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MMOB_METTR
ID   MMOB_METTR              Reviewed;         138 AA.
AC   P27356;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Methane monooxygenase regulatory protein B;
GN   Name=mmoB;
OS   Methylosinus trichosporium.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylocystaceae; Methylosinus.
OX   NCBI_TaxID=426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35070 / NCIMB 11131 / ACM 3311 / OB3b;
RX   PubMed=1904125; DOI=10.1111/j.1365-2958.1991.tb02114.x;
RA   Cardy D.L.N., Laidler V., Salmond G.P.C., Murrell J.C.;
RT   "Molecular analysis of the methane monooxygenase (MMO) gene cluster of
RT   Methylosinus trichosporium OB3b.";
RL   Mol. Microbiol. 5:335-342(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-17.
RX   PubMed=1845980; DOI=10.1016/s0021-9258(18)52470-4;
RA   Fox B.G., Liu Y., Dege J.E., Lipscomb J.D.;
RT   "Complex formation between the protein components of methane monooxygenase
RT   from Methylosinus trichosporium OB3b. Identification of sites of component
RT   interaction.";
RL   J. Biol. Chem. 266:540-550(1991).
RN   [3]
RP   STRUCTURE BY NMR.
RX   PubMed=10231531; DOI=10.1021/bi982992f;
RA   Chang S.-L., Wallar B.J., Lipscomb J.D., Mayo K.H.;
RT   "Solution structure of component B from methane monooxygenase derived
RT   through heteronuclear NMR and molecular modeling.";
RL   Biochemistry 38:5799-5812(1999).
CC   -!- FUNCTION: The B protein acts as a regulator of electron flow through
CC       the soluble mmo complex, switching the enzyme from an oxidase to a
CC       hydroxylase in the presence of the substrate.
CC   -!- SUBUNIT: The soluble methane monooxygenase (sMMO) consists of four
CC       components A/MMOH (composed of alpha/MmoX, beta/MmoY and gamma/MmoZ),
CC       B/MMOB (MmoB), C/MMOR (MmoC) and D/MMOD (MmoD).
CC   -!- SIMILARITY: Belongs to the TmoD/XamoD family. {ECO:0000305}.
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DR   EMBL; X55394; CAA39070.1; -; Genomic_DNA.
DR   PIR; S15209; D39049.
DR   PDB; 2MOB; NMR; -; A=1-138.
DR   PDB; 6VK4; X-ray; 2.35 A; D/H=1-138.
DR   PDB; 6VK5; X-ray; 1.86 A; D/H=1-138.
DR   PDB; 6VK8; X-ray; 2.03 A; D/H=1-138.
DR   PDB; 6YD0; X-ray; 1.95 A; G=1-138.
DR   PDB; 6YDI; X-ray; 1.95 A; G=1-138.
DR   PDB; 6YDU; X-ray; 1.95 A; G=1-138.
DR   PDB; 6YY3; X-ray; 2.00 A; G=1-138.
DR   PDBsum; 2MOB; -.
DR   PDBsum; 6VK4; -.
DR   PDBsum; 6VK5; -.
DR   PDBsum; 6VK8; -.
DR   PDBsum; 6YD0; -.
DR   PDBsum; 6YDI; -.
DR   PDBsum; 6YDU; -.
DR   PDBsum; 6YY3; -.
DR   AlphaFoldDB; P27356; -.
DR   BMRB; P27356; -.
DR   SMR; P27356; -.
DR   BioCyc; MetaCyc:MON-3871; -.
DR   BRENDA; 1.14.13.25; 3322.
DR   SABIO-RK; P27356; -.
DR   EvolutionaryTrace; P27356; -.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR   DisProt; DP00992; -.
DR   Gene3D; 3.90.56.10; -; 1.
DR   InterPro; IPR003454; MOase_MmoB_DmpM.
DR   InterPro; IPR036889; mOase_MmoB_DmpM_sf.
DR   Pfam; PF02406; MmoB_DmpM; 1.
DR   SUPFAM; SSF56029; SSF56029; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Monooxygenase; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1845980"
FT   CHAIN           2..138
FT                   /note="Methane monooxygenase regulatory protein B"
FT                   /id="PRO_0000096508"
FT   HELIX           4..6
FT                   /evidence="ECO:0007829|PDB:6VK5"
FT   HELIX           11..14
FT                   /evidence="ECO:0007829|PDB:6VK5"
FT   HELIX           17..24
FT                   /evidence="ECO:0007829|PDB:6VK5"
FT   HELIX           27..29
FT                   /evidence="ECO:0007829|PDB:6VK5"
FT   STRAND          37..43
FT                   /evidence="ECO:0007829|PDB:6VK5"
FT   HELIX           46..54
FT                   /evidence="ECO:0007829|PDB:6VK5"
FT   TURN            55..58
FT                   /evidence="ECO:0007829|PDB:6VK5"
FT   HELIX           59..63
FT                   /evidence="ECO:0007829|PDB:6VK5"
FT   STRAND          68..71
FT                   /evidence="ECO:0007829|PDB:6VK5"
FT   STRAND          73..87
FT                   /evidence="ECO:0007829|PDB:6VK5"
FT   HELIX           88..95
FT                   /evidence="ECO:0007829|PDB:6VK5"
FT   HELIX           101..104
FT                   /evidence="ECO:0007829|PDB:6VK5"
FT   HELIX           105..107
FT                   /evidence="ECO:0007829|PDB:6VK5"
FT   STRAND          108..118
FT                   /evidence="ECO:0007829|PDB:6VK5"
FT   STRAND          121..126
FT                   /evidence="ECO:0007829|PDB:6VK5"
FT   TURN            129..131
FT                   /evidence="ECO:0007829|PDB:6VK5"
SQ   SEQUENCE   138 AA;  14883 MW;  B8FB8731DF525E82 CRC64;
     MSSAHNAYNA GIMQKTGKAF ADEFFAEENQ VVHESNAVVL VLMKSDEIDA IIEDIVLKGG
     KAKNPSIVVE DKAGFWWIKA DGAIEIDAAE AGELLGKPFS VYDLLINVSS TVGRAYTLGT
     KFTITSELMG LDRALTDI
 
 
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