|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
1-419 |
0e+00 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 620.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 1 MKVLVIGPGGREHAIVRSLLEDPNVSEVHAAPGNAGISKLVPTHAIDGNNPEAVSALATKLGVDLVVVGPEAPLAAGVSD 80
Cdd:COG0151 1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 81 AVRAAGIPVFGPSKEAAQLEASKAFAKQIMAEAGVPTAMARVATNAEEAADALATFGAPHVVKDDGLAAGKGVVVTNDRE 160
Cdd:COG0151 81 AFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAETLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 161 EALAHAQACF------DAGGTVVIEEFLDGPEVSLFVLCDGRTTVPLSPAQDFKRIYDNDEGPNTGGMGAYTPLEWAPEG 234
Cdd:COG0151 161 EALAAVDDMLadgkfgDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVTEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 235 LVQEVIDRVAQPTVDEMARRGTPFIGVLYCGLALTSRGTRVIEFNVRFGDPETQAVLARLKTPLGALLLAAAKGELDTAe 314
Cdd:COG0151 241 LLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLDEV- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 315 ELRWSKDTAVAVVVAAENYPDTPRTGDRIRGLKKVDElEGVHVVHAGTKLdEEGKVVSAGGRVLAVVALGSDLVEAREKA 394
Cdd:COG0151 320 ELEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAEA-EGVKVFHAGTAL-EDGKLVTNGGRVLGVTALGDTLEEARERA 397
|
410 420
....*....|....*....|....*
gi 2059122299 395 YDGVELVQLEGSQFRTDIGGKAARG 419
Cdd:COG0151 398 YEAVEKIRFEGMFYRRDIGWRALKR 422
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
1-417 |
1.49e-172 |
|
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase (GARS). This enzyme appears as a monofunctional protein in prokaryotes but as part of a larger, multidomain protein in eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273315 [Multi-domain] Cd Length: 422 Bit Score: 489.90 E-value: 1.49e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 1 MKVLVIGPGGREHAIVRSLLEDPNVSEVHAAPGNAGISKLVPTH--AIDGNNPEAVSALATKLGVDLVVVGPEAPLAAGV 78
Cdd:TIGR00877 1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKnvAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 79 SDAVRAAGIPVFGPSKEAAQLEASKAFAKQIMAEAGVPTAMARVATNAEEAADALATFGAPHVVKDDGLAAGKGVVVTND 158
Cdd:TIGR00877 81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 159 REEALAHAQACF-----DAGGTVVIEEFLDGPEVSLFVLCDGRTTVPLSPAQDFKRIYDNDEGPNTGGMGAYTPLEWAPE 233
Cdd:TIGR00877 161 NEEAIKAVEDILeqkfgDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFTE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 234 GLVQEVIDRVAQPTVDEMARRGTPFIGVLYCGLALTSRGTRVIEFNVRFGDPETQAVLARLKTPLGALLLAAAKGELDTA 313
Cdd:TIGR00877 241 EVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLDEV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 314 eELRWSKDTAVAVVVAAENYPDTPRTGDRIRGLKKVdELEGVHVVHAGTKLDeEGKVVSAGGRVLAVVALGSDLVEAREK 393
Cdd:TIGR00877 321 -ELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLA-EAEGVKVFHAGTKAD-NGKLVTNGGRVLAVTALGKTLEEARER 397
|
410 420
....*....|....*....|....
gi 2059122299 394 AYDGVELVQLEGSQFRTDIGGKAA 417
Cdd:TIGR00877 398 AYEAVEYIKFEGMFYRKDIGFRAL 421
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
4-416 |
5.39e-135 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 394.88 E-value: 5.39e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 4 LVIGPGGREHAIVRSLLEDPNVSEVHAAPGNAGISK---LVPTHAIDGNNPEAVSALATKLGVDLVVVGPEAPLAAGVSD 80
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATsgdATCVPDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 81 AVRAAGIPVFGPSKEAAQLEASKAFAKQIMAEAGVPTAMARVATNAEEAADALATFGAPHVVKDDGLAAGKGVVVTNDRE 160
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 161 EALAH-----AQACF-DAGGTVVIEEFLDGPEVSLFVLCDGRTTVPLSPAQDFKRIYDNDEGPNTGGMGAYTPLEWAPEG 234
Cdd:PLN02257 161 EAYEAvdsmlVKGAFgSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 235 LVQEVIDRVAQPTVDEMARRGTPFIGVLYCGLALTSRG--TRVIEFNVRFGDPETQAVLARLKTPLGALLLAAAKGELDT 312
Cdd:PLN02257 241 LESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELSG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 313 AeELRWSKDTAVAVVVAAENYPDTPRTGDRIRGLKKVDELE-GVHVVHAGTKLDEEGKVVSAGGRVLAVVALGSDLVEAR 391
Cdd:PLN02257 321 V-SLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLDEAEAVApGVKVFHAGTALDSDGNVVAAGGRVLGVTAKGKDIAEAR 399
|
410 420
....*....|....*....|....*
gi 2059122299 392 EKAYDGVELVQLEGSQFRTDIGGKA 416
Cdd:PLN02257 400 ARAYDAVDQIDWPGGFFRRDIGWRA 424
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
101-287 |
3.66e-83 |
|
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).
