|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
962-1294 |
1.75e-150 |
|
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various eukaryotic acetyl-CoA carboxylases, N-terminal to the catalytic domain (pfam01039). This enzyme (EC:6.4.1.2) is involved in the synthesis of long-chain fatty acids, as it catalyzes the rate-limiting step in this process.
Pssm-ID: 462429 Cd Length: 718 Bit Score: 471.66 E-value: 1.75e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 962 ELDDPSKVHPAEPFTGELPAQQTLPILGEKLHQVFHSVLENLTNVMSGFCLpepvfSIKLKEWVQKLMMTLRHPSLPLLE 1041
Cdd:pfam08326 1 ALDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDN-----QVIMNETLKDLIEVLRDPELPYLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 1042 LQEIMTSVAGRIPAPVEKSVRRVMAQYASNitsvLCQFPSQQIATILDCHAATLQRKADREVFFINTQSIVQLVQRYRSG 1121
Cdd:pfam08326 76 WQEQLSALSGRIPAKLEASLRQLVERAHSR----SAEFPAKQLRKILDKFLAELVLKADRDLFEATLAPLVDLVERYRNG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 1122 IRGYMKTVVLDLLRRYLRVEHHFQQA--HYDKCVINLREQFKPDMSQVLDCIFSHAQVAKKNQLVIMLIDELCGP---DP 1196
Cdd:pfam08326 152 LKGHEYSVFASLLEEYYDVEKLFSGGnvREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNcpnVS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 1197 SLSDELISILNELTQLSKSEHCKVALRARQILIASHLPSYELRHNQVESIFLSAIDMYGH--------QFCPENLKKLIL 1268
Cdd:pfam08326 232 NVAKELRPVLKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYgesgwkhrEPSLEVLKELID 311
|
330 340
....*....|....*....|....*.
gi 767974042 1269 SETTIFDVLPTFFYHANKVVCMASLE 1294
Cdd:pfam08326 312 SKYTVFDVLPPFFYHSDPWVSLAALE 337
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
260-786 |
2.18e-136 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 425.20 E-value: 2.18e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 260 IEKVLIANNGIAAVKCMRSIRrwayEMfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 339
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCR----EL-----GIRTVAVYSDAD--RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 340 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewteddlqqg 419
Cdd:COG4770 71 KATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 420 krisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSE---IPGSP-IFLMKLA 495
Cdd:COG4770 135 -----------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREakaAFGDDrVYLEKYI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 496 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGS 575
Cdd:COG4770 204 ERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 576 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARIT 654
Cdd:COG4770 284 FYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPfTQEDIKL-----------------------RGHAIECRIN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 655 SENPDEGFKPSSGTVQELNFRSSknvwgyFSVAATGGLHE------FADSQFGHCFSWGENREEAISNMVVALKELSIRG 728
Cdd:COG4770 341 AEDPARGFLPSPGTITRLRPPGG------PGVRVDSGVYEgyeippYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEG 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 767974042 729 dFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQAEKPDimlgvvcgALNVADAM 786
Cdd:COG4770 415 -VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE--------ELALAAAM 463
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
260-766 |
1.29e-114 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 366.43 E-value: 1.29e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 260 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 339
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACK---------ELGIKTVAVHSTAD--RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 340 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPwsGSgltvewteddlqqg 419
Cdd:PRK08591 71 EITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVP--GS-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 420 krisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIP---GSP-IFLMKLA 495
Cdd:PRK08591 135 -----------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPgVYMEKYL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 496 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGS 575
Cdd:PRK08591 204 ENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 576 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARIT 654
Cdd:PRK08591 284 FYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLSiKQEDIVF-----------------------RGHAIECRIN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 655 SENPDEGFKPSSGTVQelnfrssknvwGYFsvaATGGLH--------------EFADSQFGHCFSWGENREEAISNMVVA 720
Cdd:PRK08591 341 AEDPAKNFMPSPGKIT-----------RYH---PPGGPGvrvdsavytgytipPYYDSMIGKLIVHGETREEAIARMKRA 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 767974042 721 LKELSIRGdFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQA 766
Cdd:PRK08591 407 LSEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
262-757 |
8.62e-87 |
|
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 130302 [Multi-domain] Cd Length: 1143 Bit Score: 307.52 E-value: 8.62e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 262 KVLIANNGIAAVKCMRSIrrwayemfrNERAIRFVVMVTPED------LKANAEY-IKMADHYVPVpggpnnNNYANVEL 334
