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Conserved domains on  [gi|1358786755|ref|WP_105596235|]
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MULTISPECIES: acetyl-CoA carboxylase biotin carboxylase subunit family protein [unclassified Microbacterium]

Protein Classification

ATP-grasp domain-containing protein( domain architecture ID 11418417)

ATP-grasp domain-containing protein may catalyze the ATP-assisted reaction of a carboxylic acid with a nucleophile via the formation of an acylphosphate intermediate, such as Bacillus subtilis alanine--anticapsin ligase that is part of the bacABCDEFG operon responsible for the biosynthesis of bacilysin, an irreversible inactivator of the glutaminase domain of glucosamine synthetase

EC:  6.-.-.-
Gene Ontology:  GO:0005524|GO:0016874

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
13-250 3.14e-43

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: 3.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755  13 VASALQAMHPKD--MRLATLDEHLIPTLGSIRDQFGIPGVSQEQSLRFSDKKLMKEALANSGVRTPQFVVVSADSEPPTy 90
Cdd:COG0439     5 IIAAAAELARETgiDAVLSESEFAVETAAELAEELGLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALA- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755  91 dlLVARLGSPLFVKPTCGAGSHGTRLIETEAEWRAWL-------TVRPEDVEFEVDAFLQGTLYHVDFVVGIDSSDWCSV 163
Cdd:COG0439    84 --FAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALaearaeaKAGSPNGEVLVEEFLEGREYSVEGLVRDGEVVVCSI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755 164 GEYTHPNAEFL-QGGTLGSRaLSPDDWATpiVRHAAVQALNALGAGTGVYHVELFLSSAGTVTFLEAAMRPPGAMVPDLY 242
Cdd:COG0439   162 TRKHQKPPYFVeLGHEAPSP-LPEELRAE--IGELVARALRALGYRRGAFHTEFLLTPDGEPYLIEINARLGGEHIPPLT 238

                  ....*...
gi 1358786755 243 SHIYGKNI 250
Cdd:COG0439   239 ELATGVDL 246
 
Name Accession Description Interval E-value
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
13-250 3.14e-43

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: 3.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755  13 VASALQAMHPKD--MRLATLDEHLIPTLGSIRDQFGIPGVSQEQSLRFSDKKLMKEALANSGVRTPQFVVVSADSEPPTy 90
Cdd:COG0439     5 IIAAAAELARETgiDAVLSESEFAVETAAELAEELGLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALA- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755  91 dlLVARLGSPLFVKPTCGAGSHGTRLIETEAEWRAWL-------TVRPEDVEFEVDAFLQGTLYHVDFVVGIDSSDWCSV 163
Cdd:COG0439    84 --FAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALaearaeaKAGSPNGEVLVEEFLEGREYSVEGLVRDGEVVVCSI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755 164 GEYTHPNAEFL-QGGTLGSRaLSPDDWATpiVRHAAVQALNALGAGTGVYHVELFLSSAGTVTFLEAAMRPPGAMVPDLY 242
Cdd:COG0439   162 TRKHQKPPYFVeLGHEAPSP-LPEELRAE--IGELVARALRALGYRRGAFHTEFLLTPDGEPYLIEINARLGGEHIPPLT 238

                  ....*...
gi 1358786755 243 SHIYGKNI 250
Cdd:COG0439   239 ELATGVDL 246
PRK02186 PRK02186
argininosuccinate lyase; Provisional
32-318 2.09e-14

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 74.50  E-value: 2.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755  32 EHLIPTLGSIRDQFGIPGVSQEQSLRFSDKKLMKEALANSGVRTPQFVVVSADSEppTYDLLvARLGSPLFVKPTCGAGS 111
Cdd:PRK02186   79 EYFIEVASEVARRLGLPAANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAV--ALDAL-DGLTYPVVVKPRMGSGS 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755 112 HGTRLIETEAEWRAWLTV--RPEDVEFEVDAFLQGTLYHVDfVVGIDSSDWC--SVGEYTHPNAEFLQGGtlgsrALSPD 187
Cdd:PRK02186  156 VGVRLCASVAEAAAHCAAlrRAGTRAALVQAYVEGDEYSVE-TLTVARGHQVlgITRKHLGPPPHFVEIG-----HDFPA 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755 188 DWATP----IVRhAAVQALNALGAGTGVYHVELFLsSAGTVTFLEAAMRPPGAMVPDLYSHIYGKNIQSLgVMAQWRSDG 263
Cdd:PRK02186  230 PLSAPqrerIVR-TVLRALDAVGYAFGPAHTELRV-RGDTVVIIEINPRLAGGMIPVLLEEAFGVDLLDH-VIDLHLGVA 306
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1358786755 264 ATAIiksiasPKRTGFGIWAW-IPPAPGVVVALQAP--ELPPGSELSITWRCSVGDAL 318
Cdd:PRK02186  307 AFAD------PTAKRYGAIRFvLPARSGVLRGLLFLpdDIAARPELRFHPLKQPGDAL 358
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
72-233 1.21e-04

