGVIKGFTGITQEYERPQMPELVVNTHG 200
Cdd:pfam01583 81 FISPYREDREQARELHEEG--KFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDTDK 154
|
|
| ATP-sulfurylase |
pfam01747 |
ATP-sulfurylase; This domain is the catalytic domain of ATP-sulfurylase or sulfate ... |
395-622 |
1.49e-95 |
|
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: 292.14 E-value: 1.49e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 395 DQYRLTPNELRRRFKELNADAIFAFQLRNPIHNGHALLMQDTRRQLLERGfkqpvLLLHPLGGWTKDDDVPLDVRMKQHQ 474
Cdd:pfam01747 1 DEYRLTPAETRALFKEKGWRTVVAFQTRNPLHRAHEELMKRALEELEADG-----LLLHPLVGPTKPGDVPAEVRVRCYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 475 AVLDAgVLRREDTVLAIFPSPMMYAGPTEVQWHAKARMNAGANFYIVGRDPAGMphpaketypdGNLYDATHGARVLKMA 554
Cdd:pfam01747 76 ALLEN-YLPPDRVVLALLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGV----------GDFYGPYDAQEIFDEY 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24667028 555 QGLDSMEILPFRVAAYDKSASRMAFFE-PKRKDEFEFISGTKMRTLAKTGASPPDGFMEPEAWRILATY 622
Cdd:pfam01747 145 PGELGIEPVPFREAVYCKKCGEMASTKcPHGGEDRLFISGTKVRELLREGEEPPEWFSRPEVAKVLREY 213
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
48-198 |
3.44e-92 |
|
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: 280.90 E-value: 3.44e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 48 TVWLTGLSGAGKTSIAFELEAYLVSRGIPAYGLDGDNIRTGLNKNLGFTPADREENIRRVGEVAKLFADSGVVAICSFVS 127
Cdd:cd02027 1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24667028 128 PFADDREMARKIHkdAGLKFYEIFVDTPLDVCETRDVKGLYKKAREGVIKGFTGITQEYERPQMPELVVNT 198
Cdd:cd02027 81 PYREDREAARKII--GGGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
16-220 |
1.11e-82 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 272.57 E-value: 1.11e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 16 LQVATNVTEQKHHVTRETRGKNlglcRGFRGCTVWLTGLSGAGKTSIAFELEAYLVSRGIPAYGLDGDNIRTGLNKNLGF 95
Cdd:PRK05506 434 LRRATNVHWQASDVSREARAAR----KGQKPATVWFTGLSGSGKSTIANLVERRLHALGRHTYLLDGDNVRHGLNRDLGF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 96 TPADREENIRRVGEVAKLFADSGVVAICSFVSPFADDREMARKIHKDAglKFYEIFVDTPLDVCETRDVKGLYKKAREGV 175
Cdd:PRK05506 510 SDADRVENIRRVAEVARLMADAGLIVLVSFISPFREERELARALHGEG--EFVEVFVDTPLEVCEARDPKGLYAKARAGE 587
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24667028 176 IKGFTGITQEYERPQMPELVVNTHGYTVRESTQKLVTLLEQEGII 220
Cdd:PRK05506 588 IKNFTGIDSPYEAPENPELRLDTTGRSPEELAEQVLELLRRRGAI 632
|
|
| PRK03846 |
PRK03846 |
adenylylsulfate kinase; Provisional |
20-222 |
1.43e-81 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179661 Cd Length: 198 Bit Score: 255.25 E-value: 1.43e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 20 TNVTEQKHHVTRETRGKNlglcRGFRGCTVWLTGLSGAGKTSIAFELEAYLVSRGIPAYGLDGDNIRTGLNKNLGFTPAD 99
Cdd:PRK03846 2 ENIVWHQHPVTKAQREQL----HGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 100 REENIRRVGEVAKLFADSGVVAICSFVSPFADDREMARKIHKDAglKFYEIFVDTPLDVCETRDVKGLYKKAREGVIKGF 179
Cdd:PRK03846 78 RKENIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEG--EFIEVFVDTPLAICEARDPKGLYKKARAGEIRNF 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24667028 180 TGITQEYERPQMPELVVNTHGYTVRESTQKLVTLLEQEGIIPR 222
Cdd:PRK03846 156 TGIDSVYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDIIRS 198
|
|
| apsK |
TIGR00455 |
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ... |
28-214 |
5.77e-77 |
|
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: 242.76 E-value: 5.77e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 28 HVTRETRGknlgLCRGFRGCTVWLTGLSGAGKTSIAFELEAYLVSRGIPAYGLDGDNIRTGLNKNLGFTPADREENIRRV 107
Cdd:TIGR00455 4 AITKDERQ----ALNGHRGVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 108 GEVAKLFADSGVVAICSFVSPFADDREMARKIHKDAglKFYEIFVDTPLDVCETRDVKGLYKKAREGVIKGFTGITQEYE 187
Cdd:TIGR00455 80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKG--EFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYE 157
|
170 180
....*....|....*....|....*..
