NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|19115871|ref|NP_594959|]
View 

siroheme synthase [Schizosaccharomyces pombe]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
CysG2 COG1648
Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and ...
14-197 4.03e-53

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: 171.49  E-value: 4.03e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115871  14 LIIAWRAQGKKVLIVGGGVVAAGRILHVLNADAHVIVVSPKagLCKEVAWRIQEKQVEWRDRGFLVEDLsDDVNMVLTAI 93
Cdd:COG1648   4 FPIFLDLEGRRVLVVGGGEVAARKARLLLKAGARVTVVAPE--FSPELAALAEEGRIELIKRAFEPEDL-DGAFLVIAAT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115871  94 DDPSLSSEIYKLCKSKKIPVNAADIPPECDFYFGSEIRNGPLQIMVSTNGKGPKLASLIRKKIESSINPATGMALEKTGL 173
Cdd:COG1648  81 DDEEVNARVAAAARARGILVNVVDDPELCDFIVPAIVDRGPLVIAISTGGASPVLARRLRERLEALLPPEYGDLAELLGR 160
                       170       180
                ....*....|....*....|....
gi 19115871 174 LRQKLRDIVPEPENSRKRMRWMIE 197
Cdd:COG1648 161 LRERVKARLPDGAERRRFWERLLD 184
 
Name Accession Description Interval E-value
CysG2 COG1648
Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and ...
14-197 4.03e-53

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: 171.49  E-value: 4.03e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115871  14 LIIAWRAQGKKVLIVGGGVVAAGRILHVLNADAHVIVVSPKagLCKEVAWRIQEKQVEWRDRGFLVEDLsDDVNMVLTAI 93
Cdd:COG1648   4 FPIFLDLEGRRVLVVGGGEVAARKARLLLKAGARVTVVAPE--FSPELAALAEEGRIELIKRAFEPEDL-DGAFLVIAAT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115871  94 DDPSLSSEIYKLCKSKKIPVNAADIPPECDFYFGSEIRNGPLQIMVSTNGKGPKLASLIRKKIESSINPATGMALEKTGL 173
Cdd:COG1648  81 DDEEVNARVAAAARARGILVNVVDDPELCDFIVPAIVDRGPLVIAISTGGASPVLARRLRERLEALLPPEYGDLAELLGR 160
                       170       180
                ....*....|....*....|....
gi 19115871 174 LRQKLRDIVPEPENSRKRMRWMIE 197
Cdd:COG1648 161 LRERVKARLPDGAERRRFWERLLD 184
NAD_binding_7 pfam13241
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
16-128 1.15e-41

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


Pssm-ID: 433055 [Multi-domain]  Cd Length: 104  Bit Score: 138.38  E-value: 1.15e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115871    16 IAWRAQGKKVLIVGGGVVAAGRILHVLNADAHVIVVSPKAglckevaWRIQEKQVEWRDRGFLvEDLsDDVNMVLTAIDD 95
Cdd:pfam13241   1 LFLDLRGKRVLVVGGGEVAARKARKLLEAGAKVTVVSPEI-------TPFLEGLLDLIRREFE-GDL-DGADLVIAATDD 71
                          90       100       110
                  ....*....|....*....|....*....|...
gi 19115871    96 PSLSSEIYKLCKSKKIPVNAADIPPECDFYFGS 128
Cdd:pfam13241  72 PELNERIAALARARGILVNVADDPELCDFYFPA 104
cysG_Nterm TIGR01470
siroheme synthase, N-terminal domain; This model represents a subfamily of CysG N-terminal ...
16-191 1.37e-31