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: 42.24  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755  72 GVRTPQFVVVSADSEpptYDLLVARLGSPLFVK-PTCGAGSHGTRLIETeaewrawltvrPEDVEFEVDAFLQGTLY--- 147
Cdd:pfam02222   4 GLPTPRFMAAESLEE---LIEAGQELGYPCVVKaRRGGYDGKGQYVVRS-----------EADLPQAWEELGDGPVIvee 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755 148 HVDF-----VVGIDSSDwcsvGE-YTHPNAEFLQ-GGTL----GSRALSPDDWATpiVRHAAVQALNALGaGTGVYHVEL 216
Cdd:pfam02222  70 FVPFdrelsVLVVRSVD----GEtAFYPVVETIQeDGICrlsvAPARVPQAIQAE--AQDIAKRLVDELG-GVGVFGVEL 142
                         170
                  ....*....|....*..
gi 1358786755 217 FLSSAGTVTFLEAAMRP 233
Cdd:pfam02222 143 FVTEDGDLLINELAPRP 159
 
Name Accession Description Interval E-value
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
13-250 3.14e-43

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: 3.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755  13 VASALQAMHPKD--MRLATLDEHLIPTLGSIRDQFGIPGVSQEQSLRFSDKKLMKEALANSGVRTPQFVVVSADSEPPTy 90
Cdd:COG0439     5 IIAAAAELARETgiDAVLSESEFAVETAAELAEELGLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALA- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755  91 dlLVARLGSPLFVKPTCGAGSHGTRLIETEAEWRAWL-------TVRPEDVEFEVDAFLQGTLYHVDFVVGIDSSDWCSV 163
Cdd:COG0439    84 --FAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALaearaeaKAGSPNGEVLVEEFLEGREYSVEGLVRDGEVVVCSI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755 164 GEYTHPNAEFL-QGGTLGSRaLSPDDWATpiVRHAAVQALNALGAGTGVYHVELFLSSAGTVTFLEAAMRPPGAMVPDLY 242
Cdd:COG0439   162 TRKHQKPPYFVeLGHEAPSP-LPEELRAE--IGELVARALRALGYRRGAFHTEFLLTPDGEPYLIEINARLGGEHIPPLT 238

                  ....*...
gi 1358786755 243 SHIYGKNI 250
Cdd:COG0439   239 ELATGVDL 246
PRK02186 PRK02186
argininosuccinate lyase; Provisional
32-318 2.09e-14

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 74.50  E-value: 2.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755  32 EHLIPTLGSIRDQFGIPGVSQEQSLRFSDKKLMKEALANSGVRTPQFVVVSADSEppTYDLLvARLGSPLFVKPTCGAGS 111
Cdd:PRK02186   79 EYFIEVASEVARRLGLPAANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAV--ALDAL-DGLTYPVVVKPRMGSGS 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755 112 HGTRLIETEAEWRAWLTV--RPEDVEFEVDAFLQGTLYHVDfVVGIDSSDWC--SVGEYTHPNAEFLQGGtlgsrALSPD 187
Cdd:PRK02186  156 VGVRLCASVAEAAAHCAAlrRAGTRAALVQAYVEGDEYSVE-TLTVARGHQVlgITRKHLGPPPHFVEIG-----HDFPA 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755 188 DWATP----IVRhAAVQALNALGAGTGVYHVELFLsSAGTVTFLEAAMRPPGAMVPDLYSHIYGKNIQSLgVMAQWRSDG 263
Cdd:PRK02186  230 PLSAPqrerIVR-TVLRALDAVGYAFGPAHTELRV-RGDTVVIIEINPRLAGGMIPVLLEEAFGVDLLDH-VIDLHLGVA 306
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1358786755 264 ATAIiksiasPKRTGFGIWAW-IPPAPGVVVALQAP--ELPPGSELSITWRCSVGDAL 318
Cdd:PRK02186  307 AFAD------PTAKRYGAIRFvLPARSGVLRGLLFLpdDIAARPELRFHPLKQPGDAL 358
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
60-229 6.15e-12