Pssm-ID: 395851 [Multi-domain] Cd Length: 194 Bit Score: 253.74 E-value: 3.66e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 101 ASKAFAKQIMAEAGVPTAMARVATNAEEAADALATFGAP-HVVKDDGLAAGKGVVVTNDREEALAHAQACF------DAG 173
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPaIVVKADGLAAGKGVIVASSNEEAIKAVDEILeqkkfgEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 174 GTVVIEEFLDGPEVSLFVLCDGRTTVPLSPAQDFKRIYDNDEGPNTGGMGAYTPLEWAPEGLVQEVIDRVAQPTVDEMAR 253
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 2059122299 254 RGTPFIGVLYCGLALTSRGTRVIEFNVRFGDPET 287
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
1-100 |
1.10e-46 |
|
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the N-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam00289). This domain is structurally related to the PreATP-grasp domain.
Pssm-ID: 460723 [Multi-domain] Cd Length: 102 Bit Score: 155.98 E-value: 1.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 1 MKVLVIGPGGREHAIVRSLLEDPNVSEVHAAPGNAGISKLVPTHAIDGNNPEAVSALATKLGVDLVVVGPEAPLAAGVSD 80
Cdd:pfam02844 1 MKVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLAECVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGIVD 80
|
90 100
....*....|....*....|..
gi 2059122299 81 AV--RAAGIPVFGPSKEAAQLE 100
Cdd:pfam02844 81 ALreRAAGIPVFGPSKAAAQLE 102
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
331-413 |
2.23e-29 |
|
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the C-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02787).
Pssm-ID: 460722 [Multi-domain] Cd Length: 88 Bit Score: 109.84 E-value: 2.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 331 ENYPDTPRTGDRIRGLkkvdELEGVHVVHAGTKLDEeGKVVSAGGRVLAVVALGSDLVEAREKAYDGVELVQLEGSQFRT 410
Cdd:pfam02843 9 GGYPGSYEKGDVITGL----DEAGVKVFHAGTKLKD-GKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDFEGMFYRK 83
|
...
gi 2059122299 411 DIG 413
Cdd:pfam02843 84 DIG 86
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
52-202 |
5.59e-19 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 86.08 E-value: 5.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 52 EAVSALATKLGVDLVVVGPEAPLAAgVSDAVRAAGIPvfGPSKEAAQLEASKAFAKQIMAEAGVPTAMARVATNAEEAAD 131
Cdd:COG0439 7 AAAAELARETGIDAVLSESEFAVET-AAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALA 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2059122299 132 ALATFGAPHVVKDDGLAAGKGVVVTNDREEALAHAQAC------FDAGGTVVIEEFLDGPEVSLFVLCDGRTTVPLS 202
Cdd:COG0439 84 FAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEAraeakaGSPNGEVLVEEFLEGREYSVEGLVRDGEVVVCS 160
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
62-291 |
1.12e-12 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 68.04 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 62 GVDLVVVGPEAPLAA-GVSDAVRAAGIPVFGPSkEAAQLEASKAFAKQIMAEAGVPTAMARVATNAEEAADALATFGAPH 140
Cdd:COG0189 56 EFDAVLPRIDPPFYGlALLRQLEAAGVPVVNDP-EAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 141 VVKDDGLAAGKGVVVTNDREEALAHAQACFDAG-GTVVIEEFL---DGPEVSLFVLcDGR--TTVPLSPAQDFKRIYDND 214
Cdd:COG0189 135 VLKPLDGSGGRGVFLVEDEDALESILEALTELGsEPVLVQEFIpeeDGRDIRVLVV-GGEpvAAIRRIPAEGEFRTNLAR 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2059122299 215 egpntGGMGAYTPLEwapeglvqevidrvaqPTVDEMARRGTPFIGVLYCG--LALTSRGTRVIEFNVRFGDPETQAVL 291
Cdd:COG0189 214 -----GGRAEPVELT----------------DEERELALRAAPALGLDFAGvdLIEDDDGPLVLEVNVTPGFRGLERAT 271
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
85-203 |
1.93e-11 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 64.74 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 85 AGIPVFGPSKEAAQLEASKAFAKQIMAEAGVPTAMARVATNAE--EAADALATFGAPHVVKDDGLAAGKGVVVTNDREEA 162
Cdd:COG1181 78 LGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRGElaDLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEEL 157
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2059122299 163 LAHAQACFDAGGTVVIEEFLDGPEVSLFVLcDGRTTVPLSP 203