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: 115.58  E-value: 1.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115871    16 IAWRAQGKKVLIVGGGVVAAGRILHVLNADAHVIVVSPKagLCKEVAWRIQEKQVEWRDRGFLVEDLsDDVNMVLTAIDD 95
Cdd:TIGR01470   3 VFANLEGRAVLVVGGGDVALRKARLLLKAGAQLRVIAEE--LESELTLLAEQGGITWLARCFDADIL-EGAFLVIAATDD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115871    96 PSLSSEIYKLCKSKKIPVNAADIPPECDFYFGSEIRNGPLQIMVSTNGKGPKLASLIRKKIESSINPATGMALEKTGLLR 175
Cdd:TIGR01470  80 EELNRRVAHAARARGVPVNVVDDPELCSFIFPSIVDRSPVVVAISSGGAAPVLARLLRERIETLLPPSLGDLATLAATWR 159
                         170
                  ....*....|....*.
gi 19115871   176 QKLRDIVPePENSRKR 191
Cdd:TIGR01470 160 DAVKKRLP-NGAARRR 174
PRK06718 PRK06718
NAD(P)-binding protein;
19-185 5.04e-23

NAD(P)-binding protein;


Pssm-ID: 180667 [Multi-domain]  Cd Length: 202  Bit Score: 93.17  E-value: 5.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115871   19 RAQGKKVLIVGGGVVAAGRILHVLNADAHVIVVSPKagLCKEVAWRIQEKQVEWRDRGFLVEDLSdDVNMVLTAIDDPSL 98
Cdd:PRK06718   7 DLSNKRVVIVGGGKVAGRRAITLLKYGAHIVVISPE--LTENLVKLVEEGKIRWKQKEFEPSDIV-DAFLVIAATNDPRV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115871   99 SSEIYKLcKSKKIPVNAADIPPECDFYFGSEIRNGPLQIMVSTNGKGPKLASLIRKKIESSINPATGMALEKTGLLRQKL 178
Cdd:PRK06718  84 NEQVKED-LPENALFNVITDAESGNVVFPSALHRGKLTISVSTDGASPKLAKKIRDELEALYDESYESYIDFLYECRQKI 162

                 ....*..
gi 19115871  179 RDIVPEP 185
Cdd:PRK06718 163 KELQIEK 169
 
Name Accession Description Interval E-value
CysG2 COG1648
Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and ...
14-197 4.03e-53

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: 171.49  E-value: 4.03e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115871  14 LIIAWRAQGKKVLIVGGGVVAAGRILHVLNADAHVIVVSPKagLCKEVAWRIQEKQVEWRDRGFLVEDLsDDVNMVLTAI 93
Cdd:COG1648   4 FPIFLDLEGRRVLVVGGGEVAARKARLLLKAGARVTVVAPE--FSPELAALAEEGRIELIKRAFEPEDL-DGAFLVIAAT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115871  94 DDPSLSSEIYKLCKSKKIPVNAADIPPECDFYFGSEIRNGPLQIMVSTNGKGPKLASLIRKKIESSINPATGMALEKTGL 173
Cdd:COG1648  81 DDEEVNARVAAAARARGILVNVVDDPELCDFIVPAIVDRGPLVIAISTGGASPVLARRLRERLEALLPPEYGDLAELLGR 160
                       170       180
                ....*....|....*....|....
gi 19115871 174 LRQKLRDIVPEPENSRKRMRWMIE 197
Cdd:COG1648 161 LRERVKARLPDGAERRRFWERLLD 184
NAD_binding_7 pfam13241
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
16-128 1.15e-41

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


Pssm-ID: 433055 [Multi-domain]  Cd Length: 104  Bit Score: 138.38  E-value: 1.15e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115871    16 IAWRAQGKKVLIVGGGVVAAGRILHVLNADAHVIVVSPKAglckevaWRIQEKQVEWRDRGFLvEDLsDDVNMVLTAIDD 95
Cdd:pfam13241   1 LFLDLRGKRVLVVGGGEVAARKARKLLEAGAKVTVVSPEI-------TPFLEGLLDLIRREFE-GDL-DGADLVIAATDD 71
                          90       100       110
                  ....*....|....*....|....*....|...
gi 19115871    96 PSLSSEIYKLCKSKKIPVNAADIPPECDFYFGS 128
Cdd:pfam13241  72 PELNERIAALARARGILVNVADDPELCDFYFPA 104
cysG_Nterm TIGR01470
siroheme synthase, N-terminal domain; This model represents a subfamily of CysG N-terminal ...
16-191 1.37e-31

