CBIHC_ARCFU
ID CBIHC_ARCFU Reviewed; 446 AA.
AC O29534;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Cobalamin biosynthesis protein CbiHC;
DE Includes:
DE RecName: Full=Probable cobalt-factor III C(17)-methyltransferase;
DE EC=2.1.1.-;
DE AltName: Full=Cobalt-precorrin-3 methyltransferase;
DE Short=Cobalt-precorrin-3 methylase;
DE Includes:
DE RecName: Full=Cobalt-precorrin-8 methylmutase;
DE EC=5.4.99.60;
DE AltName: Full=Cobalt-precorrin isomerase;
GN Name=cbiHC; Synonyms=cobJH; OrderedLocusNames=AF_0724;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
CC -!- FUNCTION: Bifunctional enzyme with a methyltransferase domain that
CC catalyzes the ring contraction and methylation of C-17 in cobalt-factor
CC III to form cobalt-factor IV, and an isomerase domain that catalyzes
CC the conversion of cobalt-precorrin-8 to cobyrinate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Co(II)-factor III + H(+) + S-adenosyl-L-methionine = Co(II)-
CC factor IV + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:45852,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73299, ChEBI:CHEBI:85471;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Co-precorrin-8X = cob(II)yrinate; Xref=Rhea:RHEA:16209,
CC ChEBI:CHEBI:58894, ChEBI:CHEBI:70792; EC=5.4.99.60;
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC step 3/10.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC step 9/10.
CC -!- SIMILARITY: In the N-terminal section; belongs to the precorrin
CC methyltransferase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the CobH family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000782; AAB90518.1; -; Genomic_DNA.
DR PIR; D69340; D69340.
DR AlphaFoldDB; O29534; -.
DR SMR; O29534; -.
DR STRING; 224325.AF_0724; -.
DR PRIDE; O29534; -.
DR EnsemblBacteria; AAB90518; AAB90518; AF_0724.
DR KEGG; afu:AF_0724; -.
DR eggNOG; arCOG00647; Archaea.
DR eggNOG; arCOG02247; Archaea.
DR HOGENOM; CLU_573257_0_0_2; -.
DR OMA; CIDTGMK; -.
DR PhylomeDB; O29534; -.
DR UniPathway; UPA00148; UER00225.
DR UniPathway; UPA00148; UER00230.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0043778; F:cobalt-precorrin-8 methylmutase activity; IEA:UniProtKB-EC.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016993; F:precorrin-8X methylmutase activity; IEA:InterPro.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd11646; Precorrin_3B_C17_MT; 1.
DR Gene3D; 3.30.950.10; -; 1.
DR Gene3D; 3.40.1010.10; -; 1.
DR Gene3D; 3.40.50.10230; -; 1.
DR InterPro; IPR000878; 4pyrrol_Mease.
DR InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR InterPro; IPR014422; Cbl_synth_bifunc_CbiH/CbiC.
DR InterPro; IPR003722; Cbl_synth_CobH/CbiC.
DR InterPro; IPR006363; Cbl_synth_CobJ/CibH_dom.
DR InterPro; IPR036588; CobH/CbiC_sf.
DR Pfam; PF02570; CbiC; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR PIRSF; PIRSF004874; Prcrn_mtase_isom; 1.
DR SUPFAM; SSF53790; SSF53790; 1.
DR SUPFAM; SSF63965; SSF63965; 1.
DR TIGRFAMs; TIGR01466; cobJ_cbiH; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Isomerase; Methyltransferase;
KW Multifunctional enzyme; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..446
FT /note="Cobalamin biosynthesis protein CbiHC"
FT /id="PRO_0000150405"
FT REGION 1..246
FT /note="Cobalt-factor III C(17)-methyltransferase"
FT REGION 247..446
FT /note="Cobalt-precorrin-8 methylmutase"
SQ SEQUENCE 446 AA; 48678 MW; 7341BCBC0998FFDA CRC64;
MLLLPSRGKL YVVGIGPGKE ELMTLKAKRA IEEADYIVGY QTYVDRISHL IEGKKVVTTP
MRKELDRVKI ALELAKEHVV ALISGGDPSI YGILPLVIEY AVEKKVDVEI EAIPGVTAAS
AASSLLGSAI SGDFAVVSLS DLLVPWSVVE KRLLYALSGD FVVAIYNPSS RRRKENFRKA
MEIVRRFRGD AWVGVVRNAG REGQQVEIRR VSEVDEVDMN TILIVGNSET KVVDGKMFTP
RGYSNKYNIG EKRRAERMGA STKGGMEVAR RSEEILRSFY PEEGLRGDII RRCIATTGDV
TIKDVIRFVG DTEEGVRALR DGCRIIADVH MVRAGLRRDA IVAVDFARGD DTRTASGIRN
LAEMIEGSLV AIGNSPSAAF ALCEVAEKHP PRFIVATPVG FVNAAESKEM VRKLPVPSVT
TEGPRGGSGI CAAIVNCLIE HADRPD