Cdd:COG1181 158 AAALEEAFKYDDKVLVEEFIDGREVTVGVL-GNGGPRALPP 197
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
52-202 |
1.20e-09 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 59.56 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 52 EAVSALATKLGVDLVV-VGPEAPLAAGVSDAVRAAGIPVFGPSKEAAQLEASKAFAKQIMAEAGVPTAMARVATNAEEAA 130
Cdd:COG3919 66 DALLELAERHGPDVLIpTGDEYVELLSRHRDELEEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 131 DALATFGAPHVVK--------DDGLAAGKGVVVTNDREEALAHAQACFDAGGTVVIEEFL---DGPEVSLFVLCDGRTTV 199
Cdd:COG3919 146 ALAEDLGFPVVVKpadsvgydELSFPGKKKVFYVDDREELLALLRRIAAAGYELIVQEYIpgdDGEMRGLTAYVDRDGEV 225
|
...
gi 2059122299 200 PLS 202
Cdd:COG3919 226 VAT 228
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
50-201 |
2.54e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 59.00 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 50 NPEAVSALATKLGVDLVVVGpEAPLA--AGVSDAVRAAGIPVFGPSKEAAQLEASKAFAKQIMAEAGVPT--AMARVATN 125
Cdd:PRK12833 65 NPAAILAAARQCGADAIHPG-YGFLSenAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTvpGSDGVVAS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 126 AEEAADALATFGAPHVVKDDGLAAGKGVVVTNDREE-------ALAHAQACFDAGGtVVIEEFLD-GPEVSLFVLCDGRT 197
Cdd:PRK12833 144 LDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQlaaelplAQREAQAAFGDGG-VYLERFIArARHIEVQILGDGER 222
|
....
gi 2059122299 198 TVPL 201
Cdd:PRK12833 223 VVHL 226
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
1-194 |
3.17e-09 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 57.97 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 1 MKVLVIGPGGReHAIVRSL---LEDPNVSEVHAAPGNAGISK-----LVPtHAIDGNNPEAVSALATKLGVDLVVVG--P 70
Cdd:PRK12767 2 MNILVTSAGRR-VQLVKALkksLLKGRVIGADISELAPALYFadkfyVVP-KVTDPNYIDRLLDICKKEKIDLLIPLidP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 71 EAPLAAGVSDAVRAAGIPVFGPSKEAAQLEASKAFAKQIMAEAGVPTAMARVATNAE--EAADALATFGAPHVVKDDGLA 148
Cdd:PRK12767 80 ELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEdfKAALAKGELQFPLFVKPRDGS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2059122299 149 AGKGVVVTNDREEaLAHAqacFDAGGTVVIEEFLDGPEVSLFVLCD 194
Cdd:PRK12767 160 ASIGVFKVNDKEE-LEFL---LEYVPNLIIQEFIEGQEYTVDVLCD 201
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
50-196 |
7.42e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 57.69 E-value: 7.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 50 NPEAVSALATKLGVDLVVVGpEAPLA--AGVSDAVRAAGIPVFGPSKEAAQLEASKAFAKQIMAEAGVPT--AMARVATN 125
Cdd:PRK08654 62 NIERIIDVAKKAGADAIHPG-YGFLAenPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVlpGTEEGIED 140
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2059122299 126 AEEAADALATFGAPHVVKDDGLAAGKGVVVTNDREE---ALAH----AQACFdAGGTVVIEEFLDGP-EVSLFVLCDGR 196
Cdd:PRK08654 141 IEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEEledAIEStqsiAQSAF-GDSTVFIEKYLEKPrHIEIQILADKH 218
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
80-199 |
1.01e-08 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 56.95 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 80 DAVRAAGIpVF-GPSKEAAQLEASKAFAKQIMAEAGVPTA--MARVATNAEEAADALATFGAPHVVKddglAA----GKG 152
Cdd:COG4770 93 EACEDAGI-VFiGPSPEAIRAMGDKIAAKKLMKAAGVPVVpgSDGPVQDAEEALAIAEEIGYPVLIK----ASagggGKG 167
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2059122299 153 VVVTNDREE---ALAH----AQACFdaG-GTVVIEEFLDGP---EVSlfVLCDGRTTV 199
Cdd:COG4770 168 MRVVRSEEEleeAFESarreAKAAF--GdDRVYLEKYIERPrhiEVQ--VLADKHGNV 221
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
103-212 |
1.80e-08 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 55.50 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 103 KAFAKQIMAEAGVPTAMARVATNAEEAADALATFGAPHVVKDdgLAAGK--GVVVTNDREEALAHAQACFDAGGTVVIEE 180
Cdd:PRK01372 99 KLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKP--AREGSsvGVSKVKEEDELQAALELAFKYDDEVLVEK 176
|
90 100 110
....*....|....*....|....*....|....
