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