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Conserved domains on  [gi|740821371|ref|WP_038606654|]
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cobalt-precorrin-5B (C(1))-methyltransferase CbiD [Phocaeicola dorei]

Protein Classification

cobalt-precorrin-5B (C(1))-methyltransferase; precorrin-6A/cobalt-precorrin-6A reductase family protein( domain architecture ID 11132968)

cobalt-precorrin-5B (C(1))-methyltransferase catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A| precorrin-6A/cobalt-precorrin-6A reductase catalyzes the reduction of the macrocycle of precorrin-6A or cobalt-precorrin-6A to precorrin-6B or cobalt-precorrin-6B, respectively; involved in cobalamin biosynthesis; may be partial

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CbiD COG1903
Cobalamin biosynthesis protein CbiD (cobalt-precorrin-5B C-methyltransferase) [Coenzyme ...
273-593 2.93e-141

Cobalamin biosynthesis protein CbiD (cobalt-precorrin-5B C-methyltransferase) [Coenzyme transport and metabolism]; Cobalamin biosynthesis protein CbiD (cobalt-precorrin-5B C-methyltransferase) is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


:

Pssm-ID: 441507 [Multi-domain]  Cd Length: 368  Bit Score: 414.12  E-value: 2.93e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371 273 LILGEEQKMISFRLPDDEEMTLPVSHTEIEKNSATCTVVKDAGDDPDVTHGASIVVTVSFSNHPDIRFLQGEGVGRVTLP 352
Cdd:COG1903   34 LLTGEFPDEVEITLPKGIRLTFPVEDVEIDGGSASAAVIKDAGDDPDVTHGALIFARVRLTPGPGIVIDGGEGVGTVTKP 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371 353 GLGLEIGEPAINRIPRQMIMKEL-----SALYDKGLDITISVPGGKELAQRTFNPKLGIVDGISIIGTSGIVRPFSSEAF 427
Cdd:COG1903  114 GLPLPVGEPAINPVPRRMIEEAVrevlaELGYGGGVEVTISVPEGEELAKKTLNPRLGIVGGISILGTTGIVRPMSEEAW 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371 428 VEAIRREVEVCVAVGSSRLIINSGAKSERFVKKEYpGLPAQAFVHYGNFIGETLKIAAKLKVPLVTLGIMIGKAVKLAEG 507
Cdd:COG1903  194 KASIRQEIDVARANGLDHVVLTTGNRGEKFARELL-GLPEEAFVQMGNFVGYMLKEAVRHGFKKVLLVGHIGKLVKLAAG 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371 508 NLDTHSKKVVMNKEFLKQVAMEAGCSPDVESMIERLTLARELWTLLSEEDCGKFFPCLLEHCFAHCVPLLPEG-KLTILL 586
Cdd:COG1903  273 IFNTHSRVADVRLEILAALAALAGAPPELVEAILAANTAEEALELLEEAGLDAVFDLIAERAAERARERLGGDiEVEVVL 352

                 ....*..
gi 740821371 587 IDEEGNI 593
Cdd:COG1903  353 FDRDGGI 359
CobK COG2099
Precorrin-6x reductase [Coenzyme transport and metabolism]; Precorrin-6x reductase is part of ...
1-226 2.10e-58

Precorrin-6x reductase [Coenzyme transport and metabolism]; Precorrin-6x reductase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


:

Pssm-ID: 441702  Cd Length: 251  Bit Score: 195.76  E-value: 2.10e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371   1 MILILGGTTEGRTAVKVADEAGKPYFYSTKGEW-QEIQCKHGIRI-TGGMNTEKMESFCRQNDIRLLVDAAHPFASQLHR 78
Cdd:COG2099    3 MILILGGTTEARALAEALAAAGIPVIVSLATRTgAPLLPEPGGPVrVGGFGAEGLAAYLREEGIDAVIDATHPFAAQISR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371  79 TVDETSRTLHLPVIRFERKY--PPRTENIIWCEDYTDAIYRLEKAGtDHLLALTGVQTIGKLRPYWEKHTCWFRVLERET 156
Cdd:COG2099   83 NAAAACAELGIPYLRLERPAwqAPPGDLWIEVDDLEEAAAALPELG-GRVFLTTGSKELAAFAALPPQHRLLARVLPPPE 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740821371 157 SITLAQEQGFPKENLV-----FYHAGESEalLLETLHPQAILTKESGESGGFSEKVKAAQAAKIPVFAIKRPSLP 226
Cdd:COG2099  162 VLEKCEALGLPPKNIIamrgpFSLELERA--LLRQYGIDVLVTKNSGGAGGTDAKLEAARELGIPVIMIRRPPLP 234
 