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: 115.58  E-value: 1.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115871    16 IAWRAQGKKVLIVGGGVVAAGRILHVLNADAHVIVVSPKagLCKEVAWRIQEKQVEWRDRGFLVEDLsDDVNMVLTAIDD 95
Cdd:TIGR01470   3 VFANLEGRAVLVVGGGDVALRKARLLLKAGAQLRVIAEE--LESELTLLAEQGGITWLARCFDADIL-EGAFLVIAATDD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115871    96 PSLSSEIYKLCKSKKIPVNAADIPPECDFYFGSEIRNGPLQIMVSTNGKGPKLASLIRKKIESSINPATGMALEKTGLLR 175
Cdd:TIGR01470  80 EELNRRVAHAARARGVPVNVVDDPELCSFIFPSIVDRSPVVVAISSGGAAPVLARLLRERIETLLPPSLGDLATLAATWR 159
                         170
                  ....*....|....*.
gi 19115871   176 QKLRDIVPePENSRKR 191
Cdd:TIGR01470 160 DAVKKRLP-NGAARRR 174
PRK06718 PRK06718
NAD(P)-binding protein;
19-185 5.04e-23

NAD(P)-binding protein;


Pssm-ID: 180667 [Multi-domain]  Cd Length: 202  Bit Score: 93.17  E-value: 5.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115871   19 RAQGKKVLIVGGGVVAAGRILHVLNADAHVIVVSPKagLCKEVAWRIQEKQVEWRDRGFLVEDLSdDVNMVLTAIDDPSL 98
Cdd:PRK06718   7 DLSNKRVVIVGGGKVAGRRAITLLKYGAHIVVISPE--LTENLVKLVEEGKIRWKQKEFEPSDIV-DAFLVIAATNDPRV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115871   99 SSEIYKLcKSKKIPVNAADIPPECDFYFGSEIRNGPLQIMVSTNGKGPKLASLIRKKIESSINPATGMALEKTGLLRQKL 178
Cdd:PRK06718  84 NEQVKED-LPENALFNVITDAESGNVVFPSALHRGKLTISVSTDGASPKLAKKIRDELEALYDESYESYIDFLYECRQKI 162

                 ....*..
gi 19115871  179 RDIVPEP 185
Cdd:PRK06718 163 KELQIEK 169
Sirohm_synth_C pfam14823
Sirohaem biosynthesis protein C-terminal; This domain is the C-terminus of a multifunctional ...
164-224 8.64e-23

Sirohaem biosynthesis protein C-terminal; This domain is the C-terminus of a multifunctional enzyme which catalyzes the biosynthesis of sirohaem. Both of the catalytic activities of this enzyme (precorrin-2 dehydrogenase EC:1.3.1.76) and sirohydrochlorin ferrochelatase (EC:4.99.1.4) are located in the N-terminal domain of this enzyme, pfam13241.


Pssm-ID: 434243  Cd Length: 66  Bit Score: 88.38  E-value: 8.64e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115871   164 TGMALEKTGLLRQKLRDIVPEPENSRKRMRWMIEICELWSLEELAMLDENLINRLLGYFPK 224
Cdd:pfam14823   2 LGAAIEKVGELRKKLREVAPGPEEGPKRMKWMSKVCDAWSLEELCELDEEDMENLLEFYEK 62
cysG PRK10637
siroheme synthase CysG;
21-180 8.22e-14

siroheme synthase CysG;


Pssm-ID: 182606 [Multi-domain]  Cd Length: 457  Bit Score: 70.56  E-value: 8.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115871   21 QGKKVLIVGGGVVAAGRILHVLNADAHVIVVspkaglckevAWRIQEKQVEWRDRGFL-------VEDLSDDVNMVLTAI 93
Cdd:PRK10637  11 RDRDCLLVGGGDVAERKARLLLDAGARLTVN----------ALAFIPQFTAWADAGMLtlvegpfDESLLDTCWLAIAAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115871   94 DDPSLSSEIYKLCKSKKIPVNAADIPPECDFYFGSEIRNGPLQIMVSTNGKGPKLASLIRKKIESSINPATGMALEKTGL 173
Cdd:PRK10637  81 DDDAVNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPQHLGQVAKYAGQ 160

                 ....*..
gi 19115871  174 LRQKLRD 180
Cdd:PRK10637 161 LRGRVKQ 167
Sirohm_synth_M pfam14824
Sirohaem biosynthesis protein central; This is the central domain of a multifunctional enzyme ...
135-159 9.68e-10

Sirohaem biosynthesis protein central; This is the central domain of a multifunctional enzyme which catalyzes the biosynthesis of sirohaem. Both of the catalytic activities of this enzyme (precorrin-2 dehydrogenase EC:1.3.1.76) and sirohydrochlorin ferrochelatase (EC:4.99.1.4) are located in the N-terminal domain of this enzyme, pfam13241.


Pssm-ID: 464336 [Multi-domain]  Cd Length: 25  Bit Score: 52.39  E-value: 9.68e-10
                          10        20
                  ....*....|....*....|....*
gi 19115871   135 LQIMVSTNGKGPKLASLIRKKIESS 159
Cdd:pfam14824   1 LQIAISTNGKSPRLAALIRREIERS 25
PRK06719 PRK06719
precorrin-2 dehydrogenase; Validated
21-158 3.07e-08

precorrin-2 dehydrogenase; Validated


Pssm-ID: 180668 [Multi-domain]  Cd Length: 157  Bit Score: 51.89  E-value: 3.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115871   21 QGKKVLIVGGGVVAAGRILHVLNADAHVIVVSPKagLCKEVAwriQEKQVEWRDRGFLVEDLSdDVNMVLTAIDDPSLSS 100
Cdd:PRK06719  12 HNKVVVIIGGGKIAYRKASGLKDTGAFVTVVSPE--ICKEMK---ELPYITWKQKTFSNDDIK-DAHLIYAATNQHAVNM 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 19115871  101 EIYKLCKSKKIpVNAADIPPECDFYFGSEIRNGPLQIMVSTNGKGPKLASLIRKKIES 158
Cdd:PRK06719  86 MVKQAAHDFQW-VNVVSDGTESSFHTPGVIRNDEYVVTISTSGKDPSFTKRLKQELTS 142
PRK05562 PRK05562
NAD(P)-dependent oxidoreductase;
24-181 1.32e-05

NAD(P)-dependent oxidoreductase;


Pssm-ID: 235504  Cd Length: 223  Bit Score: 45.02  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115871   24 KVLIVGGGVVAAGRILHVLNADAHVIVVSPKagLCKEVAWRIQEKQVEWRDRGFLVEDLSDDvNMVLTAIDDPSLSSEIY 103
Cdd:PRK05562  27 KVLIIGGGKAAFIKGKTFLKKGCYVYILSKK--FSKEFLDLKKYGNLKLIKGNYDKEFIKDK-HLIVIATDDEKLNNKIR 103
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19115871  104 KLCKSK-KIPVNAADiPPECDFYFGSEIRNGPLQIMVSTNGKGPKLASLIRKKIESSINPATgMALEKTGLLRQKLRDI 181
Cdd:PRK05562 104 KHCDRLyKLYIDCSD-YKKGLCIIPYQRSTKNFVFALNTKGGSPKTSVFIGEKVKNFLKKYD-DFIEYVTKIRNKAKKN 180
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
21-113 1.81e-03

UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440534 [Multi-domain]  Cd Length: 445  Bit Score: 39.29  E-value: 1.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115871  21 QGKKVLIVGGGV--VAAGRILHVLNADahVIVVSPKAGLcKEVAWRIQEKQVEWRDRGFLVEDLsDDVNMVLTAiddP-- 96
Cdd:COG0771   3 KGKKVLVLGLGKsgLAAARLLAKLGAE--VTVSDDRPAP-ELAAAELEAPGVEVVLGEHPEELL-DGADLVVKS---Pgi 75
                        90
                ....*....|....*..
gi 19115871  97 SLSSEIYKLCKSKKIPV 113
Cdd:COG0771  76 PPDHPLLKAARAAGIPV 92
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH