MOSA_AZOVD
ID MOSA_AZOVD Reviewed; 276 AA.
AC P84308; C1DFP5; Q4IT85;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Molybdenum storage protein subunit alpha;
DE AltName: Full=Mo storage protein subunit alpha;
DE Short=MoSto subunit alpha;
GN Name=mosA {ECO:0000303|PubMed:15651045}; OrderedLocusNames=Avin_43200;
OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=322710;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ / ATCC BAA-1303;
RX PubMed=19429624; DOI=10.1128/jb.00504-09;
RA Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G.,
RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA Dean D.R., Dixon R., Wood D.;
RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT to support diverse anaerobic metabolic processes.";
RL J. Bacteriol. 191:4534-4545(2009).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-28, IDENTIFICATION, FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, MOLYBDENUM-BINDING,
RP AND MASS SPECTROMETRY.
RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW;
RX PubMed=15651045; DOI=10.1002/cbic.200400263;
RA Fenske D., Gnida M., Schneider K., Meyer-Klaucke W., Schemberg J.,
RA Henschel V., Meyer A.-K., Knochel A., Muller A.;
RT "A new type of metalloprotein: the Mo storage protein from Azotobacter
RT vinelandii contains a polynuclear molybdenum-oxide cluster.";
RL ChemBioChem 6:405-413(2005).
CC -!- FUNCTION: Intracellular storage of molybdenum. Binds polyoxomolybdates.
CC Can bind at least 90 molybdenum atoms per protein molecule.
CC {ECO:0000269|PubMed:15651045}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5 to 7.0. Above pH 7.1 molybdenum is released.
CC {ECO:0000269|PubMed:15651045};
CC -!- SUBUNIT: Octamer consisting of 4 alpha and 4 beta chains.
CC {ECO:0000269|PubMed:15651045}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15651045}.
CC -!- INDUCTION: Requires molybdenum. {ECO:0000269|PubMed:15651045}.
CC -!- MASS SPECTROMETRY: Mass=29120; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15651045};
CC -!- SIMILARITY: Belongs to the UMP kinase family. Highly divergent.
CC {ECO:0000305}.
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DR EMBL; CP001157; ACO80441.1; -; Genomic_DNA.
DR RefSeq; WP_012702809.1; NC_012560.1.
DR PDB; 2OGX; X-ray; 1.60 A; A=1-276.
DR PDB; 4F6T; X-ray; 1.60 A; A=33-276.
DR PDB; 4NDO; X-ray; 1.35 A; A=1-276.
DR PDB; 4NDP; X-ray; 1.60 A; A=1-276.
DR PDB; 4NDQ; X-ray; 1.75 A; A=1-276.
DR PDB; 4NDR; X-ray; 2.00 A; A=1-276.
DR PDB; 5O5W; X-ray; 1.70 A; A=1-276.
DR PDB; 6GU5; X-ray; 1.90 A; A=2-276.
DR PDB; 6GUJ; X-ray; 2.10 A; A=2-276.
DR PDB; 6GWB; X-ray; 1.90 A; A=2-276.
DR PDB; 6GWV; X-ray; 2.80 A; A/D/F/G/J/L/M/P/R=2-276.
DR PDB; 6GX4; X-ray; 1.90 A; A=2-276.
DR PDB; 6H6W; X-ray; 1.90 A; A=2-276.
DR PDB; 6H73; X-ray; 2.30 A; A=2-276.
DR PDB; 6H74; X-ray; 1.80 A; A=2-276.
DR PDB; 6H8B; X-ray; 1.90 A; A=2-276.
DR PDB; 6H8H; X-ray; 1.90 A; A=2-276.
DR PDB; 6RIS; X-ray; 2.10 A; A=2-276.
DR PDB; 6RJ4; X-ray; 1.90 A; A/C/E=2-276.
DR PDB; 6RKD; EM; 3.20 A; A/C/E/G/I/K=1-276.
DR PDB; 6RKE; X-ray; 1.70 A; A/C/E/G/I/K=2-276.
DR PDB; 6YT3; X-ray; 2.85 A; A=1-276.
DR PDBsum; 2OGX; -.
DR PDBsum; 4F6T; -.
DR PDBsum; 4NDO; -.
DR PDBsum; 4NDP; -.
DR PDBsum; 4NDQ; -.
DR PDBsum; 4NDR; -.
DR PDBsum; 5O5W; -.
DR PDBsum; 6GU5; -.
DR PDBsum; 6GUJ; -.
DR PDBsum; 6GWB; -.
DR PDBsum; 6GWV; -.
DR PDBsum; 6GX4; -.
DR PDBsum; 6H6W; -.
DR PDBsum; 6H73; -.
DR PDBsum; 6H74; -.
DR PDBsum; 6H8B; -.
DR PDBsum; 6H8H; -.
DR PDBsum; 6RIS; -.
DR PDBsum; 6RJ4; -.
DR PDBsum; 6RKD; -.
DR PDBsum; 6RKE; -.
DR PDBsum; 6YT3; -.
DR AlphaFoldDB; P84308; -.
DR SMR; P84308; -.
DR STRING; 322710.Avin_43200; -.
DR EnsemblBacteria; ACO80441; ACO80441; Avin_43200.
DR KEGG; avn:Avin_43200; -.
DR eggNOG; COG0528; Bacteria.
DR HOGENOM; CLU_1008069_0_0_6; -.
DR OMA; YHHHEFP; -.
DR OrthoDB; 1043239at2; -.
DR EvolutionaryTrace; P84308; -.
DR Proteomes; UP000002424; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030151; F:molybdenum ion binding; IDA:UniProtKB.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR CDD; cd04255; AAK_UMPK-MosAB; 1.
DR Gene3D; 3.40.1160.10; -; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR030669; MoSto_subunit_alpha/beta.
DR Pfam; PF00696; AA_kinase; 1.
DR PIRSF; PIRSF039097; MoSto_subunit; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Metal-binding;
KW Molybdenum; Storage protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15651045"
FT CHAIN 2..276
FT /note="Molybdenum storage protein subunit alpha"
FT /id="PRO_0000143931"
FT TURN 14..17
FT /evidence="ECO:0007829|PDB:6RKE"
FT HELIX 23..30
FT /evidence="ECO:0007829|PDB:6RKE"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 55..68
FT /evidence="ECO:0007829|PDB:4NDO"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:4NDO"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 82..93
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 98..120
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 130..143
FT /evidence="ECO:0007829|PDB:4NDO"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:4NDO"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 170..181
FT /evidence="ECO:0007829|PDB:4NDO"
FT STRAND 184..194
FT /evidence="ECO:0007829|PDB:4NDO"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:4NDO"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:6GWV"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:4NDO"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 230..237
FT /evidence="ECO:0007829|PDB:4NDO"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 255..260
FT /evidence="ECO:0007829|PDB:4NDO"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:4NDO"
SQ SEQUENCE 276 AA; 29337 MW; D650915CA97D486B CRC64;
MTDTTNSIKH VISPLARQTL QDRDLTRPVA GKRPIRLLPW LQVVKIGGRV MDRGADAILP
LVEELRKLLP EHRLLILTGA GVRARHVFSV GLDLGLPVGS LAPLAASEAG QNGHILAAML
ASEGVSYVEH PTVADQLAIH LSATRAVVGS AFPPYHHHEF PGSRIPPHRA DTGAFLLADA
FGAAGLTIVE NVDGIYTADP NGPDRGQARF LPETSATDLA KSEGPLPVDR ALLDVMATAR
HIERVQVVNG LVPGRLTAAL RGEHVGTLIR TGVRPA