Name Accession Description Interval E-value
CbiD COG1903
Cobalamin biosynthesis protein CbiD (cobalt-precorrin-5B C-methyltransferase) [Coenzyme ...
273-593 2.93e-141

Cobalamin biosynthesis protein CbiD (cobalt-precorrin-5B C-methyltransferase) [Coenzyme transport and metabolism]; Cobalamin biosynthesis protein CbiD (cobalt-precorrin-5B C-methyltransferase) is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441507 [Multi-domain]  Cd Length: 368  Bit Score: 414.12  E-value: 2.93e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371 273 LILGEEQKMISFRLPDDEEMTLPVSHTEIEKNSATCTVVKDAGDDPDVTHGASIVVTVSFSNHPDIRFLQGEGVGRVTLP 352
Cdd:COG1903   34 LLTGEFPDEVEITLPKGIRLTFPVEDVEIDGGSASAAVIKDAGDDPDVTHGALIFARVRLTPGPGIVIDGGEGVGTVTKP 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371 353 GLGLEIGEPAINRIPRQMIMKEL-----SALYDKGLDITISVPGGKELAQRTFNPKLGIVDGISIIGTSGIVRPFSSEAF 427
Cdd:COG1903  114 GLPLPVGEPAINPVPRRMIEEAVrevlaELGYGGGVEVTISVPEGEELAKKTLNPRLGIVGGISILGTTGIVRPMSEEAW 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371 428 VEAIRREVEVCVAVGSSRLIINSGAKSERFVKKEYpGLPAQAFVHYGNFIGETLKIAAKLKVPLVTLGIMIGKAVKLAEG 507
Cdd:COG1903  194 KASIRQEIDVARANGLDHVVLTTGNRGEKFARELL-GLPEEAFVQMGNFVGYMLKEAVRHGFKKVLLVGHIGKLVKLAAG 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371 508 NLDTHSKKVVMNKEFLKQVAMEAGCSPDVESMIERLTLARELWTLLSEEDCGKFFPCLLEHCFAHCVPLLPEG-KLTILL 586
Cdd:COG1903  273 IFNTHSRVADVRLEILAALAALAGAPPELVEAILAANTAEEALELLEEAGLDAVFDLIAERAAERARERLGGDiEVEVVL 352

                 ....*..
gi 740821371 587 IDEEGNI 593
Cdd:COG1903  353 FDRDGGI 359
CbiD pfam01888
CbiD; CbiD is essential for cobalamin biosynthesis in both S. typhimurium and B. megaterium, ...
273-507 8.41e-116

CbiD; CbiD is essential for cobalamin biosynthesis in both S. typhimurium and B. megaterium, no functional role has been ascribed to the protein. The CbiD protein has a putative S-AdoMet binding site. It is possible that CbiD might have the same role as CobF in undertaking the C-1 methylation and deacylation reactions required during the ring contraction process.


Pssm-ID: 460373  Cd Length: 258  Bit Score: 344.76  E-value: 8.41e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371  273 LILGEEQKMISFRLPDDEEMTLPVSHTE-IEKNSATCTVVKDAGDDPDVTHGASIVVTVSFSNhPDIRFLQGEGVGRVTL 351
Cdd:pfam01888  22 LLTGEKPDEVEITLPKGERLEIPIEQVArLGEGAALAAVIKDAGDDPDVTHGAEIWARVRLLP-GGIVIDGGEGVGRVTK 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371  352 PGLGLEIGEPAINRIPRQMIMKELSAL---YDKGLDITISVPGGKELAQRTFNPKLGIVDGISIIGTSGIVRPFSSEAFV 428
Cdd:pfam01888 101 PGLPVPVGEPAINPVPRRMIEENVREVlpeYGEGVEVTISVPEGEELAKKTFNPRLGIVGGISILGTTGIVEPMSEEAYK 180
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740821371  429 EAIRREVEVCVAVGSSRLIINSGAKSERFVKKEYpGLPAQAFVHYGNFIGETLKIAAKLKVPLVTLGIMIGKAVKLAEG 507
Cdd:pfam01888 181 ASIRQELDVARANGLDTLVLTPGNYGEDFARELL-GLPEEAIVKMGNFIGFMLDEAAELGVKRILLVGHIGKLVKLAGG 258
cbiD PRK00075
cobalt-precorrin-6A synthase; Reviewed
273-593 4.37e-102

