MOAB_BACCR
ID MOAB_BACCR Reviewed; 169 AA.
AC Q816R0;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Molybdenum cofactor biosynthesis protein B;
GN Name=moaB; OrderedLocusNames=BC_4758;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), AND SUBUNIT.
RG Midwest center for structural genomics (MCSG);
RT "Crystal structure of molybdenum cofactor biosynthesis protein B.";
RL Submitted (MAY-2006) to the PDB data bank.
CC -!- FUNCTION: May be involved in the biosynthesis of molybdopterin.
CC {ECO:0000250}.
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the MoaB/Mog family. {ECO:0000305}.
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DR EMBL; AE016877; AAP11663.1; -; Genomic_DNA.
DR RefSeq; NP_834462.1; NC_004722.1.
DR RefSeq; WP_000117124.1; NZ_CP034551.1.
DR PDB; 1Y5E; X-ray; 1.90 A; A/B/C=1-169.
DR PDBsum; 1Y5E; -.
DR AlphaFoldDB; Q816R0; -.
DR SMR; Q816R0; -.
DR STRING; 226900.BC_4758; -.
DR DrugBank; DB03366; Imidazole.
DR EnsemblBacteria; AAP11663; AAP11663; BC_4758.
DR GeneID; 67509399; -.
DR KEGG; bce:BC4758; -.
DR PATRIC; fig|226900.8.peg.4921; -.
DR HOGENOM; CLU_077358_2_3_9; -.
DR OMA; TGWDGIL; -.
DR UniPathway; UPA00344; -.
DR EvolutionaryTrace; Q816R0; -.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00886; MogA_MoaB; 1.
DR Gene3D; 3.40.980.10; -; 1.
DR InterPro; IPR012245; MoaB.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR008284; MoCF_biosynth_CS.
DR PANTHER; PTHR43232; PTHR43232; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR PIRSF; PIRSF006443; MoaB; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF53218; SSF53218; 1.
DR TIGRFAMs; TIGR00177; molyb_syn; 1.
DR PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Molybdenum cofactor biosynthesis; Reference proteome.
FT CHAIN 1..169
FT /note="Molybdenum cofactor biosynthesis protein B"
FT /id="PRO_0000170967"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:1Y5E"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1Y5E"
FT HELIX 31..43
FT /evidence="ECO:0007829|PDB:1Y5E"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:1Y5E"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:1Y5E"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:1Y5E"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1Y5E"
FT HELIX 90..95
FT /evidence="ECO:0007829|PDB:1Y5E"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1Y5E"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:1Y5E"
FT HELIX 119..124
FT /evidence="ECO:0007829|PDB:1Y5E"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:1Y5E"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:1Y5E"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:1Y5E"
FT HELIX 155..166
FT /evidence="ECO:0007829|PDB:1Y5E"
SQ SEQUENCE 169 AA; 18535 MW; 8B43F09FBA52E51B CRC64;
MSVTEHKKQA PKEVRCKIVT ISDTRTEETD KSGQLLHELL KEAGHKVTSY EIVKDDKESI
QQAVLAGYHK EDVDVVLTNG GTGITKRDVT IEAVSALLDK EIVGFGELFR MISYLEDIGS
SAMLSRAIGG TIGRKVVFSM PGSSGAVRLA MNKLILPELG HITFELHRQ