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAA---------NELGIRTVAIYSEEDklslhrQKADESYqVGEGPDLGPI------EAYLSIDE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 335 IVDIAKRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewted 414
Cdd:TIGR01235 66 IIRVAKLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGT----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 415 dlqqgkrisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGS----PIF 490
Cdd:TIGR01235 135 ----------------DGPPETMEEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAfgndEVY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 491 LMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLY 570
Cdd:TIGR01235 199 VEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 571 SQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLK-------DIRLlygespwgvtpisfetpsnppl 643
Cdd:TIGR01235 279 DNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGASLPTPQlgvpnqeDIRT---------------------- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 644 aRGHVIAARITSENPDEGFKPSSGTVQElnFRSSknvwGYFSVAATGG-------LHEFADSQFGHCFSWGENREEAISN 716
Cdd:TIGR01235 337 -NGYAIQCRVTTEDPANNFQPDTGRIEA--YRSA----GGFGIRLDGGnsyagaiITPYYDSLLVKVSAWASTPEEAAAK 409
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 767974042 717 MVVALKELSIRGdFRTTVEYLINLLETESFQNNDIDTGWLD 757
Cdd:TIGR01235 410 MDRALREFRIRG-VKTNIPFLENVLGHPKFLDGSYDTRFID 449
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
420-613 |
4.33e-55 |
|
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: 190.59 E-value: 4.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 420 KRISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGSP----IFLMKLA 495
Cdd:pfam02786 10 KEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 496 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQD-G 574
Cdd:pfam02786 90 KGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALDPFsG 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 767974042 575 SFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPL 613
Cdd:pfam02786 170 EYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
651-757 |
4.04e-34 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 214878 [Multi-domain] Cd Length: 107 Bit Score: 126.76 E-value: 4.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 651 ARITSENPDEGFKPSSGTVQELNFRSSKNVwgYFSVAATGGLHE--FADSQFGHCFSWGENREEAISNMVVALKELSIRG 728
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 767974042 729 dFRTTVEYLINLLETESFQNNDIDTGWLD 757
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
895-961 |
3.26e-16 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 74.56 E-value: 3.26e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767974042 895 TVLRSPSAGKL-----TQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIKRP-GAVLEAGCVVARL 961
Cdd:pfam00364 1 TEIKSPMIGESvregvVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
896-961 |
2.60e-14 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 68.60 E-value: 2.60e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767974042 896 VLRSPSAGKLTQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIK-RPGAVLEAGCVVARL 961
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLLVVI 67
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
902-962 |
7.35e-04 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 39.39 E-value: 7.35e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767974042 902 AGKLTQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIKRP-GAVLEAGCVVARLE 962
Cdd:PRK08225 9 AGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQeGDFVNEGDVLLEIE 70
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
962-1294 |
1.75e-150 |
|
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various eukaryotic acetyl-CoA carboxylases, N-terminal to the catalytic domain (pfam01039). This enzyme (EC:6.4.1.2) is involved in the synthesis of long-chain fatty acids, as it catalyzes the rate-limiting step in this process.
Pssm-ID: 462429 Cd Length: 718 Bit Score: 471.66 E-value: 1.75e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 962 ELDDPSKVHPAEPFTGELPAQQTLPILGEKLHQVFHSVLENLTNVMSGFCLpepvfSIKLKEWVQKLMMTLRHPSLPLLE 1041
Cdd:pfam08326 1 ALDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDN-----QVIMNETLKDLIEVLRDPELPYLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 1042 LQEIMTSVAGRIPAPVEKSVRRVMAQYASNitsvLCQFPSQQIATILDCHAATLQRKADREVFFINTQSIVQLVQRYRSG 1121
Cdd:pfam08326 76 WQEQLSALSGRIPAKLEASLRQLVERAHSR----SAEFPAKQLRKILDKFLAELVLKADRDLFEATLAPLVDLVERYRNG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 1122 IRGYMKTVVLDLLRRYLRVEHHFQQA--HYDKCVINLREQFKPDMSQVLDCIFSHAQVAKKNQLVIMLIDELCGP---DP 1196
Cdd:pfam08326 152 LKGHEYSVFASLLEEYYDVEKLFSGGnvREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNcpnVS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 1197 SLSDELISILNELTQLSKSEHCKVALRARQILIASHLPSYELRHNQVESIFLSAIDMYGH--------QFCPENLKKLIL 1268
Cdd:pfam08326 232 NVAKELRPVLKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYgesgwkhrEPSLEVLKELID 311
|
330 340
....*....|....*....|....*.