cobalt-precorrin-6A synthase; Reviewed


Pssm-ID: 234615  Cd Length: 361  Bit Score: 313.68  E-value: 4.37e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371 273 LILGEEQKMISFRLPDDEEMTLPVSHTEIEKNSATCTVVKDAGDDPDVTHGASIVVTVSFSNHPDIRFLQGEGVGRVTLP 352
Cdd:PRK00075  30 LLTGEFPDTVEIDLPKGLRLEIPVESVELDGEQALAIVRKDAGDDPDVTHGAEIWARVRLNDSPGIVIRGGEGVGTVTRP 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371 353 GLGLEIGEPAINRIPRQMIMKEL-SALYDKGLDITISVPGGKELAQRTFNPKLGIVDGISIIGTSGIVRPFSSEAFVEAI 431
Cdd:PRK00075 110 GLGVPVGEPAINPVPRRMIEENVrEVLPEGGAEVTISVPEGEELAKKTLNPRLGIVGGISILGTTGIVEPMSEEAYLASI 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371 432 RREVEVCVAVGSSRLIINSGAKSERFVKKeYPGLPAQAFVHYGNFIGETLKIAAKLKVPLVTLGIMIGKAVKLAEGNLDT 511
Cdd:PRK00075 190 KQELDVARANGLDHVVLVTGNNGEDYARK-LLGLPEDAIIKMGNFVGPMLKAAARLGVKKVLLVGHPGKLIKLAAGIFHT 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371 512 HSKKVVMNKEFLKQVAMEAGCSPDVESMIERLTLARELWTLLSEEDCGKFFPCLLEHCFAHCVPLLPEG-KLTILLIDEE 590
Cdd:PRK00075 269 HSHVADARLEILAALAALAGAPLELLEKILAANTTEEALELLEEAGGEKLYDRIAERILERAREYVGGSiEVGVVLFDRD 348

                 ...
gi 740821371 591 GNI 593
Cdd:PRK00075 349 GQI 351
CobK COG2099
Precorrin-6x reductase [Coenzyme transport and metabolism]; Precorrin-6x reductase is part of ...
1-226 2.10e-58

Precorrin-6x reductase [Coenzyme transport and metabolism]; Precorrin-6x reductase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441702  Cd Length: 251  Bit Score: 195.76  E-value: 2.10e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371   1 MILILGGTTEGRTAVKVADEAGKPYFYSTKGEW-QEIQCKHGIRI-TGGMNTEKMESFCRQNDIRLLVDAAHPFASQLHR 78
Cdd:COG2099    3 MILILGGTTEARALAEALAAAGIPVIVSLATRTgAPLLPEPGGPVrVGGFGAEGLAAYLREEGIDAVIDATHPFAAQISR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371  79 TVDETSRTLHLPVIRFERKY--PPRTENIIWCEDYTDAIYRLEKAGtDHLLALTGVQTIGKLRPYWEKHTCWFRVLERET 156
Cdd:COG2099   83 NAAAACAELGIPYLRLERPAwqAPPGDLWIEVDDLEEAAAALPELG-GRVFLTTGSKELAAFAALPPQHRLLARVLPPPE 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740821371 157 SITLAQEQGFPKENLV-----FYHAGESEalLLETLHPQAILTKESGESGGFSEKVKAAQAAKIPVFAIKRPSLP 226
Cdd:COG2099  162 VLEKCEALGLPPKNIIamrgpFSLELERA--LLRQYGIDVLVTKNSGGAGGTDAKLEAARELGIPVIMIRRPPLP 234
CbiJ pfam02571
Precorrin-6x reductase CbiJ/CobK; This family consists of Precorrin-6x reductase EC:1.3.1.54. ...
2-226 2.16e-57

Precorrin-6x reductase CbiJ/CobK; This family consists of Precorrin-6x reductase EC:1.3.1.54. This enzyme catalyzes the reaction: precorrin-6Y + NADP(+) <=> precorrin-6X + NADPH. CbiJ and CobK both catalyze the reduction of macocycle in the colbalmin biosynthesis pathway.


