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CBID_SALPB
ID   CBID_SALPB              Reviewed;         379 AA.
AC   A9MT88;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Cobalt-precorrin-5B C(1)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00787};
DE            EC=2.1.1.195 {ECO:0000255|HAMAP-Rule:MF_00787};
DE   AltName: Full=Cobalt-precorrin-6A synthase {ECO:0000255|HAMAP-Rule:MF_00787};
GN   Name=cbiD {ECO:0000255|HAMAP-Rule:MF_00787}; OrderedLocusNames=SPAB_01073;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to
CC       form cobalt-precorrin-6A. {ECO:0000255|HAMAP-Rule:MF_00787}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A +
CC         S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:26285, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:60063, ChEBI:CHEBI:60064;
CC         EC=2.1.1.195; Evidence={ECO:0000255|HAMAP-Rule:MF_00787};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC       step 6/10. {ECO:0000255|HAMAP-Rule:MF_00787}.
CC   -!- SIMILARITY: Belongs to the CbiD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00787}.
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DR   EMBL; CP000886; ABX66494.1; -; Genomic_DNA.
DR   RefSeq; WP_001292918.1; NC_010102.1.
DR   AlphaFoldDB; A9MT88; -.
DR   SMR; A9MT88; -.
DR   KEGG; spq:SPAB_01073; -.
DR   PATRIC; fig|1016998.12.peg.1014; -.
DR   HOGENOM; CLU_041273_1_0_6; -.
DR   OMA; YHGKLIK; -.
DR   BioCyc; SENT1016998:SPAB_RS04485-MON; -.
DR   UniPathway; UPA00148; UER00227.
DR   Proteomes; UP000008556; Chromosome.
DR   GO; GO:0043780; F:cobalt-precorrin-5B C1-methyltransferase activity; IEA:RHEA.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046140; P:corrin biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.2110.10; -; 1.
DR   HAMAP; MF_00787; CbiD; 1.
DR   InterPro; IPR002748; CbiD.
DR   InterPro; IPR036074; CbiD_sf.
DR   PANTHER; PTHR35863; PTHR35863; 1.
DR   Pfam; PF01888; CbiD; 1.
DR   PIRSF; PIRSF026782; CbiD; 1.
DR   SUPFAM; SSF111342; SSF111342; 1.
DR   TIGRFAMs; TIGR00312; cbiD; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..379
FT                   /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT                   /id="PRO_1000083596"
SQ   SEQUENCE   379 AA;  40805 MW;  D194BC5D7E92B87D CRC64;
     MSELSFDAPV WRHGKALRKG YTTGSCATAA AKVAALMVLR QHLIHQVSIV TPSGVTLCLN
     VESPHIEGQQ AIAAIRKDGG DDVDATHGML IFARVTLNDS GEITLTGGEG IGTVTRKGVG
     LPLGSAAINR TPRHTIESAV REAIGPARGA DVEIFAPEGE ARAQKTYNSR LGILGGISII
     GTTGIVTPMS EESWKRSLSL ELEIKRASGL TRVILVPGNH GERFVREQMG VDTQAVVTMS
     NFVGYMIEEA VRLGFCQIVL VGHPGKLIKI AAGIFHTHSH IADARMETLV AHLALLGAPL
     ELLTLVSDCD TTEAAMEHIE AYGFGHIYNH LARRICLRVM QMLRFTKTPP VCDAILFSFD
     NHILGSNRPV DEIAKELQC
 
 
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