gi 767974042 1269 SETTIFDVLPTFFYHANKVVCMASLE 1294
Cdd:pfam08326 312 SKYTVFDVLPPFFYHSDPWVSLAALE 337
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
260-786 |
2.18e-136 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 425.20 E-value: 2.18e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 260 IEKVLIANNGIAAVKCMRSIRrwayEMfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 339
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCR----EL-----GIRTVAVYSDAD--RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 340 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewteddlqqg 419
Cdd:COG4770 71 KATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 420 krisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSE---IPGSP-IFLMKLA 495
Cdd:COG4770 135 -----------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREakaAFGDDrVYLEKYI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 496 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGS 575
Cdd:COG4770 204 ERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 576 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARIT 654
Cdd:COG4770 284 FYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPfTQEDIKL-----------------------RGHAIECRIN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 655 SENPDEGFKPSSGTVQELNFRSSknvwgyFSVAATGGLHE------FADSQFGHCFSWGENREEAISNMVVALKELSIRG 728
Cdd:COG4770 341 AEDPARGFLPSPGTITRLRPPGG------PGVRVDSGVYEgyeippYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEG 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 767974042 729 dFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQAEKPDimlgvvcgALNVADAM 786
Cdd:COG4770 415 -VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE--------ELALAAAM 463
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
260-766 |
1.29e-114 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 366.43 E-value: 1.29e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 260 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 339
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACK---------ELGIKTVAVHSTAD--RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 340 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPwsGSgltvewteddlqqg 419
Cdd:PRK08591 71 EITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVP--GS-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 420 krisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIP---GSP-IFLMKLA 495
Cdd:PRK08591 135 -----------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPgVYMEKYL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 496 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGS 575
Cdd:PRK08591 204 ENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 576 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARIT 654
Cdd:PRK08591 284 FYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLSiKQEDIVF-----------------------RGHAIECRIN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 655 SENPDEGFKPSSGTVQelnfrssknvwGYFsvaATGGLH--------------EFADSQFGHCFSWGENREEAISNMVVA 720
Cdd:PRK08591 341 AEDPAKNFMPSPGKIT-----------RYH---PPGGPGvrvdsavytgytipPYYDSMIGKLIVHGETREEAIARMKRA 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 767974042 721 LKELSIRGdFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQA 766
Cdd:PRK08591 407 LSEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
258-757 |
3.22e-107 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 366.00 E-value: 3.22e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 258 RVIEKVLIANNGIAAVKCMRSIrrwayemfrNERAIRFVVMVTPED------LKANAEYIkmadhyVPVPGGPNNNnYAN 331
Cdd:PRK12999 3 KKIKKVLVANRGEIAIRIFRAA---------TELGIRTVAIYSEEDklslhrFKADEAYL------IGEGKHPVRA-YLD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 332 VELIVDIAKRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSGSGltvew 411
Cdd:PRK12999 67 IDEIIRVAKQAGVDAIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGP----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 412 teddlqqgkrisvpedvydkgcVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIP---GSP 488
Cdd:PRK12999 142 ----------------------IDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKaafGND 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 489 -IFLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVE 567
Cdd:PRK12999 200 eVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 568 YLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRL-------KDIRLlygespwgvtpisfetpsn 640
Cdd:PRK12999 280 FLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGATLHDLeigipsqEDIRL------------------- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 641 pplaRGHVIAARITSENPDEGFKPSSGTVQElnFRSSknvwGYFSVAATGGLHeFADSQFGHCF--------SWGENREE 712
Cdd:PRK12999 341 ----RGYAIQCRITTEDPANNFMPDTGRITA--YRSP----GGFGVRLDGGNA-FAGAEITPYYdsllvkltAWGRTFEQ 409
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 767974042 713 AISNMVVALKELSIRGdFRTTVEYLINLLETESFQNNDIDTGWLD 757
Cdd:PRK12999 410 AVARMRRALREFRIRG-VKTNIPFLENVLKHPDFRAGDYTTSFID 453
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
260-757 |
3.58e-104 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 357.47 E-value: 3.58e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 260 IEKVLIANNG-IAavkcmrsIR--RWAYEMfrnerAIRFVVMVTPED------LKANAEY-IKMADHyvPVpggpnnNNY 329
Cdd:COG1038 4 IKKVLVANRGeIA-------IRvfRAATEL-----GIRTVAIYSEEDryslhrFKADEAYlIGEGKG--PV------DAY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 330 ANVELIVDIAKRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPwsGSgltv 409
Cdd:COG1038 64 LDIEEIIRVAKEKGVDAIHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIP--GT---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 410 ewteddlqqgkrisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIP---G 486
Cdd:COG1038 138 ---------------------EGPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKaafG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 487 SP-IFLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGT 565
Cdd:COG1038 197 DDeVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGT 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 566 VEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-------RLKDIRLlygespwgvtpisfetp 638
Cdd:COG1038 277 VEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYSLDdpeigipSQEDIRL----------------- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 639 snpplaRGHVIAARITSENPDEGFKPSSGTVQElnFRSSknvwGYFSV---AATGglheFA--------DSQFGHCFSWG 707
Cdd:COG1038 340 ------NGYAIQCRITTEDPANNFMPDTGRITA--YRSA----GGFGIrldGGNA----YTgavitpyyDSLLVKVTAWG 403
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 767974042 708 ENREEAISNMVVALKELSIRGdFRTTVEYLINLLETESFQNNDIDTGWLD 757
Cdd:COG1038 404 RTFEEAIRKMRRALREFRIRG-VKTNIPFLENVLNHPDFLAGECTTSFID 452
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
261-757 |
5.20e-103 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 336.57 E-value: 5.20e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 261 EKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIAK 340
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACR---------ELGIKTVAVYSEAD--KNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 341 RIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewteddlqqgk 420
Cdd:PRK08654 72 KAGADAIHPGYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGT----------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 421 risvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSeIPGS-----PIFLMKLA 495
Cdd:PRK08654 135 ----------EEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIESTQS-IAQSafgdsTVFIEKYL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 496 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSqDGS 575
Cdd:PRK08654 204 EKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS-NGN 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 576 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPL-HRLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARIT 654
Cdd:PRK08654 283 FYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELsFKQEDITI-----------------------RGHAIECRIN 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 655 SENPDEGFKPSSGTVQelNFRSSknvwGYFSVAATGGLH------EFADSQFGHCFSWGENREEAISNMVVALKELSIRG 728
Cdd:PRK08654 340 AEDPLNDFAPSPGKIK--RYRSP----GGPGVRVDSGVHmgyeipPYYDSMISKLIVWGRTREEAIARMRRALYEYVIVG 413
|
490 500
....*....|....*....|....*....
