COBH_PSEAE
ID COBH_PSEAE Reviewed; 208 AA.
AC Q9HZU2;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Precorrin-8X methylmutase;
DE EC=5.4.99.61;
DE AltName: Full=HBA synthase;
DE AltName: Full=Precorrin isomerase;
GN Name=cobH; OrderedLocusNames=PA2905;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Catalyzes the conversion of precorrin-8X to
CC hydrogenobyrinate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 H(+) + precorrin-8X = hydrogenobyrinate;
CC Xref=Rhea:RHEA:22512, ChEBI:CHEBI:15378, ChEBI:CHEBI:58581,
CC ChEBI:CHEBI:77873; EC=5.4.99.61;
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 8/10.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CobH/CbiC family. {ECO:0000305}.
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DR EMBL; AE004091; AAG06293.1; -; Genomic_DNA.
DR PIR; H83283; H83283.
DR RefSeq; NP_251595.1; NC_002516.2.
DR RefSeq; WP_003107929.1; NZ_QZGE01000009.1.
DR AlphaFoldDB; Q9HZU2; -.
DR SMR; Q9HZU2; -.
DR STRING; 287.DR97_5036; -.
DR PaxDb; Q9HZU2; -.
DR PRIDE; Q9HZU2; -.
DR DNASU; 882689; -.
DR EnsemblBacteria; AAG06293; AAG06293; PA2905.
DR GeneID; 882689; -.
DR KEGG; pae:PA2905; -.
DR PATRIC; fig|208964.12.peg.3046; -.
DR PseudoCAP; PA2905; -.
DR HOGENOM; CLU_084703_0_0_6; -.
DR InParanoid; Q9HZU2; -.
DR OMA; GAPIFCD; -.
DR PhylomeDB; Q9HZU2; -.
DR BioCyc; PAER208964:G1FZ6-2955-MON; -.
DR UniPathway; UPA00148; UER00219.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016993; F:precorrin-8X methylmutase activity; IEA:UniProtKB-EC.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.10230; -; 1.
DR InterPro; IPR003722; Cbl_synth_CobH/CbiC.
DR InterPro; IPR036588; CobH/CbiC_sf.
DR Pfam; PF02570; CbiC; 1.
DR SUPFAM; SSF63965; SSF63965; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Isomerase; Reference proteome.
FT CHAIN 1..208
FT /note="Precorrin-8X methylmutase"
FT /id="PRO_0000287754"
FT ACT_SITE 41
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 208 AA; 21650 MW; 24422D432CB83A66 CRC64;
MIDYIRDGQA IYRQSFATIR AEANLAGIPA DLEKLAVRVI HACGMVDVVD DLRFSPGAGA
AGRAALAAGA AILCDARMVA EGVTRSRLPA ANRVICTLNE ADVPALATEL GNTRSAVALE
HWREHLEGSV VVIGNAPTAL FYLLEMLDAG APKPALILGF PVGFVGAAES KEMLAADSRG
VPYVIVRGRR GGSAMAAAAV NALATERE
