Protein : Qrob_P0161950.2 Q. robur
Protein Identifier  ? Qrob_P0161950.2 Organism . Name  Quercus robur
Score  100.0 Score Type  egn
Protein Description  (M=3) PF01903 - CbiX Gene Prediction Quality  validated
Protein length 

Sequence

Length: 215  
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0 Synonyms

2 GO Terms

Identifier Name Description
GO:0009236 cobalamin biosynthetic process The chemical reactions and pathways resulting in the formation of cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.
GO:0016852 sirohydrochlorin cobaltochelatase activity Catalysis of the reaction: sirohydrochlorin + Co2+ = cobalt-sirohydrochlorin + 2 H+.

30 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|rcu:RCOM_1095630 1 214 + 214 Gaps:8 100.00 210 71.90 3e-101 sirohydrochlorin ferrochelatase putative (EC:4.99.1.3)
blastp_kegg lcl|pxb:103965821 1 214 + 214 Gaps:12 100.00 210 71.90 1e-100 uncharacterized LOC103965821
blastp_kegg lcl|vvi:100244073 3 214 + 212 Gaps:4 100.00 208 70.67 2e-99 sirohydrochlorin ferrochelatase-like
blastp_kegg lcl|tcc:TCM_016940 1 214 + 214 Gaps:4 100.00 210 70.48 2e-98 Sirohydrochlorin ferrochelatase B
blastp_kegg lcl|mdm:103404567 1 214 + 214 Gaps:2 85.83 247 68.40 5e-96 uncharacterized LOC103404567
blastp_kegg lcl|mdm:103421473 1 214 + 214 Gaps:4 100.00 210 67.62 7e-95 uncharacterized LOC103421473
blastp_kegg lcl|cit:102627039 1 214 + 214 Gaps:13 95.71 210 71.64 2e-94 uncharacterized LOC102627039
blastp_kegg lcl|pmum:103329819 1 214 + 214 Gaps:11 100.00 203 69.46 7e-94 uncharacterized LOC103329819
blastp_kegg lcl|pop:POPTR_0001s17900g 1 214 + 214 Gaps:14 100.00 220 66.82 3e-93 POPTRDRAFT_846329 hypothetical protein
blastp_kegg lcl|gmx:100500125 52 214 + 163 none 77.25 211 80.37 2e-90 uncharacterized LOC100500125
blastp_pdb 3lyh_B 101 193 + 93 Gaps:7 77.78 126 33.67 2e-07 mol:protein length:126 Cobalamin (Vitamin B12) biosynthesis CbiX pro
blastp_pdb 3lyh_A 101 193 + 93 Gaps:7 77.78 126 33.67 2e-07 mol:protein length:126 Cobalamin (Vitamin B12) biosynthesis CbiX pro
blastp_uniprot_sprot sp|P61817|SIRB_BACME 64 188 + 125 none 46.99 266 31.20 5e-16 Sirohydrochlorin ferrochelatase OS Bacillus megaterium GN sirB PE 3 SV 1
blastp_uniprot_sprot sp|O34632|SIRB_BACSU 73 189 + 117 none 44.83 261 29.91 5e-13 Sirohydrochlorin ferrochelatase OS Bacillus subtilis (strain 168) GN sirB PE 2 SV 1
blastp_uniprot_sprot sp|Q58380|CBIX_METJA 74 155 + 82 none 57.34 143 41.46 1e-12 Sirohydrochlorin cobaltochelatase OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) GN cbiX PE 3 SV 1
blastp_uniprot_sprot sp|P61819|CBIX_METMP 74 187 + 114 Gaps:25 96.53 144 30.22 2e-12 Sirohydrochlorin cobaltochelatase OS Methanococcus maripaludis (strain S2 / LL) GN cbiX PE 3 SV 1
blastp_uniprot_sprot sp|Q4JAI2|CBIX_SULAC 75 193 + 119 Gaps:9 92.68 123 31.58 4e-12 Sirohydrochlorin cobaltochelatase OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) GN cbiX PE 3 SV 1
blastp_uniprot_sprot sp|O87690|CBIX_BACME 76 204 + 129 Gaps:5 83.01 306 27.17 5e-12 Sirohydrochlorin cobaltochelatase OS Bacillus megaterium GN cbiX PE 1 SV 1
blastp_uniprot_sprot sp|A6UWT5|CBIX_META3 74 189 + 116 Gaps:24 97.90 143 29.29 1e-10 Sirohydrochlorin cobaltochelatase OS Methanococcus aeolicus (strain Nankai-3 / ATCC BAA-1280) GN cbiX PE 3 SV 1
blastp_uniprot_sprot sp|Q975N6|CBIX_SULTO 75 192 + 118 Gaps:6 93.33 120 28.57 2e-10 Sirohydrochlorin cobaltochelatase OS Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) GN cbiX PE 3 SV 1