gi 767974042 729 dFRTTVEYLINLLETESFQNNDIDTGWLD 757
Cdd:PRK08654 414 -VKTNIPFHKAVMENENFVRGNLHTHFIE 441
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
260-759 |
5.60e-102 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 331.99 E-value: 5.60e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 260 IEKVLIANNGIAAVKCMRSIRRWAyemfrneraIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 339
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLG---------IRTVAIYSEAD--RDALHVKMADEAYLIGGPRVQESYLNLEKIIEIA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 340 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSGSGLTvewteddlqqg 419
Cdd:PRK06111 71 KKTGAEAIHPGYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLE----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 420 krisvpedvydkgcvkDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIP---GSP-IFLMKLA 495
Cdd:PRK06111 140 ----------------DAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKAFESNKKRAAnffGNGeMYIEKYI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 496 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGS 575
Cdd:PRK06111 204 EDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 576 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPL-HRLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARIT 654
Cdd:PRK06111 284 FYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLsFTQDDIKR-----------------------SGHAIEVRIY 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 655 SENPDEgFKPSSGTVQELNFRSSKNVWGYFSVAATGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTV 734
Cdd:PRK06111 341 AEDPKT-FFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAISRLHDALEELKVEG-IKTNI 418
|
490 500
....*....|....*....|....*.
gi 767974042 735 EYLINLLETESFQNNDIDTGWL-DYL 759
Cdd:PRK06111 419 PLLLQVLEDPVFKAGGYTTGFLtKQL 444
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
260-756 |
2.27e-93 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 308.18 E-value: 2.27e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 260 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 339
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACR---------EMGIETVAVYSEAD--KDALHVQLADEAVCIGPASSKDSYLNIQNIISAT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 340 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewteddlqqg 419
Cdd:PRK05586 71 VLTGAQAIHPGFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 420 krisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGS----PIFLMKLA 495
Cdd:PRK05586 135 -----------EGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAfgddSMYIEKFI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 496 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGS 575
Cdd:PRK05586 204 ENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 576 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARIT 654
Cdd:PRK05586 284 FYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSiKQEDIKI-----------------------NGHSIECRIN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 655 SENPDEGFKPSSGTVQELNFRSSKNVwgYFSVAATGG--LHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRT 732
Cdd:PRK05586 341 AEDPKNGFMPCPGKIEELYIPGGLGV--RVDSAVYSGytIPPYYDSMIGKLIVYGKDREEAIQKMKRALGEFIIEG-VNT 417
|
490 500
....*....|....*....|....
gi 767974042 733 TVEYLINLLETESFQNNDIDTGWL 756
Cdd:PRK05586 418 NIDFQFIILEDEEFIKGTYDTSFI 441
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
260-757 |
3.94e-91 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 302.05 E-value: 3.94e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 260 IEKVLIANNGIAAVKCMRSIRrwayEMfrNERAIrfVVMVTPEDlkaNAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 339
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQ----EM--GKEAI--AIYSTADK---DALYLKYADAKICIGGAKSSESYLNIPAIISAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 340 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewteddlqqg 419
Cdd:PRK08462 73 EIFEADAIFPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGS---------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 420 krisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGS----PIFLMKLA 495
Cdd:PRK08462 137 -----------DGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENLYLAAESEALSAfgdgTMYMEKFI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 496 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGS 575
Cdd:PRK08462 206 NNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 576 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARITS 655
Cdd:PRK08462 286 FYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPSQESIKL-----------------------KGHAIECRITA 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 656 ENPdEGFKPSSGTVQEL------NFRSSKNVWGYFSVAAtgglheFADSQFGHCFSWGENREEAISNMVVALKELSIRGd 729
Cdd:PRK08462 343 EDP-KKFYPSPGKITKWiapggrNVRMDSHAYAGYVVPP------YYDSMIGKLIVWGEDRNRAIAKMKRALKEFKVEG- 414
|
490 500
....*....|....*....|....*...
gi 767974042 730 FRTTVEYLINLLETESFQNNDIDTGWLD 757
Cdd:PRK08462 415 IKTTIPFHLEMMENADFINNKYDTKYLE 442
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
260-766 |
8.89e-91 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 301.67 E-value: 8.89e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 260 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDLKANAeyIKMADHYVPVPGGPNNNNYANVELIVDIA 339
Cdd:PRK12833 5 IRKVLVANRGEIAVRIIRAAR---------ELGMRTVAACSDADRDSLA--ARMADEAVHIGPSHAAKSYLNPAAILAAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 340 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewteddlqqg 419
Cdd:PRK12833 74 RQCGADAIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGS---------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 420 krisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAED----FPILFRQVQSEIPGSPIFLMKLA 495
Cdd:PRK12833 138 -----------DGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQlaaeLPLAQREAQAAFGDGGVYLERFI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 496 QHARHLEVQILADQYgNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLY-SQDG 574
Cdd:PRK12833 207 ARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFdDARG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 575 SFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARI 653
Cdd:PRK12833 286 EFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLRfAQGDIAL-----------------------RGAALECRI 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 654 TSENPDEGFKPSSGTVQELNF------RSSKNVWGYFSVAAtgglheFADSQFGHCFSWGENREEAISNMVVALKELSIR 727
Cdd:PRK12833 343 NAEDPLRDFFPNPGRIDALVWpqgpgvRVDSLLYPGYRVPP------FYDSLLAKLIVHGEDRAAALARAARALRELRID 416
|
490 500 510
....*....|....*....|....*....|....*....
gi 767974042 728 GdFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQA 766
Cdd:PRK12833 417 G-MKTTAPLHRALLADADVRAGRFHTNFLEAWLAEWRAA 454
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
262-757 |
8.62e-87 |
|
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 130302 [Multi-domain] Cd Length: 1143 Bit Score: 307.52 E-value: 8.62e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 262 KVLIANNGIAAVKCMRSIrrwayemfrNERAIRFVVMVTPED------LKANAEY-IKMADHYVPVpggpnnNNYANVEL 334
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAA---------NELGIRTVAIYSEEDklslhrQKADESYqVGEGPDLGPI------EAYLSIDE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 335 IVDIAKRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewted 414
Cdd:TIGR01235 66 IIRVAKLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGT----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 415 dlqqgkrisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGS----PIF 490
Cdd:TIGR01235 135 ----------------DGPPETMEEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAfgndEVY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 491 LMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLY 570
Cdd:TIGR01235 199 VEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 571 SQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLK-------DIRLlygespwgvtpisfetpsnppl 643
Cdd:TIGR01235 279 DNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGASLPTPQlgvpnqeDIRT---------------------- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 644 aRGHVIAARITSENPDEGFKPSSGTVQElnFRSSknvwGYFSVAATGG-------LHEFADSQFGHCFSWGENREEAISN 716
Cdd:TIGR01235 337 -NGYAIQCRVTTEDPANNFQPDTGRIEA--YRSA----GGFGIRLDGGnsyagaiITPYYDSLLVKVSAWASTPEEAAAK 409
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 767974042 717 MVVALKELSIRGdFRTTVEYLINLLETESFQNNDIDTGWLD 757
Cdd:TIGR01235 410 MDRALREFRIRG-VKTNIPFLENVLGHPKFLDGSYDTRFID 449
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
259-757 |
1.84e-86 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 289.69 E-value: 1.84e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 259 VIEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYV-----PVPGgpnnnnYANVE 333
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACA---------EMGIRSVAIYSEAD--RHALHVKRADEAYsigadPLAG------YLNPR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 334 LIVDIAKRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewte 413
Cdd:PRK07178 64 RLVNLAVETGCDALHPGYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGS---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 414 ddlqqgkrisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIP---GSP-I 489
Cdd:PRK07178 134 -----------------EGNLADLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELEQNFPRVISEATkafGSAeV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 490 FLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYL 569
Cdd:PRK07178 197 FLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 570 YSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPL-HRLKDIRLlygespwgvtpisfetpsnpplaRGHV 648
Cdd:PRK07178 277 LDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLsYKQEDIQH-----------------------RGFA 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 649 IAARITSENPDEGFKPSSGTVQElnfrssknvwgYFSVAATG---------GLH--EFADSQFGHCFSWGENREEAISNM 717
Cdd:PRK07178 334 LQFRINAEDPKNDFLPSFGKITR-----------YYAPGGPGvrtdtaiytGYTipPYYDSMCAKLIVWALTWEEALDRG 402
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 767974042 718 VVALKELSIRGdFRTTVEYLINLLETESFQNNDIDTGWLD 757
