PDUO_MYCTU
ID PDUO_MYCTU Reviewed; 193 AA.
AC P9WP99; L0T6A0; P64803; Q10622;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Corrinoid adenosyltransferase;
DE EC=2.5.1.17;
DE AltName: Full=Cob(II)alamin adenosyltransferase;
DE AltName: Full=Cob(II)yrinic acid a,c-diamide adenosyltransferase;
DE AltName: Full=Cobinamide/cobalamin adenosyltransferase;
GN OrderedLocusNames=Rv1314c; ORFNames=MTCY373.34c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RG Mycobacterium tuberculosis structural genomics consortium (TB);
RT "Crystal structure of a putative pduO-type ATP:cobalamin
RT adenosyltransferase from Mycobacterium tuberculosis.";
RL Submitted (MAR-2006) to the PDB data bank.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + 2 cob(II)yrinate a,c diamide + reduced [electron-
CC transfer flavoprotein] = 2 adenosylcob(III)yrinate a,c-diamide + 3
CC H(+) + oxidized [electron-transfer flavoprotein] + 2 triphosphate;
CC Xref=Rhea:RHEA:11528, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18036, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:58503,
CC ChEBI:CHEBI:58537; EC=2.5.1.17;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + 2 cob(II)alamin + reduced [electron-transfer
CC flavoprotein] = 2 adenosylcob(III)alamin + 3 H(+) + oxidized
CC [electron-transfer flavoprotein] + 2 triphosphate;
CC Xref=Rhea:RHEA:28671, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16304, ChEBI:CHEBI:18036,
CC ChEBI:CHEBI:18408, ChEBI:CHEBI:30616, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307; EC=2.5.1.17;
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Cob(I)alamin adenosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44071.1; -; Genomic_DNA.
DR PIR; F70775; F70775.
DR RefSeq; NP_215830.1; NC_000962.3.
DR RefSeq; WP_003406839.1; NZ_NVQJ01000059.1.
DR PDB; 2G2D; X-ray; 2.00 A; A=1-193.
DR PDB; 6WGS; X-ray; 1.50 A; A=1-193.
DR PDB; 6WGU; X-ray; 1.65 A; A=1-193.
DR PDB; 6WGV; X-ray; 2.15 A; A=1-193.
DR PDB; 6WH5; X-ray; 1.87 A; A/B/C=1-193.
DR PDBsum; 2G2D; -.
DR PDBsum; 6WGS; -.
DR PDBsum; 6WGU; -.
DR PDBsum; 6WGV; -.
DR PDBsum; 6WH5; -.
DR AlphaFoldDB; P9WP99; -.
DR SMR; P9WP99; -.
DR STRING; 83332.Rv1314c; -.
DR PaxDb; P9WP99; -.
DR DNASU; 886925; -.
DR GeneID; 45425287; -.
DR GeneID; 886925; -.
DR KEGG; mtu:Rv1314c; -.
DR TubercuList; Rv1314c; -.
DR eggNOG; COG2096; Bacteria.
DR OMA; HQACTVV; -.
DR PhylomeDB; P9WP99; -.
DR UniPathway; UPA00148; UER00233.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008817; F:cob(I)yrinic acid a,c-diamide adenosyltransferase activity; IBA:GO_Central.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1200.10; -; 1.
DR InterPro; IPR016030; CblAdoTrfase-like.
DR InterPro; IPR036451; CblAdoTrfase-like_sf.
DR InterPro; IPR029499; PduO-typ.
DR PANTHER; PTHR12213; PTHR12213; 1.
DR Pfam; PF01923; Cob_adeno_trans; 1.
DR SUPFAM; SSF89028; SSF89028; 1.
DR TIGRFAMs; TIGR00636; PduO_Nterm; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cobalamin biosynthesis; Cytoplasm;
KW Nucleotide-binding; Porphyrin biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..193
FT /note="Corrinoid adenosyltransferase"
FT /id="PRO_0000103798"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 137..142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:6WH5"
FT TURN 12..15
FT /evidence="ECO:0007829|PDB:6WH5"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:6WGS"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:6WGS"
FT HELIX 31..53
FT /evidence="ECO:0007829|PDB:6WGS"
FT HELIX 57..77
FT /evidence="ECO:0007829|PDB:6WGS"
FT HELIX 94..108
FT /evidence="ECO:0007829|PDB:6WGS"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:6WH5"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:6WGU"
FT HELIX 124..149
FT /evidence="ECO:0007829|PDB:6WGS"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:6WGS"
FT HELIX 157..176
FT /evidence="ECO:0007829|PDB:6WGS"
SQ SEQUENCE 193 AA; 20694 MW; 2FB302A9F5A5208B CRC64;
MAVHLTRIYT RTGDDGTTGL SDMSRVAKTD ARLVAYADCD EANAAIGAAL ALGHPDTQIT
DVLRQIQNDL FDAGADLSTP IVENPKHPPL RIAQSYIDRL EGWCDAYNAG LPALKSFVLP
GGSPLSALLH VARTVVRRAE RSAWAAVDAH PEGVSVLPAK YLNRLSDLLF ILSRVANPDG
DVLWRPGGDR TAS
