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Conserved domains on  [gi|1330141305|ref|WP_102329325|]
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bifunctional precorrin-2 dehydrogenase/sirohydrochlorin ferrochelatase [Vibrio breoganii]

Protein Classification

bifunctional precorrin-2 dehydrogenase/sirohydrochlorin ferrochelatase( domain architecture ID 11447222)

bifunctional precorrin-2 dehydrogenase/sirohydrochlorin ferrochelatase catalyzes the dehydrogenation of precorrin-2 to form sirohydrochlorin, a precursor in both siroheme and adenosylcobalamin biosynthesis, as well as the subsequent ferrochelation of sirohydrochlorin to siroheme

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CysG2 COG1648
Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and ...
 1-184 1.82e-81

Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and metabolism]; Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) is part of the Pathway/BioSystem: Heme biosynthesis


:

Pssm-ID: 441254 [Multi-domain]  Cd Length: 211  Bit Score: 245.45  E-value: 1.82e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330141305   1 MRYFPLFYDLYHKPVLVVGGGEVASRKVESLLKAGAFVSVVSPTLEPFLLSLYEEEKLSWIKGFYQQELIEEFVQIWATT 80
Cdd:COG1648     1 MDYFPIFLDLEGRRVLVVGGGEVAARKARLLLKAGARVTVVAPEFSPELAALAEEGRIELIKRAFEPEDLDGAFLVIAAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330141305  81 DNPDLNHRVHADAKRAGIMVNVVDDTEYCDFITPSMINRGRIQVAFSSGGSSPVLIRNLRRTFEAVLPQNLGLLADFAAS 160
Cdd:COG1648    81 DDEEVNARVAAAARARGILVNVVDDPELCDFIVPAIVDRGPLVIAISTGGASPVLARRLRERLEALLPPEYGDLAELLGR 160

                         170       180
                  ....*....|....*....|....
gi 1330141305 161 KRADIKAKLPDVTRRRLFWEYFFE 184
Cdd:COG1648   161 LRERVKARLPDGAERRRFWERLLD 184
TP_methylase super family cl00304
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
 224-263 7.25e-05

S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide.


The actual alignment was detected with superfamily member cd11642:

Pssm-ID: 444820  Cd Length: 228  Bit Score: 43.19  E-value: 7.25e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1330141305 224 DFEMLTLKALRLMQSAEMVLYHHKLDAVFADSCRRDAERI 263
Cdd:cd11642     7 DPDLLTLKALRALQQADVVLYDRLVSPEILALAPPGAELI 46
 
Name Accession Description Interval E-value
CysG2 COG1648
Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and ...
 1-184 1.82e-81

Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and metabolism]; Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 441254 [Multi-domain]  Cd Length: 211  Bit Score: 245.45  E-value: 1.82e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330141305   1 MRYFPLFYDLYHKPVLVVGGGEVASRKVESLLKAGAFVSVVSPTLEPFLLSLYEEEKLSWIKGFYQQELIEEFVQIWATT 80
Cdd:COG1648     1 MDYFPIFLDLEGRRVLVVGGGEVAARKARLLLKAGARVTVVAPEFSPELAALAEEGRIELIKRAFEPEDLDGAFLVIAAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330141305  81 DNPDLNHRVHADAKRAGIMVNVVDDTEYCDFITPSMINRGRIQVAFSSGGSSPVLIRNLRRTFEAVLPQNLGLLADFAAS 160
Cdd:COG1648    81 DDEEVNARVAAAARARGILVNVVDDPELCDFIVPAIVDRGPLVIAISTGGASPVLARRLRERLEALLPPEYGDLAELLGR 160

                         170       180
                  ....*....|....*....|....
gi 1330141305 161 KRADIKAKLPDVTRRRLFWEYFFE 184
Cdd:COG1648   161 LRERVKARLPDGAERRRFWERLLD 184
cysG_Nterm TIGR01470
siroheme synthase, N-terminal domain; This model represents a subfamily of CysG N-terminal ...
 4-184 3.95e-61

siroheme synthase, N-terminal domain; This model represents a subfamily of CysG N-terminal region-related sequences. All sequences in the seed alignment for this model are N-terminal regions of known or predicted siroheme synthases. The C-terminal region of each is uroporphyrin-III C-methyltransferase (EC 2.1.1.107), which catalyzes the first step committed to the biosynthesis of either siroheme or cobalamin (vitamin B12) rather than protoheme (heme). The region represented by this model completes the process of oxidation and iron insertion to yield siroheme. Siroheme is a cofactor for nitrite and sulfite reductases, so siroheme synthase is CysG of cysteine biosynthesis in some organisms. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 130536 [Multi-domain]  Cd Length: 205  Bit Score: 193.39  E-value: 3.95e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330141305   4 FPLFYDLYHKPVLVVGGGEVASRKVESLLKAGAFVSVVSPTLEPFLLSLYEEEKLSWIKGFYQQELIEEFVQIWATTDNP 83
Cdd:TIGR01470   1 LPVFANLEGRAVLVVGGGDVALRKARLLLKAGAQLRVIAEELESELTLLAEQGGITWLARCFDADILEGAFLVIAATDDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330141305  84 DLNHRVHADAKRAGIMVNVVDDTEYCDFITPSMINRGRIQVAFSSGGSSPVLIRNLRRTFEAVLPQNLGLLADFAASKRA 163
Cdd:TIGR01470  81 ELNRRVAHAARARGVPVNVVDDPELCSFIFPSIVDRSPVVVAISSGGAAPVLARLLRERIETLLPPSLGDLATLAATWRD 160

                         170       180
                  ....*....|....*....|.
gi 1330141305 164 DIKAKLPDVTRRRLFWEYFFE 184
Cdd:TIGR01470 161 AVKKRLPNGAARRRFWEKFFD 181
cysG PRK10637
siroheme synthase CysG;
1-263 4.52e-55

siroheme synthase CysG;


Pssm-ID: 182606 [Multi-domain]  Cd Length: 457  Bit Score: 185.35  E-value: 4.52e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330141305   1 MRYFPLFYDLYHKPVLVVGGGEVASRKVESLLKAGAFVSVVSPTLEPFLLSLYEEEKLSWIKGFYQQELIEEFVQIWATT 80
Cdd:PRK10637    1 MDHLPIFCQLRDRDCLLVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTLVEGPFDESLLDTCWLAIAAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330141305  81 DNPDLNHRVHADAKRAGIMVNVVDDTEYCDFITPSMINRGRIQVAFSSGGSSPVLIRNLRRTFEAVLPQNLGLLADFAAS 160
Cdd:PRK10637   81 DDDAVNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPQHLGQVAKYAGQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330141305 161 KRADIKAKLPDVTRRRLFWEYFFEATEVKSSQTKSQLQACYEAT--LDSKQFEPSCSVSWIETG-SDFEMLTLKALRLMQ 237
Cdd:PRK10637  161 LRGRVKQQFATMGERRRFWEKLFVNDRLAQSLANNDQKAVTETTeqLFSEPLDHRGEVVLVGAGpGDAGLLTLKGLQQIQ 240

                         250       260
                  ....*....|....*....|....*.
gi 1330141305 238 SAEMVLYHHKLDAVFADSCRRDAERI 263
Cdd:PRK10637  241 QADVVVYDRLVSDDIMNLVRRDADRV 266
NAD_binding_7 pfam13241
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
 6-115 6.35e-37

Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.


Pssm-ID: 433055 [Multi-domain]  Cd Length: 104  Bit Score: 127.59  E-value: 6.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330141305   6 LFYDLYHKPVLVVGGGEVASRKVESLLKAGAFVSVVSPTLEPFLlslyeEEKLSWIKGFYQqELIEEFVQIWATTDNPDL 85
Cdd:pfam13241   1 LFLDLRGKRVLVVGGGEVAARKARKLLEAGAKVTVVSPEITPFL-----EGLLDLIRREFE-GDLDGADLVIAATDDPEL 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 1330141305  86 NHRVHADAKRAGIMVNVVDDTEYCDFITPS 115
Cdd:pfam13241  75 NERIAALARARGILVNVADDPELCDFYFPA 104
SUMT cd11642
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ...
 224-263 7.25e-05

Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen III methyltransferase, SUMT); SUMT is an enzyme of the cobalamin and siroheme biosynthetic pathway. It catalyzes the first of three steps leading to the formation of siroheme from uroporphyrinogen III; it transfers two methyl groups from S-adenosyl-L-methionine to the C-2 and C-7 atoms of uroporphyrinogen III to yield precorrin-2 via the intermediate formation of precorrin-1. Precorrin-2 is also a precursor for the biosynthesis of vitamin B12, coenzyme F430, siroheme and heme d1. This family includes proteins in which the SUMT domain is fused to other functional domains, such as to a uroporphyrinogen-III synthase domain to form bifunctional uroporphyrinogen-III methylase/uroporphyrinogen-III synthase, or to a dual function dehydrogenase-chelatase domain, as in the case of the multifunctional S-adenosyl-L-methionine (SAM)-dependent bismethyltransferase/dehydrogenase/ferrochelatase CysG, which catalyzes all three steps that transform uroporphyrinogen III into siroheme.


Pssm-ID: 381169  Cd Length: 228  Bit Score: 43.19  E-value: 7.25e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1330141305 224 DFEMLTLKALRLMQSAEMVLYHHKLDAVFADSCRRDAERI 263
Cdd:cd11642     7 DPDLLTLKALRALQQADVVLYDRLVSPEILALAPPGAELI 46
CysG COG0007
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ...
 224-263 1.27e-04

Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; Uroporphyrinogen-III methylase (siroheme synthase) is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 439778 [Multi-domain]  Cd Length: 245  Bit Score: 42.75  E-value: 1.27e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1330141305 224 DFEMLTLKALRLMQSAEMVLYHHKLDAVFADSCRRDAERI 263
Cdd:COG0007    13 DPDLLTLKALRALQQADVVLYDRLVSPEILALARPDAELI 52
 
Name Accession Description Interval E-value
CysG2 COG1648
Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and ...
 1-184 1.82e-81

Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and metabolism]; Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 441254 [Multi-domain]  Cd Length: 211  Bit Score: 245.45  E-value: 1.82e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330141305   1 MRYFPLFYDLYHKPVLVVGGGEVASRKVESLLKAGAFVSVVSPTLEPFLLSLYEEEKLSWIKGFYQQELIEEFVQIWATT 80
Cdd:COG1648     1 MDYFPIFLDLEGRRVLVVGGGEVAARKARLLLKAGARVTVVAPEFSPELAALAEEGRIELIKRAFEPEDLDGAFLVIAAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330141305  81 DNPDLNHRVHADAKRAGIMVNVVDDTEYCDFITPSMINRGRIQVAFSSGGSSPVLIRNLRRTFEAVLPQNLGLLADFAAS 160
Cdd:COG1648    81 DDEEVNARVAAAARARGILVNVVDDPELCDFIVPAIVDRGPLVIAISTGGASPVLARRLRERLEALLPPEYGDLAELLGR 160

                         170       180
                  ....*....|....*....|....
gi 1330141305 161 KRADIKAKLPDVTRRRLFWEYFFE 184
Cdd:COG1648   161 LRERVKARLPDGAERRRFWERLLD 184
cysG_Nterm TIGR01470
siroheme synthase, N-terminal domain; This model represents a subfamily of CysG N-terminal ...
 4-184 3.95e-61

siroheme synthase, N-terminal domain; This model represents a subfamily of CysG N-terminal region-related sequences. All sequences in the seed alignment for this model are N-terminal regions of known or predicted siroheme synthases. The C-terminal region of each is uroporphyrin-III C-methyltransferase (EC 2.1.1.107), which catalyzes the first step committed to the biosynthesis of either siroheme or cobalamin (vitamin B12) rather than protoheme (heme). The region represented by this model completes the process of oxidation and iron insertion to yield siroheme. Siroheme is a cofactor for nitrite and sulfite reductases, so siroheme synthase is CysG of cysteine biosynthesis in some organisms. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 130536 [Multi-domain]  Cd Length: 205  Bit Score: 193.39  E-value: 3.95e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330141305   4 FPLFYDLYHKPVLVVGGGEVASRKVESLLKAGAFVSVVSPTLEPFLLSLYEEEKLSWIKGFYQQELIEEFVQIWATTDNP 83
Cdd:TIGR01470   1 LPVFANLEGRAVLVVGGGDVALRKARLLLKAGAQLRVIAEELESELTLLAEQGGITWLARCFDADILEGAFLVIAATDDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330141305  84 DLNHRVHADAKRAGIMVNVVDDTEYCDFITPSMINRGRIQVAFSSGGSSPVLIRNLRRTFEAVLPQNLGLLADFAASKRA 163
Cdd:TIGR01470  81 ELNRRVAHAARARGVPVNVVDDPELCSFIFPSIVDRSPVVVAISSGGAAPVLARLLRERIETLLPPSLGDLATLAATWRD 160

                         170       180
                  ....*....|....*....|.
gi 1330141305 164 DIKAKLPDVTRRRLFWEYFFE 184
Cdd:TIGR01470 161 AVKKRLPNGAARRRFWEKFFD 181
cysG PRK10637
siroheme synthase CysG;
1-263 4.52e-55

siroheme synthase CysG;