gi 24667028 188 RPQMPELVVNTHGYTVRESTQKLVTLL 214
Cdd:TIGR00455 158 APENPEVVLDTDQNDREECVGQIIEKL 184
|
|
| MET3 |
COG2046 |
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP ... |
242-626 |
9.43e-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: 9.43e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 242 EALRHEAESLQAIEISTVELQWVQVLAEGwAY-PLRGFMREDEYLQTLHFNTLQSGMdgsyreNHSVPIVLSATQADKDR 320
Cdd:COG2046 23 EALLEEAKGLPSIELSSRALSDLEMIAIG-GFsPLTGFMNKADYESVVENMRLADGL------LWPIPITLDVSEEDAAG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 321 LDGCSSLTLK-YQGKAVAILRRPEFY-FQRKEErlARQ-FGTSNPNHPYSKQVYESGDYLVGGDLAVIERIRWEDgLDQY 397
Cdd:COG2046 96 LKEGDEVALRdEEGEPLAVLEVEEIYeYDKEEE--AEKvYGTTDPAHPGVAKLYERGDVYLGGPITLLNRPKHPD-FPDY 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 398 RLTPNELRRRFKELNADAIFAFQLRNPIHNGHALLMqdtrRQLLER--GfkqpvLLLHPLGGWTKDDDVPLDVRMKQHQA 475
Cdd:COG2046 173 RLTPAETRALFEEKGWKTVVAFQTRNPMHRAHEYLQ----KRALETvdG-----LLIHPLVGETKPGDIPAEVRVRCYEA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 476 VLDAGVlrREDTV-LAIFPSPMMYAGPTEVQWHAKARMNAGANFYIVGRDPAGM-----PHPAKE---TYPDGNLydath 546
Cdd:COG2046 244 LLENYY--PKDRVlLSGLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGVgdyygPYDAQEifdEFPPGEL----- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 547 garvlkmaqgldSMEILPFRVAAYDKSASRMAFFE--PKRKDEFEFISGTKMRTLAKTGASPPDGFMEPEAWRILATYYQ 624
Cdd:COG2046 317 ------------GIEPLKFEEAFYCKKCGGMATSKtcPHDKEDRVSLSGTKVREMLREGEEPPPEFSRPEVAEILRKYYQ 384
|
..
gi 24667028 625 NL 626
Cdd:COG2046 385 PF 386
|
|
| PRK00889 |
PRK00889 |
adenylylsulfate kinase; Provisional |
45-221 |
5.69e-65 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179157 Cd Length: 175 Bit Score: 211.03 E-value: 5.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 45 RGCTVWLTGLSGAGKTSIAFELEAYLVSRGIPAYGLDGDNIRTGLNKNLGFTPADREENIRRVGEVAKLFADSGVVAICS 124
Cdd:PRK00889 3 RGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 125 FVSPFADDREMARkiHKDAglKFYEIFVDTPLDVCETRDVKGLYKKAREGVIKGFTGITQEYERPQMPELVVNTHGYTVR 204
Cdd:PRK00889 83 AISPYRETREEVR--ANIG--NFLEVFVDAPLEVCEQRDVKGLYAKARAGEIKHFTGIDDPYEPPLNPEVECRTDLESLE 158
|
170
....*....|....*..
gi 24667028 205 ESTQKLVTLLEQEGIIP 221
Cdd:PRK00889 159 ESVDKVLQKLEELGYLV 175
|
|
| sat |
PRK04149 |
sulfate adenylyltransferase; Reviewed |
237-626 |
1.08e-64 |
|
sulfate adenylyltransferase; Reviewed
Pssm-ID: 235227 Cd Length: 391 Bit Score: 217.81 E-value: 1.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 237 ESIATEALRHEAESLQAIEISTVELQWVQVLAEGWAYPLRGFMREDEYLQTLHFNTLQSGMDGSYrenhsvPIVLSATQA 316
Cdd:PRK04149 17 EGRDREEILEEAESLPRIELDERAASDLEMIAIGGFSPLTGFMGREDYDSVVEEMRLANGLVWSI------PITLDVSEE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 317 DKDRLDGCSSLTLKYQGKAVAILRRPEFYFQRKEERLARQFGTSNPNHPYSKQVYESGDYLVGGDLAVIERIRWEDgLDQ 396
Cdd:PRK04149 91 DAASLKEGDEVALVYKGEPYGVLEVEEIYTYDKKKEAEKVYKTTDEKHPGVKKLYEQGDVYLAGPVTLLNRKFHEP-FPR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 397 YRLTPNELRRRFKELNADAIFAFQLRNPIHNGHALLMqdtrRQLLE--RGfkqpvLLLHPLGGWTKDDDVPLDVRMKQHQ 474
Cdd:PRK04149 170 FWLTPAETRELFEEKGWKTVVAFQTRNPPHRAHEYLQ----KCALEivDG-----LLLNPLVGETKSGDIPAEVRMEAYE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 475 AVLDAgVLRREDTVLAIFPSPMMYAGPTEVQWHAKARMNAGANFYIVGRDPAGMphpaketypdGNLYDaTHGARVLKMA 554
Cdd:PRK04149 241 ALLKN-YYPKDRVLLSVTPAAMRYAGPREAIFHAIVRKNYGCTHFIVGRDHAGV----------GDYYG-PYDAQEIFDE 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24667028 555 QGLDSMEILP--FRVAAYDKSASRMAFFE--PKRKDEFEFISGTKMRTLAKTGASPPDGFMEPEAWRILATYYQNL 626
Cdd:PRK04149 309 FTEEELGITPlkFEEAFYCPKCGGMASEKtcPHGKEDRVHLSGTKVREMLREGEKPPPEFSRPEVAEVLIKGLKKY 384
|
|
| PRK05537 |
PRK05537 |
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase; |
42-220 |
1.63e-58 |
|
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
Pssm-ID: 180124 [Multi-domain] Cd Length: 568 Bit Score: 206.06 E-value: 1.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 42 RGFRGCTVWLTGLSGAGKTSIAFELEAYLVS-RGIPAYGLDGDNIRTGLNKNLGFTPADREENIRRVGEVAKLFADSGVV 120
Cdd:PRK05537 388 RHKQGFTVFFTGLSGAGKSTIAKALMVKLMEmRGRPVTLLDGDVVRKHLSSELGFSKEDRDLNILRIGFVASEITKNGGI 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 121 AICSFVSPFADDREMARKIHKDAGlKFYEIFVDTPLDVCETRDVKGLYKKAREGVIKGFTGITQEYERPQMPELVVNTHG 200
Cdd:PRK05537 468 AICAPIAPYRATRREVREMIEAYG-GFIEVHVATPLEVCEQRDRKGLYAKAREGKIKGFTGISDPYEPPANPELVIDTTN 546
|
170 180
....*....|....*....|
gi 24667028 201 YTVRESTQKLVTLLEQEGII 220
Cdd:PRK05537 547 VTPDECAHKILLYLEEKGYL 566
|
|
| PUA_2 |
pfam14306 |
PUA-like domain; This PUA like domain is found at the N-terminus of ATP-sulfurylase enzymes. |
230-387 |
6.78e-56 |
|
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: 186.57 E-value: 6.78e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 230 LPELYPSESiATEALRHEAESLQAIEISTVELQWVQVLAEGWAYPLRGFMREDEYLQTLHFNTLQsgmDGSYrenHSVPI 309
Cdd:pfam14306 8 LVDLVVRDA-EREELLAEAAELPSIELSKRELCDLELIAIGGFSPLTGFMGEADYLSVLEFMRLA---DGLL---WSIPI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24667028 310 VLSATQADKDRLDGCSSLTLKYQ-GKAVAILRRPEFYFQRKEERLARQFGTSNPNHPYSKQVYESGDYLVGGDLAVIER 387
Cdd:pfam14306 81 TLDVSEEDAASLKEGDRVALRDPeGEPLAILTVEEIYEPDKEEEAEKVFGTTDPAHPGVKKLYEQGDFYVGGDIEVLNR 159
|
|
| PRK05537 |
PRK05537 |
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase; |
230-623 |
2.05e-49 |
|
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
Pssm-ID: 180124 [Multi-domain] Cd Length: 568 Bit Score: 181.02 E-value: 2.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 230 LPELYPSESIAtEALRHEAESLQAIEISTVELQWVQVLAEGWAYPLRGFMREDEYLQTLHFNTLQsgmDGSYrenHSVPI 309
Cdd:PRK05537 9 LPNLYVSPESR-EKLKAEALSLPSLDLSPRQICDLELLMNGGFSPLKGFMGRADYECVLENMRLA---DGTL---WPIPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 310 VLSATQADKDRLDGCSSLTLKYQ-GKAVAILRRPEFYFQRKEERLARQFGTSNPNHPYSKQVYE-SGDYLVGGDLAVIER 387
Cdd:PRK05537 82 TLDVSEKFAAGLEIGERIALRDQeGVLLAILTVSDIWEPDKEREAEAVFGTTDPAHPGVNYLHRwAGKFYLGGPLTGIQL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 388 IRWEDgLDQYRLTPNELRRRFKELNADAIFAFQLRNPIHNGHALLMQDTRRQLlergfkQPVLLLHPLGGWTKDDDVPLD 467
Cdd:PRK05537 162 PVHYD-FVQLRLTPAELRARFRKLGWRRVVAFQTRNPLHRAHEELTKRAAREV------GANLLIHPVVGMTKPGDIDHF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 468 VRMKQHQAVLDAgvLRREDTVLAIFPSPMMYAGPTEVQWHAKARMNAGANFYIVGRDPAGmPHPAKETYPDGNLYDATHg 547
Cdd:PRK05537 235 TRVRCYEALLDK--YPPATTLLSLLPLAMRMAGPREALWHAIIRRNYGCTHFIVGRDHAG-PGKDSRGKPFYGPYDAQE- 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24667028 548 arVLKMAQGLDSMEILPFRVAAYDKSASRMAFF-EPKRKDEFEFISGTKMRTLAKTGASPPDGFMEPEAWRILATYY 623
Cdd:PRK05537 311 --LFAKYADEIGITMVPFKEMVYVQDKAQYVPVdEVPQGATVLTISGTELRRRLREGLEIPEWFSFPEVVAELRRTY 385
|
|
| PRK05541 |
PRK05541 |
adenylylsulfate kinase; Provisional |
46-219 |
6.82e-21 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 235498 Cd Length: 176 Bit Score: 90.11 E-value: 6.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 46 GCTVWLTGLSGAGKTSIAFELEAYLVSRGIPAYGLDGDNIRtglnKNLGFTPADREENI---RRVGEVAKLFADSGVVAI 122
Cdd:PRK05541 7 GYVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELR----EILGHYGYDKQSRIemaLKRAKLAKFLADQGMIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 123 CSFVSPFADDREMARKIHKdaglKFYEIFVDTPLDVCETRDVKGLYKKAREGVIKGFTGITQEYERPQmPELVVNTHGYT 202
Cdd:PRK05541 83 VTTISMFDEIYAYNRKHLP----NYFEVYLKCDMEELIRRDQKGLYTKALKGEIKNVVGVDIPFDEPK-ADLVIDNSCRT 157
|
170
....*....|....*...
