ID MOAB_ECOLI Reviewed; 170 AA.
AC P0AEZ9; P30746;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=Molybdenum cofactor biosynthesis protein B;
GN Name=moaB; Synonyms=chlA2; OrderedLocusNames=b0782, JW0765;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8361352; DOI=10.1111/j.1365-2958.1993.tb01652.x;
RA Rivers S.L., McNairn E., Blasco F., Giordano G., Boxer D.H.;
RT "Molecular genetic analysis of the moa operon of Escherichia coli K-12
RT required for molybdenum cofactor biosynthesis.";
RL Mol. Microbiol. 8:1071-1081(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP BINDING OF MPT, AND LACK OF FUNCTION AS MPT ADENYLYLTRANSFERASE.
RX PubMed=18154309; DOI=10.1021/bi7020487;
RA Bevers L.E., Hagedoorn P.L., Santamaria-Araujo J.A., Magalon A.,
RA Hagen W.R., Schwarz G.;
RT "Function of MoaB proteins in the biosynthesis of the molybdenum and
RT tungsten cofactors.";
RL Biochemistry 47:949-956(2008).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=15159566; DOI=10.1107/s0907444904007164;
RA Bader G., Gomez-Ortiz M., Haussmann C., Bacher A., Huber R., Fischer M.;
RT "Structure of the molybdenum-cofactor biosynthesis protein MoaB of
RT Escherichia coli.";
RL Acta Crystallogr. D 60:1068-1075(2004).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), GTP BINDING, AND SUBUNIT.
RX PubMed=15269205; DOI=10.1074/jbc.m407694200;
RA Sanishvili R., Beasley S., Skarina T., Glesne D., Joachimiak A.,
RA Edwards A., Savchenko A.;
RT "The crystal structure of Escherichia coli MoaB suggests a probable role in
RT molybdenum cofactor synthesis.";
RL J. Biol. Chem. 279:42139-42146(2004).
CC -!- FUNCTION: May be involved in the biosynthesis of molybdopterin. Can
CC bind GTP and has low GTPase activity. Can bind MPT, but has no MPT
CC adenylyl transferase activity.
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC -!- SUBUNIT: Homohexamer. Dimer of trimers. {ECO:0000269|PubMed:15269205}.
CC -!- INDUCTION: By anaerobiosis, repressed by the molybdenum cofactor.
CC -!- SIMILARITY: Belongs to the MoaB/Mog family. {ECO:0000305}.
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DR EMBL; X70420; CAA49862.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73869.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35440.1; -; Genomic_DNA.
DR PIR; S34999; S31880.
DR RefSeq; NP_415303.1; NC_000913.3.
DR RefSeq; WP_000084639.1; NZ_SSZK01000002.1.
DR PDB; 1MKZ; X-ray; 1.60 A; A/B=1-170.
DR PDB; 1R2K; X-ray; 2.10 A; A/B=2-170.
DR PDBsum; 1MKZ; -.
DR PDBsum; 1R2K; -.
DR AlphaFoldDB; P0AEZ9; -.
DR SMR; P0AEZ9; -.
DR BioGRID; 4259950; 23.
DR IntAct; P0AEZ9; 4.
DR STRING; 511145.b0782; -.
DR SWISS-2DPAGE; P0AEZ9; -.
DR jPOST; P0AEZ9; -.
DR PaxDb; 511145-b0782; -.
DR EnsemblBacteria; AAC73869; AAC73869; b0782.
DR GeneID; 75204897; -.
DR GeneID; 945396; -.
DR KEGG; ecj:JW0765; -.
DR KEGG; eco:b0782; -.
DR PATRIC; fig|1411691.4.peg.1496; -.
DR EchoBASE; EB1553; -.
DR eggNOG; COG0521; Bacteria.
DR HOGENOM; CLU_077358_2_2_6; -.
DR InParanoid; P0AEZ9; -.
DR OMA; TGWDGIL; -.
DR OrthoDB; 9784492at2; -.
DR PhylomeDB; P0AEZ9; -.
DR BioCyc; EcoCyc:MONOMER0-1501; -.
DR UniPathway; UPA00344; -.
DR EvolutionaryTrace; P0AEZ9; -.
DR PRO; PR:P0AEZ9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0034214; P:protein hexamerization; IDA:EcoCyc.
DR CDD; cd00886; MogA_MoaB; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR InterPro; IPR012245; MoaB.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR013484; MoaB_proteobac.
DR InterPro; IPR008284; MoCF_biosynth_CS.
DR NCBIfam; TIGR02667; moaB_proteo; 1.
DR NCBIfam; TIGR00177; molyb_syn; 1.
DR PANTHER; PTHR43232; MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN B; 1.
DR PANTHER; PTHR43232:SF2; MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN B; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR PIRSF; PIRSF006443; MoaB; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
DR PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; GTP-binding;
KW Molybdenum cofactor biosynthesis; Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8361352"
FT CHAIN 2..170
FT /note="Molybdenum cofactor biosynthesis protein B"
FT /id="PRO_0000170970"
FT BINDING 110
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:1MKZ"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:1MKZ"
FT HELIX 28..39
FT /evidence="ECO:0007829|PDB:1MKZ"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:1MKZ"
FT HELIX 54..66
FT /evidence="ECO:0007829|PDB:1MKZ"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1MKZ"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:1MKZ"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1MKZ"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:1MKZ"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:1MKZ"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1MKZ"
FT HELIX 100..114
FT /evidence="ECO:0007829|PDB:1MKZ"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:1MKZ"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:1MKZ"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:1MKZ"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:1MKZ"
FT HELIX 151..155
FT /evidence="ECO:0007829|PDB:1MKZ"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:1MKZ"
SQ SEQUENCE 170 AA; 18665 MW; C9AA21A7E12E53B0 CRC64;
MSQVSTEFIP TRIAILTVSN RRGEEDDTSG HYLRDSAQEA GHHVVDKAIV KENRYAIRAQ
VSAWIASDDV QVVLITGGTG LTEGDQAPEA LLPLFDREVE GFGEVFRMLS FEEIGTSTLQ
SRAVAGVANK TLIFAMPGST KACRTAWENI IAPQLDARTR PCNFHPHLKK
//