Pssm-ID: 460596  Cd Length: 248  Bit Score: 193.06  E-value: 2.16e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371    2 ILILGGTTEGRTAVKVADEAGKPYFYSTKGEWQE--IQCKHGIRITGGMNTEKMESFCRQNDIRLLVDAAHPFASQLHRT 79
Cdd:pfam02571   2 ILLLGGTSEARELAEALAEAGIPVIVSVATRYGAplLPEAGGEVRVGGFGAEGLAALLREEGIDAVVDATHPFAAEISAN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371   80 VDETSRTLHLPVIRFERKY--PPRTENIIWCEDYTDAIYRLEKAGtDHLLALTGVQTIGKLRPYWEKHTCWFRVLERETS 157
Cdd:pfam02571  82 AAAACAELGIPYLRLERPSweAQPGDRWIEVDSYEEAAEALAELG-GRVLLTTGSKELAAFAPLLPGHRLLARVLPPPEV 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740821371  158 ITLAQEQGFPKENLV-----FYHAGESEalLLETLHPQAILTKESGESGGFSEKVKAAQAAKIPVFAIKRPSLP 226
Cdd:pfam02571 161 LEKCLPLGFPPKNIIamrgpFSLELERA--LLRQYGIDVLVTKDSGGAGGTDEKLEAARELGIPVIVIRRPPLP 232
cbiD TIGR00312
cobalamin biosynthesis protein CbiD; This protein has been shown by cloning into E. coli to be ...
273-543 1.82e-48

cobalamin biosynthesis protein CbiD; This protein has been shown by cloning into E. coli to be required for cobalamin biosynthesis. role_id [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273008  Cd Length: 347  Bit Score: 172.37  E-value: 1.82e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371  273 LILGEEQKMISFRLPDDEEMTLPVSHTE-IEKNSATCTVVKDAGDDPDVTHGASIVVTVSFSN-HPDIRFLQGEGVGRVT 350
Cdd:TIGR00312  14 LTKGCPDSVVLELLEPGRTLEIAIEQGElLGGHRALAIVIKEPGNDLDLTRHTEIIAEVEFTPgEGKLIIQGGEGVGIVT 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371  351 LPGLGLEIGEPAINRIPRQMIMKELSALY--DKGLDITISVPGGKELAQRTFNPKLGIVDGISIIGTSGIVRPFSSEAFV 428
Cdd:TIGR00312  94 KPGLQVREGEAAINPYPRRMIRHNLQPYLsdDETLMVTLSLPLGRTLATRTSNPALGIVGGLSILGTTGIARPMSAEAYL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371  429 EAIRREVEVCVAVGSSRLIINSGAKSERFVkKEYPGLPAQAFVHYGNFIGETLKIAAKLKVPLVTLGIMIGKAVKLAEGN 508
Cdd:TIGR00312 174 ASLACQIDTAAAQGHQCLVFVPGNIGLDLA-RQWGVPLDDEIIKTANFLGSMLVAAAAVGVEEILLLGHAGKLIKLAGGI 252
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 740821371  509 LDTHSKKVVMNKEFLKQVAMEAGC----------SPDVESMIERL 543
Cdd:TIGR00312 253 FHTHSHLADGRLEILAAQAVLAGLpyplvqeigqAPTTEEGIKLL 297
PRK08057 PRK08057
cobalt-precorrin-6x reductase; Reviewed
1-226 4.09e-35

cobalt-precorrin-6x reductase; Reviewed


Pssm-ID: 236144  Cd Length: 248  Bit Score: 132.64  E-value: 4.09e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371   1 MILILGGTTEGRTAVKVADEAGKPYFYSTKGEW---QEIQCKhgIRITGGMNTEKMESFCRQNDIRLLVDAAHPFASQLH 77
Cdd:PRK08057   4 RILLLGGTSEARALARALAAAGVDIVLSLAGRTggpADLPGP--VRVGGFGGAEGLAAYLREEGIDLVIDATHPYAAQIS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371  78 RTVDETSRTLHLPVIRFERkyPPRTE----NIIWCEDYTDAIYRLekAGTDHLLALTGVQTIGKLRPYWEKHTCWFRVLE 153
Cdd:PRK08057  82 ANAAAACRALGIPYLRLER--PSWLPqpgdRWIEVDDIEEAAEAL--APFRRVLLTTGRQPLAHFAAILPEHRLLVRVLP 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740821371 154 RETSITlaqeqGFPKENLV-----FyhAGESEALLLETLHPQAILTKESGESgGFSEKVKAAQAAKIPVFAIKRPSLP 226
Cdd:PRK08057 158 PPEVLL-----GLPRAEIIalrgpF--SLELERALLRQHRIDVVVTKNSGGA-GTEAKLEAARELGIPVVMIARPALP 227
precor6x_red TIGR00715
precorrin-6x reductase; This enzyme catalyzes a step in cobalamin biosynthesis. It has been ...
2-226 1.56e-26

precorrin-6x reductase; This enzyme catalyzes a step in cobalamin biosynthesis. It has been identified experimentally in Pseudomonas denitrificans and has been shown to be part of cobalamin biosynthetic operons in several other species. This enzyme was found to be a monomer by gel filtration. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273231  Cd Length: 256  Bit Score: 108.78  E-value: 1.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371    2 ILILGGTTEGRTAVKVADEAGKPYFYSTKGEW-QEIQCKHGIR--ITGGMNTEKMESFCRQNDIRLLVDAAHPFASQLHR 78
Cdd:TIGR00715   3 VLLMGGTVDSRAIAKGLIAQGIEILVTVTTSEgKHLYPIHQALtvHTGALDPQELREFLKRHSIDILVDATHPFAAQITT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371   79 TVDETSRTLHLPVIRFERKYPPRTENIIWCEDYTDAIyRLEKAGTDH---LLALTGVQTIGKLRPYWEKHTCWFRVLERE 155
Cdd:TIGR00715  83 NATAVCKELGIPYVRFERPPLALGKNIIEVPDIEEAT-RVAYQPYLRgkrVFLTAGASWLSHFSLSQDEAVVFVRVLPYP 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740821371  156 TSITLAQEQGFPKENLVFYH---AGESEALLLETLHPQAILTKESGESGGFSEKVKAAQAAKIPVFAIKRPSLP 226
Cdd:TIGR00715 162 QALAQALKLGFPSDRIIAMRgpfSEELEKALLREYRIDAVVTKASGEQGGELEKVKAAEALGINVIRIARPQTI 235
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
148-222 1.42e-03

D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ribose binding protein (ttRBP); Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group are belonging to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability.


Pssm-ID: 380622 [Multi-domain]  Cd Length: 272  Bit Score: 40.77  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371 148 WFRVLErETSITLAQEQGFpkENLVFYHAGES--EALLLETL---HPQAILTKESGESGGFSEkVKAAQAAKIPVFAIKR 222
Cdd:cd19967   13 FFVVEA-EGAKEKAKELGY--EVTVFDHQNDTakEAELFDTAiasGAKAIILDPADADASIAA-VKKAKDAGIPVFLIDR 88
 
Name Accession Description Interval E-value
CbiD COG1903
Cobalamin biosynthesis protein CbiD (cobalt-precorrin-5B C-methyltransferase) [Coenzyme ...
273-593 2.93e-141

Cobalamin biosynthesis protein CbiD (cobalt-precorrin-5B C-methyltransferase) [Coenzyme transport and metabolism]; Cobalamin biosynthesis protein CbiD (cobalt-precorrin-5B C-methyltransferase) is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441507 [Multi-domain]  Cd Length: 368  Bit Score: 414.12  E-value: 2.93e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371 273 LILGEEQKMISFRLPDDEEMTLPVSHTEIEKNSATCTVVKDAGDDPDVTHGASIVVTVSFSNHPDIRFLQGEGVGRVTLP 352
Cdd:COG1903   34 LLTGEFPDEVEITLPKGIRLTFPVEDVEIDGGSASAAVIKDAGDDPDVTHGALIFARVRLTPGPGIVIDGGEGVGTVTKP 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371 353 GLGLEIGEPAINRIPRQMIMKEL-----SALYDKGLDITISVPGGKELAQRTFNPKLGIVDGISIIGTSGIVRPFSSEAF 427
Cdd:COG1903  114 GLPLPVGEPAINPVPRRMIEEAVrevlaELGYGGGVEVTISVPEGEELAKKTLNPRLGIVGGISILGTTGIVRPMSEEAW 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371 428 VEAIRREVEVCVAVGSSRLIINSGAKSERFVKKEYpGLPAQAFVHYGNFIGETLKIAAKLKVPLVTLGIMIGKAVKLAEG 507
Cdd:COG1903  194 KASIRQEIDVARANGLDHVVLTTGNRGEKFARELL-GLPEEAFVQMGNFVGYMLKEAVRHGFKKVLLVGHIGKLVKLAAG 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371 508 NLDTHSKKVVMNKEFLKQVAMEAGCSPDVESMIERLTLARELWTLLSEEDCGKFFPCLLEHCFAHCVPLLPEG-KLTILL 586
Cdd:COG1903  273 IFNTHSRVADVRLEILAALAALAGAPPELVEAILAANTAEEALELLEEAGLDAVFDLIAERAAERARERLGGDiEVEVVL 352

                 ....*..
gi 740821371 587 IDEEGNI 593
Cdd:COG1903  353 FDRDGGI 359
CbiD pfam01888
CbiD; CbiD is essential for cobalamin biosynthesis in both S. typhimurium and B. megaterium, ...
273-507 8.41e-116

CbiD; CbiD is essential for cobalamin biosynthesis in both S. typhimurium and B. megaterium, no functional role has been ascribed to the protein. The CbiD protein has a putative S-AdoMet binding site. It is possible that CbiD might have the same role as CobF in undertaking the C-1 methylation and deacylation reactions required during the ring contraction process.


Pssm-ID: 460373  Cd Length: 258  Bit Score: 344.76  E-value: 8.41e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371  273 LILGEEQKMISFRLPDDEEMTLPVSHTE-IEKNSATCTVVKDAGDDPDVTHGASIVVTVSFSNhPDIRFLQGEGVGRVTL 351
Cdd:pfam01888  22 LLTGEKPDEVEITLPKGERLEIPIEQVArLGEGAALAAVIKDAGDDPDVTHGAEIWARVRLLP-GGIVIDGGEGVGRVTK 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371  352 PGLGLEIGEPAINRIPRQMIMKELSAL---YDKGLDITISVPGGKELAQRTFNPKLGIVDGISIIGTSGIVRPFSSEAFV 428
Cdd:pfam01888 101 PGLPVPVGEPAINPVPRRMIEENVREVlpeYGEGVEVTISVPEGEELAKKTFNPRLGIVGGISILGTTGIVEPMSEEAYK 180
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740821371  429 EAIRREVEVCVAVGSSRLIINSGAKSERFVKKEYpGLPAQAFVHYGNFIGETLKIAAKLKVPLVTLGIMIGKAVKLAEG 507
Cdd:pfam01888 181 ASIRQELDVARANGLDTLVLTPGNYGEDFARELL-GLPEEAIVKMGNFIGFMLDEAAELGVKRILLVGHIGKLVKLAGG 258
cbiD PRK00075
cobalt-precorrin-6A synthase; Reviewed
273-593 4.37e-102

cobalt-precorrin-6A synthase; Reviewed


Pssm-ID: 234615  Cd Length: 361  Bit Score: 313.68  E-value: 4.37e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371 273 LILGEEQKMISFRLPDDEEMTLPVSHTEIEKNSATCTVVKDAGDDPDVTHGASIVVTVSFSNHPDIRFLQGEGVGRVTLP 352
Cdd:PRK00075  30 LLTGEFPDTVEIDLPKGLRLEIPVESVELDGEQALAIVRKDAGDDPDVTHGAEIWARVRLNDSPGIVIRGGEGVGTVTRP 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371 353 GLGLEIGEPAINRIPRQMIMKEL-SALYDKGLDITISVPGGKELAQRTFNPKLGIVDGISIIGTSGIVRPFSSEAFVEAI 431
Cdd:PRK00075 110 GLGVPVGEPAINPVPRRMIEENVrEVLPEGGAEVTISVPEGEELAKKTLNPRLGIVGGISILGTTGIVEPMSEEAYLASI 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371 432 RREVEVCVAVGSSRLIINSGAKSERFVKKeYPGLPAQAFVHYGNFIGETLKIAAKLKVPLVTLGIMIGKAVKLAEGNLDT 511
Cdd:PRK00075 190 KQELDVARANGLDHVVLVTGNNGEDYARK-LLGLPEDAIIKMGNFVGPMLKAAARLGVKKVLLVGHPGKLIKLAAGIFHT 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371 512 HSKKVVMNKEFLKQVAMEAGCSPDVESMIERLTLARELWTLLSEEDCGKFFPCLLEHCFAHCVPLLPEG-KLTILLIDEE 590
Cdd:PRK00075 269 HSHVADARLEILAALAALAGAPLELLEKILAANTTEEALELLEEAGGEKLYDRIAERILERAREYVGGSiEVGVVLFDRD 348

                 ...
gi 740821371 591 GNI 593
Cdd:PRK00075 349 GQI 351
CobK COG2099
Precorrin-6x reductase [Coenzyme transport and metabolism]; Precorrin-6x reductase is part of ...
1-226 2.10e-58