Pssm-ID: 182606 [Multi-domain]  Cd Length: 457  Bit Score: 185.35  E-value: 4.52e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330141305   1 MRYFPLFYDLYHKPVLVVGGGEVASRKVESLLKAGAFVSVVSPTLEPFLLSLYEEEKLSWIKGFYQQELIEEFVQIWATT 80
Cdd:PRK10637    1 MDHLPIFCQLRDRDCLLVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTLVEGPFDESLLDTCWLAIAAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330141305  81 DNPDLNHRVHADAKRAGIMVNVVDDTEYCDFITPSMINRGRIQVAFSSGGSSPVLIRNLRRTFEAVLPQNLGLLADFAAS 160
Cdd:PRK10637   81 DDDAVNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPQHLGQVAKYAGQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330141305 161 KRADIKAKLPDVTRRRLFWEYFFEATEVKSSQTKSQLQACYEAT--LDSKQFEPSCSVSWIETG-SDFEMLTLKALRLMQ 237
Cdd:PRK10637  161 LRGRVKQQFATMGERRRFWEKLFVNDRLAQSLANNDQKAVTETTeqLFSEPLDHRGEVVLVGAGpGDAGLLTLKGLQQIQ 240

                         250       260
                  ....*....|....*....|....*.
gi 1330141305 238 SAEMVLYHHKLDAVFADSCRRDAERI 263
Cdd:PRK10637  241 QADVVVYDRLVSDDIMNLVRRDADRV 266
NAD_binding_7 pfam13241
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
 6-115 6.35e-37

Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.


Pssm-ID: 433055 [Multi-domain]  Cd Length: 104  Bit Score: 127.59  E-value: 6.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330141305   6 LFYDLYHKPVLVVGGGEVASRKVESLLKAGAFVSVVSPTLEPFLlslyeEEKLSWIKGFYQqELIEEFVQIWATTDNPDL 85
Cdd:pfam13241   1 LFLDLRGKRVLVVGGGEVAARKARKLLEAGAKVTVVSPEITPFL-----EGLLDLIRREFE-GDLDGADLVIAATDDPEL 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 1330141305  86 NHRVHADAKRAGIMVNVVDDTEYCDFITPS 115
Cdd:pfam13241  75 NERIAALARARGILVNVADDPELCDFYFPA 104
PRK06718 PRK06718
NAD(P)-binding protein;
5-167 9.91e-29

NAD(P)-binding protein;


Pssm-ID: 180667 [Multi-domain]  Cd Length: 202  Bit Score: 109.35  E-value: 9.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330141305   5 PLFYDLYHKPVLVVGGGEVASRKVESLLKAGAFVSVVSPTLEPFLLSLYEEEKLSWI-KGFYQQELIEEFVQIwATTDNP 83
Cdd:PRK06718    3 PLMIDLSNKRVVIVGGGKVAGRRAITLLKYGAHIVVISPELTENLVKLVEEGKIRWKqKEFEPSDIVDAFLVI-AATNDP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330141305  84 DLNHRVHADAKRaGIMVNVVDDTEYCDFITPSMINRGRIQVAFSSGGSSPVLIRNLRRTFEAVLPQNLGLLADFAASKRA 163
Cdd:PRK06718   82 RVNEQVKEDLPE-NALFNVITDAESGNVVFPSALHRGKLTISVSTDGASPKLAKKIRDELEALYDESYESYIDFLYECRQ 160


                  ....
gi 1330141305 164 DIKA 167
Cdd:PRK06718  161 KIKE 164
PRK06719 PRK06719
precorrin-2 dehydrogenase; Validated
 4-149 2.42e-19

precorrin-2 dehydrogenase; Validated


Pssm-ID: 180668 [Multi-domain]  Cd Length: 157  Bit Score: 83.09  E-value: 2.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330141305   4 FPLFYDLYHKPVLVVGGGEVASRKVESLLKAGAFVSVVSPTLepfLLSLYEEEKLSWIKGFYQQELIEEFVQIWATTDNP 83
Cdd:PRK06719    5 YPLMFNLHNKVVVIIGGGKIAYRKASGLKDTGAFVTVVSPEI---CKEMKELPYITWKQKTFSNDDIKDAHLIYAATNQH 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1330141305  84 DLNHRVhadaKRAG---IMVNVVDDTEYCDFITPSMINRGRIQVAFSSGGSSPVLIRNLRRTFEAVLPQ 149
Cdd:PRK06719   82 AVNMMV----KQAAhdfQWVNVVSDGTESSFHTPGVIRNDEYVVTISTSGKDPSFTKRLKQELTSILPK 146
CysG_dimerizer pfam10414
Sirohaem synthase dimerization region; Bacterial sulfur metabolism depends on the ...
 152-184 2.17e-08

Sirohaem synthase dimerization region; Bacterial sulfur metabolism depends on the iron-containing porphinoid sirohaem. CysG, S-adenosyl-L-methionine (SAM)-dependent bis-methyltransferase, dehydrogenase and ferrochelatase, synthesizes sirohaem from uroporphyrinogen III via reactions which encompass two branchpoint intermediates in tetrapyrrole biosynthesis, diverting flux first from protoporphyrin IX biosynthesis and then from cobalamin (vitamin B12) biosynthesis. CysG is a dimer of two structurally similar protomers held together asymmetrically through a number of salt-bridges across complementary residues in the CysG_dimerizer region to produce a series of active sites, accounting for CysG's multifunctionality, catalysing four diverse reactions: two SAM-dependent methylations, NAD+-dependent tetrapyrrole dehydrogenation and metal chelation. The CysG_dimerizer region holding the two protomers together is of 74 residues.


Pssm-ID: 431269 [Multi-domain]  Cd Length: 56  Bit Score: 49.86  E-value: 2.17e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1330141305 152 GLLADFAASKRADIKAKLPDVTRRRLFWEYFFE 184
Cdd:pfam10414   1 GRLAALAGRFRDRVKARLPDVAARRRFWERVFD 33
PRK05562 PRK05562
NAD(P)-dependent oxidoreductase;
15-135 5.70e-08

NAD(P)-dependent oxidoreductase;


Pssm-ID: 235504  Cd Length: 223  Bit Score: 52.34  E-value: 5.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330141305  15 VLVVGGGEVASRKVESLLKAGAFVSVVSPTLEPFLLSLYEEEKLSWIKGFYQQELIEEFVQIWATTDNPDLNHRVHADAK 94
Cdd:PRK05562   28 VLIIGGGKAAFIKGKTFLKKGCYVYILSKKFSKEFLDLKKYGNLKLIKGNYDKEFIKDKHLIVIATDDEKLNNKIRKHCD 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1330141305  95 RAGIMVNVVDDTEYCDFITPSMINRGRIQVAFSSGGSSPVL 135
Cdd:PRK05562  108 RLYKLYIDCSDYKKGLCIIPYQRSTKNFVFALNTKGGSPKT 148
SUMT cd11642
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ...
 224-263 7.25e-05

Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen III methyltransferase, SUMT); SUMT is an enzyme of the cobalamin and siroheme biosynthetic pathway. It catalyzes the first of three steps leading to the formation of siroheme from uroporphyrinogen III; it transfers two methyl groups from S-adenosyl-L-methionine to the C-2 and C-7 atoms of uroporphyrinogen III to yield precorrin-2 via the intermediate formation of precorrin-1. Precorrin-2 is also a precursor for the biosynthesis of vitamin B12, coenzyme F430, siroheme and heme d1. This family includes proteins in which the SUMT domain is fused to other functional domains, such as to a uroporphyrinogen-III synthase domain to form bifunctional uroporphyrinogen-III methylase/uroporphyrinogen-III synthase, or to a dual function dehydrogenase-chelatase domain, as in the case of the multifunctional S-adenosyl-L-methionine (SAM)-dependent bismethyltransferase/dehydrogenase/ferrochelatase CysG, which catalyzes all three steps that transform uroporphyrinogen III into siroheme.


Pssm-ID: 381169  Cd Length: 228  Bit Score: 43.19  E-value: 7.25e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1330141305 224 DFEMLTLKALRLMQSAEMVLYHHKLDAVFADSCRRDAERI 263
Cdd:cd11642     7 DPDLLTLKALRALQQADVVLYDRLVSPEILALAPPGAELI 46
CysG COG0007
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ...
 224-263 1.27e-04

Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; Uroporphyrinogen-III methylase (siroheme synthase) is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 439778 [Multi-domain]  Cd Length: 245  Bit Score: 42.75  E-value: 1.27e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1330141305 224 DFEMLTLKALRLMQSAEMVLYHHKLDAVFADSCRRDAERI 263
Cdd:COG0007    13 DPDLLTLKALRALQQADVVLYDRLVSPEILALARPDAELI 52
 
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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