blastp_uniprot_sprot sp|Q8TY77|CBIX_METKA 75 194 + 120 Gaps:20 97.90 143 26.43 9e-10 Sirohydrochlorin cobaltochelatase OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) GN cbiX PE 3 SV 1
blastp_uniprot_sprot sp|O27448|CBIX_METTH 75 192 + 118 Gaps:16 92.31 143 27.27 3e-09 Sirohydrochlorin cobaltochelatase OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) GN cbiX PE 1 SV 2
rpsblast_cdd gnl|CDD|178357 69 214 + 146 none 94.81 154 78.77 2e-80 PLN02757 PLN02757 sirohydrochlorine ferrochelatase.
rpsblast_cdd gnl|CDD|110864 81 184 + 104 none 98.11 106 43.27 4e-30 pfam01903 CbiX CbiX. The function of CbiX is uncertain however it is found in cobalamin biosynthesis operons and so may have a related function. Some CbiX proteins contain a striking histidine-rich region at their C-terminus which suggests that it might be involved in metal chelation.
rpsblast_cdd gnl|CDD|48643 75 175 + 101 none 100.00 101 38.61 5e-27 cd03416 CbiX_SirB_N Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB) N-terminal domain. SirB catalyzes the ferro-chelation of sirohydrochlorin to siroheme the prosthetic group of sulfite and nitrite reductases. CbiX is a cobaltochelatase responsible for the chelation of Co2+ into sirohydrochlorin an important step in the vitamin B12 biosynthetic pathway. CbiX often contains a C-terminal histidine-rich region that may be important for metal delivery and/or storage and may also contain an iron-sulfur center. Both are found in a wide range of bacteria. This subgroup also contains single domain proteins from archaea and bacteria which may represent the ancestral form of class II chelatases before domain duplication occurred..
rpsblast_cdd gnl|CDD|32321 72 210 + 139 Gaps:9 95.10 245 31.33 5e-22 COG2138 COG2138 Uncharacterized conserved protein [Function unknown].
rpsblast_cdd gnl|CDD|48641 74 192 + 119 Gaps:2 100.00 117 27.35 2e-18 cd03414 CbiX_SirB_C Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB) C-terminal domain. SirB catalyzes the ferro-chelation of sirohydrochlorin to siroheme the prosthetic group of sulfite and nitrite reductases. CbiX is a cobaltochelatase responsible for the chelation of Co2+ into sirohydrochlorin an important step in the vitamin B12 biosynthetic pathway. CbiX often contains a C-terminal histidine-rich region that may be important for metal delivery and/or storage and may also contain an iron-sulfur center. Both CbiX and SirB are found in a wide range of bacteria..
rpsblast_cdd gnl|CDD|179168 75 189 + 115 Gaps:7 96.83 126 33.61 3e-18 PRK00923 PRK00923 sirohydrochlorin cobaltochelatase Reviewed.
rpsblast_cdd gnl|CDD|180254 76 193 + 118 Gaps:9 37.31 335 29.60 5e-10 PRK05782 PRK05782 bifunctional sirohydrochlorin cobalt chelatase/precorrin-8X methylmutase Validated.
rpsblast_cdd gnl|CDD|48642 76 152 + 77 Gaps:1 60.80 125 35.53 6e-08 cd03415 CbiX_CbiC Archaeal sirohydrochlorin cobalt chelatase (CbiX) single domain. Proteins in this subgroup contain a single CbiX domain N-terminal to a precorrin-8X methylmutase (CbiC) domain. CbiX is a cobaltochelatase responsible for the chelation of Co2+ into sirohydrochlorin while CbiC catalyzes the conversion of cobalt-precorrin 8 to cobyrinic acid by methyl rearrangement. Both CbiX and CbiC are involved in vitamin B12 biosynthesis..

3 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
SUPERFAMILY 74 191 118 SSF53800 none none none
Gene3D 74 194 121 G3DSA:3.40.50.1400 none none none
Pfam 81 185 105 PF01903 "KEGG:00860+4.99.1.3","MetaCyc:PWY-7377","UniPathway:UPA00148" CbiX IPR002762

0 Localization

0 Qtllist

0 Targeting