gi 2059122299 181 FLDGPEVSLFVLcDGR--TTVPLSPAQDFkriYD 212
Cdd:PRK01372 177 YIKGRELTVAVL-GGKalPVIEIVPAGEF---YD 206
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
106-195 |
6.37e-08 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 52.69 E-value: 6.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 106 AKQIMAEAGVPTA--MARVATNAEEAADALATFGAPHVVKDDGLAAGKGVVVTNDREE-------ALAHAQACFdAGGTV 176
Cdd:pfam02786 5 FKAAMKEAGVPTVpgTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEElaelfalALAEAPAAF-GNPQV 83
|
90 100
....*....|....*....|
gi 2059122299 177 VIEEFLDGP-EVSLFVLCDG 195
Cdd:pfam02786 84 LVEKSLKGPkHIEYQVLRDA 103
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
76-194 |
1.03e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 53.88 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 76 AGVSDAVRAAGIPVFGPSKEAAQLEASKAFAKQIMAEAGVP------TAMArvatNAEEAADALATFGAPHVVKDDGLAA 149
Cdd:PRK06111 89 ASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPvvpgitTNLE----DAEEAIAIARQIGYPVMLKASAGGG 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2059122299 150 GKGVVVTNDrEEALAHA-------QACFDAGGTVVIEEFLDGPE-VSLFVLCD 194
Cdd:PRK06111 165 GIGMQLVET-EQELTKAfesnkkrAANFFGNGEMYIEKYIEDPRhIEIQLLAD 216
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
103-184 |
1.76e-07 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 53.62 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 103 KAFAKQIMAEAGVPTAMARVATNAEEAADALATFGAPHVVK-DDGlAAGKGVVVT-NDREEALAHAQACFDAGGTVVIEE 180
Cdd:PRK14016 215 KELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKpLDG-NHGRGVTVNiTTREEIEAAYAVASKESSDVIVER 293
|
....
gi 2059122299 181 FLDG 184
Cdd:PRK14016 294 YIPG 297
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
49-200 |
2.44e-07 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 53.05 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 49 NNPEAVS---ALATKL-----------------GVDLVVVGPEAPLAAGVSDAVRAAGIPVFGPSKEAA-QLEASKAFaK 107
Cdd:PRK12815 597 NNPETVStdyDTADRLyfepltledvlnvaeaeNIKGVIVQFGGQTAINLAKGLEEAGLTILGTSPDTIdRLEDRDRF-Y 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 108 QIMAEAGVPTAMARVATNAEEAADALATFGAPHVVKDDGLAAGKGVVVTNDrEEALahaQACFDAGGT----VVIEEFLD 183
Cdd:PRK12815 676 QLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYD-EPAL---EAYLAENASqlypILIDQFID 751
|
170
....*....|....*...
gi 2059122299 184 GPEVSLFVLCDGR-TTVP 200
Cdd:PRK12815 752 GKEYEVDAISDGEdVTIP 769
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
84-183 |
3.50e-07 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 52.08 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 84 AAGIPVFgPSKEAAQLEASKAFAKQIMAEAGVPTAMARVATNAEEAADALATFGAPHVVK------DdglaaGKGVVVTN 157
Cdd:PRK06019 83 AARVPVP-PGPDALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKtrrggyD-----GKGQWVIR 156
|
90 100
....*....|....*....|....*.