Cdd:PRK07178 403 RRALDDMRVQG-VKTTIPYYQEILRNPEFRSGQFNTSFVE 441
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
260-780 |
3.86e-69 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 240.87 E-value: 3.86e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 260 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNnYANVELIVDIA 339
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACR---------DLHIKSVAIYTEPD--RECLHVKIADEAYRIGTDPIKG-YLDVKRIVEIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 340 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPwsgsgltvewteddlqqg 419
Cdd:PRK08463 70 KACGADAIHPGYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVP------------------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 420 krisvpedvydkGCVKDVDEGLEA----AERIGFPLMIKASEGGGGKGIRKAESAEDFPILF----RQVQSEIPGSPIFL 491
Cdd:PRK08463 132 ------------GTEKLNSESMEEikifARKIGYPVILKASGGGGGRGIRVVHKEEDLENAFesckREALAYFNNDEVFM 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 492 MKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYS 571
Cdd:PRK08463 200 EKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 572 QDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLhrlkdirllygespwgvtpisfETPSNPPLARGHVIAA 651
Cdd:PRK08463 280 DYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEIL----------------------DLEQSDIKPRGFAIEA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 652 RITSENPDEGFKPSSGTVQEL------NFRSSKNVWGYFSVAAtgglheFADSQFGHCFSWGENREEAISNMVVALKELS 725
Cdd:PRK08463 338 RITAENVWKNFIPSPGKITEYypalgpSVRVDSHIYKDYTIPP------YYDSMLAKLIVKATSYDLAVNKLERALKEFV 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767974042 726 IRGdFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQA------EKPDIMLGVVCGAL 780
Cdd:PRK08463 412 IDG-IRTTIPFLIAITKTREFRRGYFDTSYIETHMQELLEKtedrhqENKEEVIAAIAAAL 471
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
420-613 |
4.33e-55 |
|
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: 190.59 E-value: 4.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 420 KRISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGSP----IFLMKLA 495
Cdd:pfam02786 10 KEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 496 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQD-G 574
Cdd:pfam02786 90 KGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALDPFsG 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 767974042 575 SFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPL 613
Cdd:pfam02786 170 EYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
260-378 |
1.65e-43 |
|
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp domain. The family contains the N-terminus of biotin carboxylase enzymes, and propionyl-CoA carboxylase A chain.
Pssm-ID: 425585 [Multi-domain] Cd Length: 108 Bit Score: 153.41 E-value: 1.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 260 IEKVLIANNGIAAVKCMRSIRRWAyemfrneraIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 339
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELG---------IRTVAVYSEAD--ANSLHVRLADEAVCLGPGPASESYLNIDAIIDAA 69
|
90 100 110
....*....|....*....|....*....|....*....
gi 767974042 340 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEA 378
Cdd:pfam00289 70 KETGADAIHPGYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
332-612 |
2.30e-40 |
|
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: 150.41 E-value: 2.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 332 VELIVDIAKRIPVQAVWAGWGHASEnpKLPELLCKNGVAflGPPSEAMWALGDKIASTVVAQTLQVPTlPWSGsgltvew 411
Cdd:COG0439 6 IAAAAELARETGIDAVLSESEFAVE--TAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PGFA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 412 teddlqqgkrisvpedvydkgCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEI----PGS 487
Cdd:COG0439 74 ---------------------LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAkagsPNG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 488 PIFLMKLAQHaRHLEVQILADQyGNAVSlfgrdCSIQRRHQK---IVE---EAPATIAPlAIFEFMEQCAIRLAKTVGYV 561
Cdd:COG0439 133 EVLVEEFLEG-REYSVEGLVRD-GEVVV-----CSITRKHQKppyFVElghEAPSPLPE-ELRAEIGELVARALRALGYR 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 767974042 562 -SAGTVEYLYSQDGSFHFLELNPRLQVEH--PCTEMIADVNLPAAQLQIAMGVP 612
Cdd:COG0439 205 rGAFHTEFLLTPDGEPYLIEINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
651-757 |
4.04e-34 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 214878 [Multi-domain] Cd Length: 107 Bit Score: 126.76 E-value: 4.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 651 ARITSENPDEGFKPSSGTVQELNFRSSKNVwgYFSVAATGGLHE--FADSQFGHCFSWGENREEAISNMVVALKELSIRG 728
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 767974042 729 dFRTTVEYLINLLETESFQNNDIDTGWLD 757
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
651-757 |
3.23e-30 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 426981 [Multi-domain] Cd Length: 108 Bit Score: 115.67 E-value: 3.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 651 ARITSENPDEGFKPSSGTVQELNFRSSKNVWGYFSVAATGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdF 730
Cdd:pfam02785 2 ARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG-V 80
|
90 100
....*....|....*....|....*..