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: 65.51  E-value: 6.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755  60 DKKLMKEALANSGVRTPQFVVVSADsEPPTYDLLVARLGSPLFVKPTCGAGSHGTRLIETEAEWR-AWLTVRPEDVEFEV 138
Cdd:COG1181    95 DKALTKRVLAAAGLPTPPYVVLRRG-ELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAaALEEAFKYDDKVLV 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755 139 DAFLQGTlyhvDFVVGI--DSSDWCS-VGEYThPNAEF-------LQGGT---LGSRaLSPDDWATpiVRHAAVQALNAL 205
Cdd:COG1181   174 EEFIDGR----EVTVGVlgNGGPRALpPIEIV-PENGFydyeakyTDGGTeyiCPAR-LPEELEER--IQELALKAFRAL 245
                         170       180
                  ....*....|....*....|....
gi 1358786755 206 GaGTGVYHVELFLSSAGTVTFLEA 229
Cdd:COG1181   246 G-CRGYARVDFRLDEDGEPYLLEV 268
PRK07206 PRK07206
hypothetical protein; Provisional
60-240 2.70e-07

hypothetical protein; Provisional


Pssm-ID: 180883 [Multi-domain]  Cd Length: 416  Bit Score: 51.95  E-value: 2.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755  60 DKKLMKEALANSGVRTPQFVVVSADSEPPTYdLLVARL-GSPLFVKPTCGAGSHGTRLIETEAEWR-AWLTV--RPEDVE 135
Cdd:PRK07206  108 NKAEMINALAEAGLPAARQINTADWEEAEAW-LRENGLiDRPVVIKPLESAGSDGVFICPAKGDWKhAFNAIlgKANKLG 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755 136 FEVDA-----FLQGTLYHVDFVVGIDSSDWCSVGEYTHPNAEflQGGTLGSRalspDDW--ATPIVRHAAV----QALNA 204
Cdd:PRK07206  187 LVNETvlvqeYLIGTEYVVNFVSLDGNHLVTEIVRYHKTSLN--SGSTVYDY----DEFldYSEPEYQELVdytkQALDA 260
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1358786755 205 LGAGTGVYHVELFLSSAGTVtFLEAAMRPPGAMVPD 240
Cdd:PRK07206  261 LGIKNGPAHAEVMLTADGPR-LIEIGARLDGGLHPD 295
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
59-150 3.21e-07

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 51.42  E-value: 3.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755  59 SDKKLMKEALANSGVRTPQFVVVsADSEPPTYDLLVARLGSPLFVKPTCGAGSHGTRLIETEAEWRAWLTVRPEDVefeV 138
Cdd:PRK12767  110 NDKWLTYEFLKENGIPTPKSYLP-ESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYVPNLI---I 185
                          90
                  ....*....|..
gi 1358786755 139 DAFLQGTLYHVD 150
Cdd:PRK12767  186 QEFIEGQEYTVD 197
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
60-149 1.33e-05

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 46.26  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755  60 DKKLMKEALANSGVRTPQFVVVSADSEPptyDLLVARLGSPLFVKPTCGAGSHGTRLIETEAEWR-AWLTVRPEDVEFEV 138
Cdd:PRK01372   98 DKLRTKLVWQAAGLPTPPWIVLTREEDL---LAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQaALELAFKYDDEVLV 174
                          90
                  ....*....|.
gi 1358786755 139 DAFLQGTLYHV 149
Cdd:PRK01372  175 EKYIKGRELTV 185
ddl PRK01966
D-alanine--D-alanine ligase;
60-105 1.77e-05

D-alanine--D-alanine ligase;


Pssm-ID: 234993 [Multi-domain]  Cd Length: 333  Bit Score: 45.88  E-value: 1.77e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1358786755  60 DKKLMKEALANSGVRTPQFVVVSA-DSEPPTYDLLVARLGSPLFVKP 105
Cdd:PRK01966  123 DKILTKRLLAAAGIPVAPYVVLTRgDWEEASLAEIEAKLGLPVFVKP 169
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
72-233 1.21e-04

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: 42.24  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755  72 GVRTPQFVVVSADSEpptYDLLVARLGSPLFVK-PTCGAGSHGTRLIETeaewrawltvrPEDVEFEVDAFLQGTLY--- 147
Cdd:pfam02222   4 GLPTPRFMAAESLEE---LIEAGQELGYPCVVKaRRGGYDGKGQYVVRS-----------EADLPQAWEELGDGPVIvee 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358786755 148 HVDF-----VVGIDSSDwcsvGE-YTHPNAEFLQ-GGTL----GSRALSPDDWATpiVRHAAVQALNALGaGTGVYHVEL 216
Cdd:pfam02222  70 FVPFdrelsVLVVRSVD----GEtAFYPVVETIQeDGICrlsvAPARVPQAIQAE--AQDIAKRLVDELG-GVGVFGVEL 142
                         170
                  ....*....|....*..
gi 1358786755 217 FLSSAGTVTFLEAAMRP 233
Cdd:pfam02222 143 FVTEDGDLLINELAPRP 159
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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