gi 2059122299 158 DREEaLAHAQACFdAGGTVVIEEFLD 183
Cdd:PRK06019 157 SAED-LEAAWALL-GSVPCILEEFVP 180
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
87-194 |
9.25e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 50.87 E-value: 9.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 87 IPVFGPSKEAAQLEASKAFAKQIMAEAGVPT--AMARVATNAEEAADALATFGAPHVVKDDGLAAGKGVVVTNDREE--- 161
Cdd:PRK05586 100 IVFIGPDSETIELMGNKSNAREIMIKAGVPVvpGSEGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEElik 179
|
90 100 110
....*....|....*....|....*....|....*...
gi 2059122299 162 ----ALAHAQACFdAGGTVVIEEFLDGPE-VSLFVLCD 194
Cdd:PRK05586 180 afntAKSEAKAAF-GDDSMYIEKFIENPKhIEFQILGD 216
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
86-185 |
1.17e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 50.51 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 86 GIPVFGPSKEAAQLEASKAFAKQIMAEAGVPTAM-ARVATNAEEAADALAT-FGAPHVVKDDGLAAGKGVVVTNDREE-- 161
Cdd:PRK08462 101 NIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPgSDGALKSYEEAKKIAKeIGYPVILKAAAGGGGRGMRVVEDESDle 180
|
90 100
....*....|....*....|....*....
gi 2059122299 162 -----ALAHAQACFdAGGTVVIEEFLDGP 185
Cdd:PRK08462 181 nlylaAESEALSAF-GDGTMYMEKFINNP 208
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
74-199 |
1.51e-06 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 50.26 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 74 LAAGVSDAVRAAGIPVFGPSKEAAQL-EASKAFaKQIMAEAGVPTAMARVATNAEEAADALATFGAPHVVKddglAA--- 149
Cdd:COG0458 86 LAVELEEAGILEGVKILGTSPDAIDLaEDRELF-KELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVR----PSyvl 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2059122299 150 -GKGVVVTNDREEALAHAQACFDAGGT--VVIEEFLDG-PEVSLFVLCDGRTTV 199
Cdd:COG0458 161 gGRGMGIVYNEEELEEYLERALKVSPDhpVLIDESLLGaKEIEVDVVRDGEDNV 214
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
106-170 |
2.61e-06 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 48.03 E-value: 2.61e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 106 AKQIMAEAGVPTAMARVATNAEEAADALATFGAP-HVVKDDGLAAGK----GVVVTNDREEALAHAQACF 170
Cdd:pfam08442 7 AKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKvYVVKAQVLAGGRgkagGVKLAKSPEEAKEVAKEML 76
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
85-212 |
2.74e-06 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 48.96 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 85 AGIPVFGPSKEAAQLEASKAFAKQIMAEAGVPTAMARVATNAEEA----ADALATFGAPHVVKddglAA--GK--GVVVT 156
Cdd:PRK01966 106 LGIPYVGCGVLASALSMDKILTKRLLAAAGIPVAPYVVLTRGDWEeaslAEIEAKLGLPVFVK----PAnlGSsvGISKV 181
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2059122299 157 NDREE---ALAHAQAcFDAggTVVIEEFLDGPEVSLFVLC-DGRTTVP--LSPAQDFkriYD 212
Cdd:PRK01966 182 KNEEElaaALDLAFE-YDR--KVLVEQGIKGREIECAVLGnDPKASVPgeIVKPDDF---YD 237
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
106-168 |
3.80e-06 |
|
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439815 [Multi-domain] Cd Length: 388 Bit Score: 48.89 E-value: 3.80e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2059122299 106 AKQIMAEAGVPTAMARVATNAEEAADALATFG-APHVVKDDGLAAGK----GVVVTNDREEALAHAQA 168
Cdd:COG0045 8 AKELLAKYGVPVPRGIVATTPEEAVAAAEELGgPPVVVKAQVHAGGRgkagGVKLAKSPEEAREAAEE 75
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
107-183 |
7.08e-06 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 47.76 E-value: 7.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 107 KQIMAEAGVPTAMARVATNAEEAADALATFGAPHVVK------DdglaaGKGVVVTNDREEALAHAQAcfDAGGTVVIEE 180
Cdd:COG0026 94 KAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKtrrggyD-----GKGQVVIKSAADLEAAWAA--LGGGPCILEE 166
|
...
gi 2059122299 181 FLD 183
Cdd:COG0026 167 FVP 169
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
106-168 |
8.25e-06 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 47.78 E-value: 8.25e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2059122299 106 AKQIMAEAGVPTAMARVATNAEEAADALAT-FGAPHVVKDDGLAAGK----GVVVTNDREEALAHAQA 168
Cdd:PRK00696 8 AKELFAKYGVPVPRGIVATTPEEAVEAAEElGGGVWVVKAQVHAGGRgkagGVKLAKSPEEAREFAKQ 75
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
44-183 |
2.12e-05 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 46.28 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 44 HAIDGNNPEAVSALATKLGVDLVVVGPEApLAAGVSDAVRAAGIPVFgPSKEAAQL----EASKAFAKQimaEAGVPTAM 119
Cdd:PRK09288 57 HVIDMLDGDALRAVIEREKPDYIVPEIEA-IATDALVELEKEGFNVV-PTARATRLtmnrEGIRRLAAE---ELGLPTSP 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2059122299 120 ARVATNAEEAADALATFGAPHVVKDDGLAAGKGVVVTNDREE-------ALAHAQAcfdAGGTVVIEEFLD 183
Cdd:PRK09288 132 YRFADSLEELRAAVEEIGYPCVVKPVMSSSGKGQSVVRSPEDiekaweyAQEGGRG---GAGRVIVEEFID 199
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
80-196 |
2.26e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 46.33 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 80 DAVRAAGIPVFGPSKEAAQLEASKAFAKQIMAEAGVPT---AMARVATnAEEAADALATFGAPHVVKDDGLAAGKGVVVT 156
Cdd:PRK08591 93 EICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVvpgSDGPVDD-EEEALAIAKEIGYPVIIKATAGGGGRGMRVV 171
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2059122299 157 NDREE-------ALAHAQACFDAGGtVVIEEFLDGP---EVSlfVLCDGR 196
Cdd:PRK08591 172 RTEAElekafsmARAEAKAAFGNPG-VYMEKYLENPrhiEIQ--VLADGH 218
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
79-198 |
2.56e-05 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 46.76 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 79 SDAVRAAGIPvfGPSKEAAQLEASKAFAKQIMAEAGVPTAMARVATNAEEAADALATFGAPHVVKDDGLAAGKGVVVTND 158
Cdd:PRK02186 86 SEVARRLGLP--AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCAS 163
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2059122299 159 REEALAHAQACFDAGG-TVVIEEFLDGPEVSLFVLCDGRTT 198
Cdd:PRK02186 164 VAEAAAHCAALRRAGTrAALVQAYVEGDEYSVETLTVARGH 204
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
111-183 |
4.90e-05 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 43.78 E-value: 4.90e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2059122299 111 AEAGVPTAMARVATNAEEAADALATFGAPHVVKDDGLA-AGKGVVVTNDREEALAHAQACFDagGTVVIEEFLD 183
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLPQAWEELGD--GPVIVEEFVP 72
|
|
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
106-143 |
1.48e-04 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 43.96 E-value: 1.48e-04
10 20 30
....*....|....*....|....*....|....*...
gi 2059122299 106 AKQIMAEAGVPTAMARVATNAEEAADALATFGAPHVVK 143
Cdd:COG1042 493 AKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLK 530
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
112-285 |
1.91e-04 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 41.60 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 112 EAGVPTAMARVATNAEEAADALatfgaphVVK-DDGlAAGKGVVVTNDREEALAhaqacfdAGGTVVIEEFLDGPEVSLF 190
Cdd:pfam02655 13 NAGVPTPETLQAEELLREEKKY-------VVKpRDG-CGGEGVRKVENGREDEA-------FIENVLVQEFIEGEPLSVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 191 VLCDGRTTVPLSpaqdFKRIY-DNDEGPN--TGGMgayTPLEWAPEGLVQEVIDRVAQPTVDEMARRGTPFIgvlycgla 267
Cdd:pfam02655 78 LLSDGEKALPLS----VNRQYiDNGGSGFvyAGNV---TPSRTELKEEIIELAEEVVECLPGLRGYVGVDLV-------- 142
|
170
....*....|....*...
gi 2059122299 268 LTSRGTRVIEFNVRFGDP 285
Cdd:pfam02655 143 LKDNEPYVIEVNPRITTS 160
|
|
| PRK02471 |
PRK02471 |
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB; |
101-197 |
3.22e-04 |
|
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
Pssm-ID: 179427 [Multi-domain] Cd Length: 752 Bit Score: 42.99 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 101 ASKAFAKQIMAEAGVPTAMARVATNAEEAadalatfgaphvVKDDGLAAGKGVVV----TN---------------DREE 161
Cdd:PRK02471 487 ENKVVTKKILAEAGFPVPAGDEFTSLEEA------------LADYSLFADKAIVVkpksTNfglgisifkepasleDYEK 554
|
90 100 110
....*....|....*....|....*....|....*.
gi 2059122299 162 ALAHAqacFDAGGTVVIEEFLDGPEVSLFVLcDGRT 197
Cdd:PRK02471 555 ALEIA---FREDSSVLVEEFIVGTEYRFFVL-DGKV 586
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
2-184 |
4.14e-04 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 42.68 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 2 KVLVIGPGG--------------------REHAIvRSLLEDPNVSEVHAAPGNAGISKLVPTHaidgnnPEAVSALATKL 61
Cdd:TIGR01369 8 KILVIGSGPivigqaaefdysgsqackalKEEGY-RVILVNSNPATIMTDPEMADKVYIEPLT------PEAVEKIIEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 62 GVD--LVVVGPEAPLAAGV----SDAVRAAGIPVFGPSKEAAQL-EASKAFaKQIMAEAGVPTAMARVATNAEEAADALA 134
Cdd:TIGR01369 81 RPDaiLPTFGGQTALNLAVeleeSGVLEKYGVEVLGTPVEAIKKaEDRELF-REAMKEIGEPVPESEIAHSVEEALAAAK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2059122299 135 TFGAPHVVKDDGLAAGKGVVVTNDREEALAHAQACFDAG--GTVVIEEFLDG 184
Cdd:TIGR01369 160 EIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAG 211
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
78-279 |
5.96e-04 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 41.56 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 78 VSDAVRAAGIPVFGPSKeaAQLEAS-KAFAKQIMAEAGVPTAMARVATNAEEAADALATFGAPHVVKDDGLAAGKGVVVT 156
Cdd:TIGR00768 65 VLRYLESLGVPVINSSD--AILNAGdKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 157 NDREEA---LAHAQACFDAGGTVVIEEFLDGPE---VSLFVLCDgrtTVPLSpaqdFKRIYDNDEGPNTGGMGAYTPLEW 230
Cdd:TIGR00768 143 RDRQAAeslLEHFEQLNGPQNLFLVQEYIKKPGgrdIRVFVVGD---EVVAA----IYRITSGHWRSNLARGGKAEPCSL 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2059122299 231 APEglvqevidrvaqptVDEMARRGTPFIGVLYCGLAL--TSRGTRVIEFN 279
Cdd:TIGR00768 216 TEE--------------IEELAIKAAKALGLDVAGVDLleSEDGLLVNEVN 252
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
49-281 |
9.56e-04 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 41.52 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 49 NNPEAVSA---LATKL-----------------GVDLVVVGPEAPLAAGVSDAVRAAGIPVFGPSKEAA-QLEASKAFAk 107
Cdd:TIGR01369 596 YNPETVSTdydTSDRLyfepltfedvmniieleKPEGVIVQFGGQTPLNLAKALEEAGVPILGTSPESIdRAEDREKFS- 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 108 QIMAEAGVPTAMARVATNAEEAADALATFGAPHVVKDDGLAAGKGVVVTNDREEALAHAQACFDAGGT--VVIEEFL-DG 184
Cdd:TIGR01369 675 ELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEhpVLIDKYLeDA 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 185 PEVSLFVLCDGRTTvpLSPAqdfkrIYDNDE--GPNTGGMGAYTPlewaPEGLVQEVIDRVAQpTVDEMArRGTPFIGVL 262
Cdd:TIGR01369 755 VEVDVDAVSDGEEV--LIPG-----IMEHIEeaGVHSGDSTCVLP----PQTLSAEIVDRIKD-IVRKIA-KELNVKGLM 821
|
250
....*....|....*....
gi 2059122299 263 YCGLALTSRGTRVIEFNVR 281
Cdd:TIGR01369 822 NIQFAVKDGEVYVIEVNPR 840
|
|
| PRK14572 |
PRK14572 |
D-alanyl-alanine synthetase A; Provisional |
82-192 |
2.98e-03 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173036 [Multi-domain] Cd Length: 347 Bit Score: 39.50 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 82 VRAAGIPVFGPSKEAAQLEASKAFAKQIMAEAGVPTA------MARVATNAEEAADALATFGAPHVVKDDGLAAGKGVVV 155
Cdd:PRK14572 110 LDTLGIPYTGSGVLASALAMDKTRANQIFLQSGQKVApffeleKLKYLNSPRKTLLKLESLGFPQFLKPVEGGSSVSTYK 189
|
90 100 110
....*....|....*....|....*....|....*..
