FUMI_SPHMC
ID FUMI_SPHMC Reviewed; 422 AA.
AC D2D3B2;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Aminopentol aminotransferase;
DE EC=2.6.1.-;
GN Name=fumI;
OS Sphingopyxis macrogoltabida (Sphingomonas macrogoltabidus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=33050;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MTA144;
RX PubMed=19922747; DOI=10.1016/j.jbiotec.2009.11.004;
RA Heinl S., Hartinger D., Thamhesl M., Vekiru E., Krska R., Schatzmayr G.,
RA Moll W.-D., Grabherr R.;
RT "Degradation of fumonisin B1 by the consecutive action of two bacterial
RT enzymes.";
RL J. Biotechnol. 145:120-129(2010).
RN [2]
RP PURIFICATION, AND SUBCELLULAR LOCATION.
RC STRAIN=MTA144;
RX PubMed=20718948; DOI=10.1186/1475-2859-9-62;
RA Hartinger D., Heinl S., Schwartz H.E., Grabherr R., Schatzmayr G.,
RA Haltrich D., Moll W.D.;
RT "Enhancement of solubility in Escherichia coli and purification of an
RT aminotransferase from Sphingopyxis sp. MTA144 for deamination of hydrolyzed
RT fumonisin B(1).";
RL Microb. Cell Fact. 9:62-62(2010).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=MTA144;
RX PubMed=21503761; DOI=10.1007/s00253-011-3248-9;
RA Hartinger D., Schwartz H., Hametner C., Schatzmayr G., Haltrich D.,
RA Moll W.D.;
RT "Enzyme characteristics of aminotransferase FumI of Sphingopyxis sp. MTA144
RT for deamination of hydrolyzed fumonisin B(1).";
RL Appl. Microbiol. Biotechnol. 91:757-768(2011).
CC -!- FUNCTION: Involved in degradation of fumonisin B1. Catalyzes the
CC deamination of aminopentol (HFB1) to 2-keto-HFB1. Pyruvate is the
CC preferred cosubstrate, but it can also use several other alpha-keto
CC acids as amino group acceptors. {ECO:0000269|PubMed:21503761}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3S,5R,10R,12S,14S,15R,16R)-2-amino-12,16-dimethylicosane-
CC 3,5,10,14,15-pentol + pyruvate = (3S,5R,10R,12S,14S,15R,16R)-
CC 3,5,10,14,15-pentahydroxy-12,16-dimethylicosan-2-one + L-alanine;
CC Xref=Rhea:RHEA:51068, ChEBI:CHEBI:15361, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:62526, ChEBI:CHEBI:133941;
CC Evidence={ECO:0000269|PubMed:21503761};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:21503761};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.1 uM for HFB1 {ECO:0000269|PubMed:21503761};
CC KM=490 uM for pyruvate {ECO:0000269|PubMed:21503761};
CC Note=kcat is 104 min(-1).;
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:21503761};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:21503761};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20718948}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; FJ426269; ACS27061.1; -; Genomic_DNA.
DR PDB; 6HBS; X-ray; 1.65 A; A/B=1-422.
DR PDB; 6HBV; X-ray; 1.65 A; A/B=1-422.
DR PDBsum; 6HBS; -.
DR PDBsum; 6HBV; -.
DR AlphaFoldDB; D2D3B2; -.
DR SMR; D2D3B2; -.
DR BioCyc; MetaCyc:MON-16401; -.
DR BRENDA; 2.6.1.B3; 8963.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Pyridoxal phosphate; Transferase.
FT CHAIN 1..422
FT /note="Aminopentol aminotransferase"
FT /id="PRO_0000418897"
FT MOD_RES 258
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT HELIX 5..17
FT /evidence="ECO:0007829|PDB:6HBS"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:6HBS"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:6HBS"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:6HBS"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:6HBS"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:6HBS"
FT HELIX 72..82
FT /evidence="ECO:0007829|PDB:6HBS"
FT HELIX 94..105
FT /evidence="ECO:0007829|PDB:6HBS"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:6HBS"
FT HELIX 118..133
FT /evidence="ECO:0007829|PDB:6HBS"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:6HBS"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:6HBS"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:6HBS"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:6HBS"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:6HBS"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:6HBS"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:6HBS"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:6HBS"
FT HELIX 210..223
FT /evidence="ECO:0007829|PDB:6HBS"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:6HBS"
FT TURN 232..237
FT /evidence="ECO:0007829|PDB:6HBS"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:6HBS"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:6HBS"
FT TURN 258..263
FT /evidence="ECO:0007829|PDB:6HBS"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:6HBS"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:6HBS"
FT HELIX 276..281
FT /evidence="ECO:0007829|PDB:6HBS"
FT TURN 287..290
FT /evidence="ECO:0007829|PDB:6HBS"
FT HELIX 292..307
FT /evidence="ECO:0007829|PDB:6HBS"
FT HELIX 310..332
FT /evidence="ECO:0007829|PDB:6HBS"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:6HBS"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:6HBS"
FT HELIX 356..367
FT /evidence="ECO:0007829|PDB:6HBS"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:6HBS"
FT HELIX 386..405
FT /evidence="ECO:0007829|PDB:6HBS"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:6HBS"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:6HBV"
SQ SEQUENCE 422 AA; 46292 MW; 11868245D726DB57 CRC64;
MANGTRQKDL RERAERVIPG GMYGHESTRL LPPEFPQFFR RALGARIWDA DEQPYIDYMC
AYGPNLLGYR QSEIEAAADA QRLLGDTMTG PSEIMVNLAE AFVGMVRHAD WAMFCKNGSD
ATSTAMVLAR AHTGRKTILC AKGAYHGASP WNTPHTAGIL ASDRVHVAYY TYNDAQSLSD
AFKAHDGDIA AVFATPFRHE VFEDQALAQL EFARTARKCC DETGALLVVD DVRAGFRVAR
DCSWTHLGIE PDLSCWGKCF ANGYPISALL GSNKARDAAR DIFVTGSFWF SAVPMAAAIE
TLRIIRETPY LETLIASGAA LRAGLEAQSQ RHGLELKQTG PAQMPQIFFA DDPDFRIGYA
WAAACLKGGV YVHPYHNMFL SAAHTVDDVT ETLEATDRAF SAVLRDFASL QPHPILMQLA
GA