Precorrin-6x reductase [Coenzyme transport and metabolism]; Precorrin-6x reductase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441702  Cd Length: 251  Bit Score: 195.76  E-value: 2.10e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371   1 MILILGGTTEGRTAVKVADEAGKPYFYSTKGEW-QEIQCKHGIRI-TGGMNTEKMESFCRQNDIRLLVDAAHPFASQLHR 78
Cdd:COG2099    3 MILILGGTTEARALAEALAAAGIPVIVSLATRTgAPLLPEPGGPVrVGGFGAEGLAAYLREEGIDAVIDATHPFAAQISR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371  79 TVDETSRTLHLPVIRFERKY--PPRTENIIWCEDYTDAIYRLEKAGtDHLLALTGVQTIGKLRPYWEKHTCWFRVLERET 156
Cdd:COG2099   83 NAAAACAELGIPYLRLERPAwqAPPGDLWIEVDDLEEAAAALPELG-GRVFLTTGSKELAAFAALPPQHRLLARVLPPPE 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740821371 157 SITLAQEQGFPKENLV-----FYHAGESEalLLETLHPQAILTKESGESGGFSEKVKAAQAAKIPVFAIKRPSLP 226
Cdd:COG2099  162 VLEKCEALGLPPKNIIamrgpFSLELERA--LLRQYGIDVLVTKNSGGAGGTDAKLEAARELGIPVIMIRRPPLP 234
CbiJ pfam02571
Precorrin-6x reductase CbiJ/CobK; This family consists of Precorrin-6x reductase EC:1.3.1.54. ...
2-226 2.16e-57

Precorrin-6x reductase CbiJ/CobK; This family consists of Precorrin-6x reductase EC:1.3.1.54. This enzyme catalyzes the reaction: precorrin-6Y + NADP(+) <=> precorrin-6X + NADPH. CbiJ and CobK both catalyze the reduction of macocycle in the colbalmin biosynthesis pathway.


Pssm-ID: 460596  Cd Length: 248  Bit Score: 193.06  E-value: 2.16e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371    2 ILILGGTTEGRTAVKVADEAGKPYFYSTKGEWQE--IQCKHGIRITGGMNTEKMESFCRQNDIRLLVDAAHPFASQLHRT 79
Cdd:pfam02571   2 ILLLGGTSEARELAEALAEAGIPVIVSVATRYGAplLPEAGGEVRVGGFGAEGLAALLREEGIDAVVDATHPFAAEISAN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371   80 VDETSRTLHLPVIRFERKY--PPRTENIIWCEDYTDAIYRLEKAGtDHLLALTGVQTIGKLRPYWEKHTCWFRVLERETS 157
Cdd:pfam02571  82 AAAACAELGIPYLRLERPSweAQPGDRWIEVDSYEEAAEALAELG-GRVLLTTGSKELAAFAPLLPGHRLLARVLPPPEV 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740821371  158 ITLAQEQGFPKENLV-----FYHAGESEalLLETLHPQAILTKESGESGGFSEKVKAAQAAKIPVFAIKRPSLP 226
Cdd:pfam02571 161 LEKCLPLGFPPKNIIamrgpFSLELERA--LLRQYGIDVLVTKDSGGAGGTDEKLEAARELGIPVIVIRRPPLP 232
cbiD TIGR00312
cobalamin biosynthesis protein CbiD; This protein has been shown by cloning into E. coli to be ...
273-543 1.82e-48

cobalamin biosynthesis protein CbiD; This protein has been shown by cloning into E. coli to be required for cobalamin biosynthesis. role_id [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273008  Cd Length: 347  Bit Score: 172.37  E-value: 1.82e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371  273 LILGEEQKMISFRLPDDEEMTLPVSHTE-IEKNSATCTVVKDAGDDPDVTHGASIVVTVSFSN-HPDIRFLQGEGVGRVT 350
Cdd:TIGR00312  14 LTKGCPDSVVLELLEPGRTLEIAIEQGElLGGHRALAIVIKEPGNDLDLTRHTEIIAEVEFTPgEGKLIIQGGEGVGIVT 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371  351 LPGLGLEIGEPAINRIPRQMIMKELSALY--DKGLDITISVPGGKELAQRTFNPKLGIVDGISIIGTSGIVRPFSSEAFV 428
Cdd:TIGR00312  94 KPGLQVREGEAAINPYPRRMIRHNLQPYLsdDETLMVTLSLPLGRTLATRTSNPALGIVGGLSILGTTGIARPMSAEAYL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371  429 EAIRREVEVCVAVGSSRLIINSGAKSERFVkKEYPGLPAQAFVHYGNFIGETLKIAAKLKVPLVTLGIMIGKAVKLAEGN 508
Cdd:TIGR00312 174 ASLACQIDTAAAQGHQCLVFVPGNIGLDLA-RQWGVPLDDEIIKTANFLGSMLVAAAAVGVEEILLLGHAGKLIKLAGGI 252
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 740821371  509 LDTHSKKVVMNKEFLKQVAMEAGC----------SPDVESMIERL 543
Cdd:TIGR00312 253 FHTHSHLADGRLEILAAQAVLAGLpyplvqeigqAPTTEEGIKLL 297
PRK08057 PRK08057
cobalt-precorrin-6x reductase; Reviewed
1-226 4.09e-35