gi 767974042 731 RTTVEYLINLLETESFQNNDIDTGWLD 757
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLE 107
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
895-961 |
3.26e-16 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 74.56 E-value: 3.26e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767974042 895 TVLRSPSAGKL-----TQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIKRP-GAVLEAGCVVARL 961
Cdd:pfam00364 1 TEIKSPMIGESvregvVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
896-961 |
2.60e-14 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 68.60 E-value: 2.60e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767974042 896 VLRSPSAGKLTQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIK-RPGAVLEAGCVVARL 961
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLLVVI 67
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
314-613 |
3.50e-12 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 69.96 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 314 ADHYVPVPGgPNNNNYANVELIVDIAKRIPVQAVWA---GWGHA-SEN-PKLPEllcknGVAFLGPPSEAMWALGDKIAS 388
Cdd:COG3919 48 VDEVVVVPD-PGDDPEAFVDALLELAERHGPDVLIPtgdEYVELlSRHrDELEE-----HYRLPYPDADLLDRLLDKERF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 389 TVVAQTLQVPtlpwsgsgltvewteddlqqgkrisVPEDVYdkgcVKDVDEGLEAAERIGFPLMIKASEG--------GG 460
Cdd:COG3919 122 YELAEELGVP-------------------------VPKTVV----LDSADDLDALAEDLGFPVVVKPADSvgydelsfPG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 461 GKGIRKAESAEDFPILFRQ---------VQSEIPG--SPIFLmklaqharhleVQILADQYGNAVSLFGrdcsiqrrHQK 529
Cdd:COG3919 173 KKKVFYVDDREELLALLRRiaaagyeliVQEYIPGddGEMRG-----------LTAYVDRDGEVVATFT--------GRK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 530 IVEeAPATIAPLAIFEF-----MEQCAIRLAKTVGYVSAGTVEYLY-SQDGSFHFLELNPRLQVEHPCTEmIADVNLPAA 603
Cdd:COG3919 234 LRH-YPPAGGNSAARESvddpeLEEAARRLLEALGYHGFANVEFKRdPRDGEYKLIEINPRFWRSLYLAT-AAGVNFPYL 311
|
330
....*....|
gi 767974042 604 QLQIAMGVPL 613
Cdd:COG3919 312 LYDDAVGRPL 321
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
408-639 |
5.02e-08 |
|
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: 57.70 E-value: 5.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 408 TVEWTED-DLQQGKRISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASE--GGGGKGIrkAESAEDFPILFRQVQSEI 484
Cdd:TIGR01369 121 AIKKAEDrELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPVIVRPAFtlGGTGGGI--AYNREELKEIAERALSAS 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 485 PGSPIFLMKLAQHARHLEVQILADQYGNAVSLfgrdCSIQR-----RH--QKIVeeapatIAP---LAIFEF--MEQCAI 552
Cdd:TIGR01369 199 PINQVLVEKSLAGWKEIEYEVMRDSNDNCITV----CNMENfdpmgVHtgDSIV------VAPsqtLTDKEYqmLRDASI 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 553 RLAKTVGYVSAGTVEY-LYSQDGSFHFLELNPRLQ---------VEHPctemIADVnlpAAQLqiAMGVPLHRLK-DIRl 621
Cdd:TIGR01369 269 KIIRELGIEGGCNVQFaLNPDSGRYYVIEVNPRVSrssalaskaTGYP----IAKV---AAKL--AVGYTLDELKnPVT- 338
|
250
....*....|....*...
gi 767974042 622 lygespwGVTPISFEtPS 639
Cdd:TIGR01369 339 -------GTTPASFE-PS 348
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
432-584 |
4.13e-07 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 54.78 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 432 GCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDfpiLFRQVQSEI---PGSPIFLMKLAQHARHLEVQILAD 508
Cdd:PLN02735 721 GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDK---LKTYLETAVevdPERPVLVDKYLSDATEIDVDALAD 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 509 QYGNAV-----------SLFGRD--CSIQRrhQKIVEEAPATIaplaifefmEQCAIRLAKTVGYVSAGTVEYLYSQDGS 575
Cdd:PLN02735 798 SEGNVViggimehieqaGVHSGDsaCSLPT--QTIPSSCLATI---------RDWTTKLAKRLNVCGLMNCQYAITPSGE 866
|
....*....
gi 767974042 576 FHFLELNPR 584
Cdd:PLN02735 867 VYIIEANPR 875
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
434-613 |
1.38e-06 |
|
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: 53.08 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 434 VKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGSPIFLMKLAQHARHLEVQILADqyGNA 513
Cdd:TIGR01369 690 ATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSD--GEE 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 514 VSLFGrdcsIQrRHqkiVEEA-----------PATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSqDGSFHFLELN 582
Cdd:TIGR01369 768 VLIPG----IM-EH---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVK-DGEVYVIEVN 838
|
170 180 190
....*....|....*....|....*....|.
gi 767974042 583 PRLQVEHPCTEMIADVNLPAAQLQIAMGVPL 613
Cdd:TIGR01369 839 PRASRTVPFVSKATGVPLAKLAVRVMLGKKL 869
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
434-584 |
1.11e-05 |
|
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: 49.49 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 434 VKDVDEGLEAAERIGFPLMIKASE--GGGGKGIrkAESAEDFPILFRQVQSEIPGSPIFLMKLAQHARHLEVQILADQYG 511
Cdd:COG0458 135 ATSVEEALAIAEEIGYPVIVRPSYvlGGRGMGI--VYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGED 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 512 NAVSLfgrdCSIQrrHqkiVEEA------PATIAP-----LAIFEFMEQCAIRLAKTVGYVSAGTVEYLYsQDGSFHFLE 580
Cdd:COG0458 213 NVIIV----GIME--H---IEPAgvhsgdSICVAPpqtlsDKEYQRLRDATLKIARALGVVGLCNIQFAV-DDGRVYVIE 282
|
....
gi 767974042 581 LNPR 584
Cdd:COG0458 283 VNPR 286
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
422-584 |
4.86e-04 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 43.72 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 422 ISVPeDVYDKGCVKDVDEGLEAAErIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQ-----VQSEIPGSPIflmklaq 496
Cdd:PRK12767 124 IPTP-KSYLPESLEDFKAALAKGE-LQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYvpnliIQEFIEGQEY------- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 497 harhlEVQILADQYGNAVSLFGRdcsiqRRH--------QKIVEEAPAtiaplaIFEFMEqcaiRLAKTVGYVSAGTVEY 568
Cdd:PRK12767 195 -----TVDVLCDLNGEVISIVPR-----KRIevragetsKGVTVKDPE------LFKLAE----RLAEALGARGPLNIQC 254
|
170
....*....|....*.
gi 767974042 569 LYSqDGSFHFLELNPR 584
Cdd:PRK12767 255 FVT-DGEPYLFEINPR 269
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
902-962 |
7.35e-04 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 39.39 E-value: 7.35e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767974042 902 AGKLTQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIKRP-GAVLEAGCVVARLE 962
Cdd:PRK08225 9 AGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQeGDFVNEGDVLLEIE 70
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
434-473 |
1.11e-03 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 43.55 E-value: 1.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 767974042 434 VKDVDEGLEAAERIGFPLMIKAS--EGGGGKGIrkAESAEDF 473
Cdd:PRK05294 149 AHSMEEALEVAEEIGYPVIIRPSftLGGTGGGI--AYNEEEL 188
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
434-598 |
1.67e-03 |
|
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: 41.85 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 434 VKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEipGSPIFLmklaqharhleVQ--ILADQyg 511
Cdd:COG0189 117 TRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEALTEL--GSEPVL-----------VQefIPEED-- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 512 navslfGRD-----------CSIQRR----HQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGtVEYLYSQDGsF 576
Cdd:COG0189 182 ------GRDirvlvvggepvAAIRRIpaegEFRTNLARGGRAEPVELTDEERELALRAAPALGLDFAG-VDLIEDDDG-P 253
|
170 180
....*....|....*....|..
gi 767974042 577 HFLELNPRlqvehPCTEMIADV 598
Cdd:COG0189 254 LVLEVNVT-----PGFRGLERA 270
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
895-962 |
1.69e-03 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 38.46 E-value: 1.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767974042 895 TVLRSPSAGklTQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRV-KYIKRPGAVLEAGCVVARLE 962
Cdd:PRK07051 13 TFYRRPSPD--APPYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVvEFLVEDGEPVEAGQVLARIE 79
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
442-586 |
3.78e-03 |
|
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: 39.68 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974042 442 EAAERIGFPLMIKASEGGGGKGIRKAE--SAEDFPILFRQVQSEIPGSPIFLMKLAQHARHLEVQIlADQY-GNAVSLF- 517
Cdd:pfam02655 25 EELLREEKKYVVKPRDGCGGEGVRKVEngREDEAFIENVLVQEFIEGEPLSVSLLSDGEKALPLSV-NRQYiDNGGSGFv 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767974042 518 ---GRDCSIQRRHQKIVEEApatiaplaifefmEQCAIRLAKTVGYVSagtVEYLYSqDGSFHFLELNPRLQ 586
Cdd:pfam02655 104 yagNVTPSRTELKEEIIELA-------------EEVVECLPGLRGYVG---VDLVLK-DNEPYVIEVNPRIT 158
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
434-464 |
7.68e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 40.52 E-value: 7.68e-03
10 20 30
....*....|....*....|....*....|.
gi 767974042 434 VKDVDEGLEAAERIGFPLMIKASEGGGGKGI 464
Cdd:PRK14016 235 VTSAEDAWEAAEEIGYPVVVKPLDGNHGRGV 265
|
|
| |