gi 2059122299 156 TNDREEALAHAQACFDAGGTVVIEEFLDGPEVSLFVL 192
Cdd:PRK14572 190 ITNAEQLMTLLALIFESDSKVMSQSFLSGTEVSCGVL 226
|
|
| Peripla_BP_6 |
pfam13458 |
Periplasmic binding protein; This family includes a diverse range of periplasmic binding ... |
47-93 |
3.83e-03 |
|
Periplasmic binding protein; This family includes a diverse range of periplasmic binding proteins.
Pssm-ID: 433225 [Multi-domain] Cd Length: 342 Bit Score: 39.18 E-value: 3.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2059122299 47 DGNNPEAVSALATKL----GVDLVVVGPEAPLAAGVSDAVRAAGIPVFGPS 93
Cdd:pfam13458 50 DQGDPDVAAAAARRLvdqdGVDAIVGGVSSAVALAVAEVLAKKGVPVIGPA 100
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
80-187 |
4.80e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 39.35 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 80 DAVRAAGIPVFGPSKEAAQLEASKAFAKQIMAEAGVPT--AMARVATNAEEAADALATFGAPHVVKDDGLAAGKGVVVTN 157
Cdd:PRK12999 97 RACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVipGSEGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVR 176
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2059122299 158 DREE-------ALAHAQACFdaG-GTVVIEEFLDGP---EV 187
Cdd:PRK12999 177 SEEEleeaferAKREAKAAF--GnDEVYLEKYVENPrhiEV 215
|
|
| LivK |
COG0683 |
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ... |
25-183 |
5.95e-03 |
|
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid transport and metabolism];
Pssm-ID: 440447 [Multi-domain] Cd Length: 314 Bit Score: 38.37 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 25 VSEVHAAPGNAGIsKLVPTHAIDGNNPEAVSALATKL----GVDLVVVGPEAPLAAGVSDAVRAAGIPVFGPSkeaaqle 100
Cdd:COG0683 31 VEEINAAGGVLGR-KIELVVEDDASDPDTAVAAARKLidqdKVDAIVGPLSSGVALAVAPVAEEAGVPLISPS------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 101 askAFAKQIMAEAGVPTaMARVATNAEEAADALATFgaphVVKDDGL----------AAGKGVVvtndrEEALAHAQAcf 170
Cdd:COG0683 103 ---ATAPALTGPECSPY-VFRTAPSDAQQAEALADY----LAKKLGAkkvallyddyAYGQGLA-----AAFKAALKA-- 167
|
170
....*....|...
gi 2059122299 171 dAGGTVVIEEFLD 183
Cdd:COG0683 168 -AGGEVVGEEYYP 179
|
|
| PRK07206 |
PRK07206 |
hypothetical protein; Provisional |
44-281 |
5.99e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 180883 [Multi-domain] Cd Length: 416 Bit Score: 38.86 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 44 HAIDGNNPEAVSALAtKLGVDLVVVGPEAplaaGVSDAVRAAGI--PVFGPSKEAAQLEASKAFAKQIMAEAGVPTAMAR 121
Cdd:PRK07206 53 VIINGDIDDLVEFLR-KLGPEAIIAGAES----GVELADRLAEIltPQYSNDPALSSARRNKAEMINALAEAGLPAARQI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 122 VATNAEEAA---DALATFGAPHVVKDDGLAAGKGVVVTNDREEAlahaQACFDA-----------GGTVVIEEFLDGPE- 186
Cdd:PRK07206 128 NTADWEEAEawlRENGLIDRPVVIKPLESAGSDGVFICPAKGDW----KHAFNAilgkanklglvNETVLVQEYLIGTEy 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059122299 187 VSLFVLCDGRTTVplSPAQDFKRIYDNDegpntgGMGAYTPLEWAP--EGLVQEVIDRVAQpTVDEMARRgtpfIGVLYC 264
Cdd:PRK07206 204 VVNFVSLDGNHLV--TEIVRYHKTSLNS------GSTVYDYDEFLDysEPEYQELVDYTKQ-ALDALGIK----NGPAHA 270
|
250
....*....|....*..
gi 2059122299 265 GLALTSRGTRVIEFNVR 281
Cdd:PRK07206 271 EVMLTADGPRLIEIGAR 287
|
|
| |