cobalt-precorrin-6x reductase; Reviewed


Pssm-ID: 236144  Cd Length: 248  Bit Score: 132.64  E-value: 4.09e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371   1 MILILGGTTEGRTAVKVADEAGKPYFYSTKGEW---QEIQCKhgIRITGGMNTEKMESFCRQNDIRLLVDAAHPFASQLH 77
Cdd:PRK08057   4 RILLLGGTSEARALARALAAAGVDIVLSLAGRTggpADLPGP--VRVGGFGGAEGLAAYLREEGIDLVIDATHPYAAQIS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371  78 RTVDETSRTLHLPVIRFERkyPPRTE----NIIWCEDYTDAIYRLekAGTDHLLALTGVQTIGKLRPYWEKHTCWFRVLE 153
Cdd:PRK08057  82 ANAAAACRALGIPYLRLER--PSWLPqpgdRWIEVDDIEEAAEAL--APFRRVLLTTGRQPLAHFAAILPEHRLLVRVLP 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740821371 154 RETSITlaqeqGFPKENLV-----FyhAGESEALLLETLHPQAILTKESGESgGFSEKVKAAQAAKIPVFAIKRPSLP 226
Cdd:PRK08057 158 PPEVLL-----GLPRAEIIalrgpF--SLELERALLRQHRIDVVVTKNSGGA-GTEAKLEAARELGIPVVMIARPALP 227
precor6x_red TIGR00715
precorrin-6x reductase; This enzyme catalyzes a step in cobalamin biosynthesis. It has been ...
2-226 1.56e-26

precorrin-6x reductase; This enzyme catalyzes a step in cobalamin biosynthesis. It has been identified experimentally in Pseudomonas denitrificans and has been shown to be part of cobalamin biosynthetic operons in several other species. This enzyme was found to be a monomer by gel filtration. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273231  Cd Length: 256  Bit Score: 108.78  E-value: 1.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371    2 ILILGGTTEGRTAVKVADEAGKPYFYSTKGEW-QEIQCKHGIR--ITGGMNTEKMESFCRQNDIRLLVDAAHPFASQLHR 78
Cdd:TIGR00715   3 VLLMGGTVDSRAIAKGLIAQGIEILVTVTTSEgKHLYPIHQALtvHTGALDPQELREFLKRHSIDILVDATHPFAAQITT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371   79 TVDETSRTLHLPVIRFERKYPPRTENIIWCEDYTDAIyRLEKAGTDH---LLALTGVQTIGKLRPYWEKHTCWFRVLERE 155
Cdd:TIGR00715  83 NATAVCKELGIPYVRFERPPLALGKNIIEVPDIEEAT-RVAYQPYLRgkrVFLTAGASWLSHFSLSQDEAVVFVRVLPYP 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740821371  156 TSITLAQEQGFPKENLVFYH---AGESEALLLETLHPQAILTKESGESGGFSEKVKAAQAAKIPVFAIKRPSLP 226
Cdd:TIGR00715 162 QALAQALKLGFPSDRIIAMRgpfSEELEKALLREYRIDAVVTKASGEQGGELEKVKAAEALGINVIRIARPQTI 235
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
148-222 1.42e-03

D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ribose binding protein (ttRBP); Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group are belonging to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability.


Pssm-ID: 380622 [Multi-domain]  Cd Length: 272  Bit Score: 40.77  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740821371 148 WFRVLErETSITLAQEQGFpkENLVFYHAGES--EALLLETL---HPQAILTKESGESGGFSEkVKAAQAAKIPVFAIKR 222
Cdd:cd19967   13 FFVVEA-EGAKEKAKELGY--EVTVFDHQNDTakEAELFDTAiasGAKAIILDPADADASIAA-VKKAKDAGIPVFLIDR 88
 
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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