gi 24667028 203 VREST-QKLVTLLEQEGI 219
Cdd:PRK05541 158 SLDEKvDLILNKLKLRLI 175
|
|
| Kti12 |
COG4088 |
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ... |
51-219 |
1.65e-10 |
|
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: 60.51 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 51 LTGLSGAGKTSIAFELEAYLVSRGIPAYGLDGDNIRTGLNKNLGFTPAdREENIRRVGE-VAKLFADSGVVAIcsfvspf 129
Cdd:COG4088 9 LTGPPGSGKTTFAKALAQRLYAEGIAVALLHSDDFRRFLVNESFPKET-YEEVVEDVRTtTADNALDNGYSVI------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 130 ADD----REMARKIHKDAGLK--FYEIFVDTPLDVCETRDVKGLYKKAREGVIKGFtgitQEYERP---QMPELVVNTHG 200
Cdd:COG4088 81 VDGtfyyRSWQRDFRNLAKHKapIHIIYLKAPLETALRRNRERGEPIPERVIARMY----RKFDKPgtkDRPDLVIDTTE 156
|
170
....*....|....*....
gi 24667028 201 YTVRESTQKLVTLLEQEGI 219
Cdd:COG4088 157 DSVSETLDAILKAIETWGI 175
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
49-162 |
1.16e-07 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 51.84 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 49 VWLTGLSGAGKTSIAFELEAYLvsrgiPAYGLDGDNIRTGLNKNLGFTPADREENIRRV----GEVAKLFADSGVVAICS 124
Cdd:COG0645 2 ILVCGLPGSGKSTLARALAERL-----GAVRLRSDVVRKRLFGAGLAPLERSPEATARTyarlLALARELLAAGRSVILD 76
|
90 100 110
....*....|....*....|....*....|....*...
gi 24667028 125 FVSPFADDREMARKIHKDAGLKFYEIFVDTPLDVCETR 162
Cdd:COG0645 77 ATFLRRAQREAFRALAEEAGAPFVLIWLDAPEEVLRER 114
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
49-165 |
2.40e-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: 47.30 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 49 VWLTGLSGAGKTSIAFELEAYLvsrgiPAYGLDGDNIRTGLNKNLGFTPADREENI----RRVGEVAKLFADSGVVAIcs 124
Cdd:pfam13671 2 ILLVGLPGSGKSTLARRLLEEL-----GAVRLSSDDERKRLFGEGRPSISYYTDATdrtyERLHELARIALRAGRPVI-- 74
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 24667028 125 FVSPFADDREMARKIH--KDAGLKFYEIFVDTPLDVCETRDVK 165
Cdd:pfam13671 75 LDATNLRRDERARLLAlaREYGVPVRIVVFEAPEEVLRERLAA 117
|
|
| GntK |
cd02021 |
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ... |
51-174 |
1.11e-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: 39.93 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667028 51 LTGLSGAGKTSIAFELEAYLVSRGIpayglDGDNIRTGLNK-----NLGFTPADRE---ENIRRVGEVAKLFADSGVVAI 122
Cdd:cd02021 4 VMGVSGSGKSTVGKALAERLGAPFI-----DGDDLHPPANIakmaaGIPLNDEDRWpwlQALTDALLAKLASAGEGVVVA 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 24667028 123 CSF--VSPfaddREMARKIHKDAGLKFyeIFVDTPLDVCETRDvkglykKAREG 174
Cdd:cd02021 79 CSAlkRIY----RDILRGGAANPRVRF--VHLDGPREVLAERL------AARKG 120
|
|
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